[1]	NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANT THR-344. PubMed=2328727 [NCBI, ExPASy, EBI, Israel, Japan] Kastner P., Krust A., Turcotte B., Stropp U., Tora L., Gronemeyer H., Chambon P.; "Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B."; EMBO J. 9:1603-1614(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-660. DOI=10.1016/0006-291X(87)91416-1; PubMed=3551956 [NCBI, ExPASy, EBI, Israel, Japan] Misrahi M., Atger M., D'Auriol L., Loosfelt H., Meriel C., Fridlansky F., Guiochon-Mantel A., Galibert F., Milgrom E.; "Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA."; Biochem. Biophys. Res. Commun. 143:740-748(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-660. Kieback D.G., Agoulnik I.U., Tong X.-W.; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/j.ympev.2007.12.026; PubMed=18375150 [NCBI, ExPASy, EBI, Israel, Japan] Chen C., Opazo J.C., Erez O., Uddin M., Santolaya-Forgas J., Goodman M., Grossman L.I., Romero R., Wildman D.E.; "The human progesterone receptor shows evidence of adaptive evolution associated with its ability to act as a transcription factor."; Mol. Phylogenet. Evol. 47:637-649(2008).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-50; VAL-120; LEU-186; ARG-301; THR-344; SER-444; LEU-529; PRO-536; VAL-651 AND LEU-865. NIEHS SNPs program; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.; Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]	PROTEIN SEQUENCE OF 11-22 AND 673-679, PHOSPHORYLATION AT SER-20; SER-102; SER-130; SER-162; SER-190; SER-213; SER-345 AND SER-676, AND MASS SPECTROMETRY. DOI=10.1074/jbc.M009805200; PubMed=11110801 [NCBI, ExPASy, EBI, Israel, Japan] Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L.; "Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites."; J. Biol. Chem. 276:8475-8483(2001).
[8]	PHOSPHORYLATION AT SER-81 AND SER-162. DOI=10.1210/me.9.8.1029; PubMed=7476977 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Beck C.A., Poletti A., Edwards D.P., Weigel N.L.; "Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor."; Mol. Endocrinol. 9:1029-1040(1995).
[9]	PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345. DOI=10.1074/jbc.271.32.19546; PubMed=8702648 [NCBI, ExPASy, EBI, Israel, Japan] Beck C.A., Zhang Y., Altmann M., Weigel N.L., Edwards D.P.; "Stoichiometry and site-specific phosphorylation of human progesterone receptor in native target cells and in the baculovirus expression system."; J. Biol. Chem. 271:19546-19555(1996).
[10]	PHOSPHORYLATION AT SER-162; SER-190 AND SER-400. DOI=10.1210/me.11.6.823; PubMed=9171245 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Beck C.A., Poletti A., Clement J.P. IV, Prendergast P., Yip T.-T., Hutchens T.W., Edwards D.P., Weigel N.L.; "Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo."; Mol. Endocrinol. 11:823-832(1997).
[11]	PHOSPHORYLATION AT SER-190 AND SER-294. DOI=10.1210/me.14.1.52; PubMed=10628747 [NCBI, ExPASy, EBI, Israel, Japan] Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T., Weigel N.L., Edwards D.P.; "Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody."; Mol. Endocrinol. 14:52-65(2000).
[12]	PHOSPHORYLATION AT SER-294, UBIQUITINATION, AND MUTAGENESIS OF SER-294; SER-344 AND SER-345. DOI=10.1073/pnas.97.3.1032; PubMed=10655479 [NCBI, ExPASy, EBI, Israel, Japan] Lange C.A., Shen T., Horwitz K.B.; "Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome."; Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000).
[13]	INTERACTION WITH SMARD1. DOI=10.1128/MCB.23.17.6210-6220.2003; PubMed=12917342 [NCBI, ExPASy, EBI, Israel, Japan] Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.; "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."; Mol. Cell. Biol. 23:6210-6220(2003).
[14]	PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-400. DOI=10.1128/MCB.24.24.10542-10557.2004; PubMed=15572662 [NCBI, ExPASy, EBI, Israel, Japan] Pierson-Mullany L.K., Lange C.A.; "Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2."; Mol. Cell. Biol. 24:10542-10557(2004).
[15]	PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION, AND FUNCTION. DOI=10.1128/MCB.25.8.2885-2898.2005; PubMed=15798179 [NCBI, ExPASy, EBI, Israel, Japan] Narayanan R., Edwards D.P., Weigel N.L.; "Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity."; Mol. Cell. Biol. 25:2885-2898(2005).
[16]	INTERACTION WITH UNC45A. DOI=10.1128/MCB.26.5.1722-1730.2006; PubMed=16478993 [NCBI, ExPASy, EBI, Israel, Japan] Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.; "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."; Mol. Cell. Biol. 26:1722-1730(2006).
[17]	SUMOYLATION AT LYS-7; LYS-388 AND LYS-531, INTERACTION WITH PIAS3, FUNCTION, AND MUTAGENESIS OF LYS-7; LYS-388 AND LYS-531. DOI=10.1093/nar/gkl691; PubMed=17020914 [NCBI, ExPASy, EBI, Israel, Japan] Man J.-H., Li H.-Y., Zhang P.-J., Zhou T., He K., Pan X., Liang B., Li A.-L., Zhao J., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.; "PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus."; Nucleic Acids Res. 34:5552-5566(2006).
[18]	INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION AT LYS-388, FUNCTION, AND MUTAGENESIS OF LYS-388. DOI=10.1038/sj.emboj.7601602; PubMed=17347654 [NCBI, ExPASy, EBI, Israel, Japan] Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X., Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.; "CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome."; EMBO J. 26:1831-1842(2007).
[19]	PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, AND MUTAGENESIS OF SER-294 AND LYS-388. DOI=10.1210/me.2007-0248; PubMed=17717077 [NCBI, ExPASy, EBI, Israel, Japan] Daniel A.R., Faivre E.J., Lange C.A.; "Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells."; Mol. Endocrinol. 21:2890-2906(2007).
[20]	PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-294. DOI=10.1016/j.steroids.2006.11.009; PubMed=17173941 [NCBI, ExPASy, EBI, Israel, Japan] Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A., Lange C.A.; "Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth."; Steroids 72:188-201(2007).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[22]	PHOSPHORYLATION AT SER-294; SER-345 AND SER-400, INTERACTION WITH SP1, FUNCTION, AND MUTAGENESIS OF SER-344; SER-345 AND SER-400. DOI=10.1210/me.2007-0437; PubMed=18202149 [NCBI, ExPASy, EBI, Israel, Japan] Faivre E.J., Daniel A.R., Hillard C.J., Lange C.A.; "Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors."; Mol. Endocrinol. 22:823-837(2008).
[23]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 682-933. DOI=10.1038/30775; PubMed=9620806 [NCBI, ExPASy, EBI, Israel, Japan] Williams S.P., Sigler P.B.; "Atomic structure of progesterone complexed with its receptor."; Nature 393:392-396(1998).
[24]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 676-933. DOI=10.1074/jbc.M504144200; PubMed=15937332 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Olland A.M., Zhu Y., Cohen J., Berrodin T., Chippari S., Appavu C., Li S., Wilhem J., Chopra R., Fensome A., Zhang P., Wrobel J., Unwalla R.J., Lyttle C.R., Winneker R.C.; "Molecular and pharmacological properties of a potent and selective novel nonsteroidal progesterone receptor agonist tanaproget."; J. Biol. Chem. 280:28468-28475(2005).

Comments

FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation.
FUNCTION: Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation.
SUBUNIT: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2 MAPK.
INTERACTION:
Q9H467:CUEDC2; NbExp=5; IntAct=EBI-78539, EBI-1248228;
Q8WYK2:JDP2; NbExp=1; IntAct=EBI-78539, EBI-1248415;
Q9Y618:NCOR2; NbExp=1; IntAct=EBI-78539, EBI-80830;
P55345:PRMT2; NbExp=1; IntAct=EBI-78539, EBI-78458;
Q96GM5:SMARCD1; NbExp=1; IntAct=EBI-78539, EBI-358489;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both homone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases.
SUBCELLULAR LOCATION: Isoform A: Nucleus. Cytoplasm. Note=Mainly nuclear.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name B

Isoform ID P06401-1

This is the isoform sequence displayed in this entry.

Name A

Isoform ID P06401-2

Features which should be applied to build the isoform sequence: VSP_003706.
DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-binding domain.
PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1.
PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.
SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.
SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pgr/";.
WEB RESOURCE: Name=Wikipedia; Note=Progesterone receptor entry; URL="http://en.wikipedia.org/wiki/Progesterone_receptor";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X51730; CAA36018.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15716; AAA60081.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016381; AAD01587.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ234979; ABB72139.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY525610; AAS00096.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471065; EAW67000.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00219021; -.
IPI00297419; -.

S09971; QRHUP.

NP_000917.3; -.

3D structure databases

PDB

1A28; X-ray; 1.80 A; A/B=678-933.	[ExPASy / RCSB / EBI]
1E3K; X-ray; 2.80 A; A/B=676-933.	[ExPASy / RCSB / EBI]
1SQN; X-ray; 1.45 A; A/B=673-933.	[ExPASy / RCSB / EBI]
1SR7; X-ray; 1.46 A; A/B=676-933.	[ExPASy / RCSB / EBI]
1ZUC; X-ray; 2.00 A; A/B=676-933.	[ExPASy / RCSB / EBI]
2C7A; X-ray; 2.50 A; A/B=563-640.	[ExPASy / RCSB / EBI]
2OVH; X-ray; 2.00 A; A=678-933.	[ExPASy / RCSB / EBI]
2OVM; X-ray; 2.60 A; A=678-933.	[ExPASy / RCSB / EBI]
2W8Y; X-ray; 1.80 A; A/B=678-933.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1A28; -.
1E3K; -.
1SQN; -.
1SR7; -.
1ZUC; -.
2C7A; -.
2OVH; -.
2OVM; -.
2W8Y; -.

ModBase

P06401.

Protein-protein interaction databases

DIP

DIP:578N; -.
DIP:5967N; -.

IntAct

P06401; 5.

PTM databases

PhosphoSite

P06401; -.

Organism-specific databases

GC11M100414; -.

HIX0035826; -.

HGNC:8910; PGR.

PGR.

CAB000068; -.
HPA004751; -.
HPA008428; -.
HPA017176; -.

MIM

607311; gene. [NCBI / EBI]

PharmGKB

PA266; -.

Gene expression databases

P06401; -.

P06401; -.

HS_PGR; -.

ENSG00000082175; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0047485;	Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0043565;	Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0005496;	Molecular function: steroid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003707;	Molecular function: steroid hormone receptor activity (traceable author statement from ProtInc).
GO:0003700;	Molecular function: transcription factor activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007267;	Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008946; Nucl_hormone_rcpt_ligand-bd.
IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
IPR000128; Progest_rcpt_N.
IPR001723; Str_hrmn_rcpt.
IPR001628; Znf_hrmn_rcpt.
IPR013088; Znf_NHR/GATA.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
G3DSA:3.30.50.10; Znf_NHR/GATA; 1.

Pfam

PF00104; Hormone_recep; 1.
PF02161; Prog_receptor; 1.
PF00105; zf-C4; 1.
Pfam graphical view of domain structure.

PRINTS

PR00544; PROGESTRONER.
PR00398; STRDHORMONER.
PR00047; STROIDFINGER.

ProDom

PD000035; Znf_C4steroid; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00430; HOLI; 1.
SM00399; ZnF_C4; 1.
SMART graphical view of domain structure.

PROSITE

PS00031; NUCLEAR_REC_DBD_1; 1.
PS51030; NUCLEAR_REC_DBD_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P06401; -.

Genome annotation databases

Ensembl

ENSG00000082175; Homo sapiens. [Contig view]

GeneID

5241; -.

KEGG

hsa:5241; -.

Phylogenomic databases

HOGENOM

P06401; -.

HOVERGEN

P06401; -.

OMA

P06401; CLLPRDG.

Other

DrugBank

DB00304; Desogestrel.
DB01395; Drospirenone.
DB00378; Dydrogesterone.
DB00823; Ethynodiol Diacetate.
DB00294; Etonogestrel.
DB00367; Levonorgestrel.
DB00603; Medroxyprogesterone.
DB00351; Megestrol.
DB00834; Mifepristone.
DB00717; Norethindrone.
DB00957; Norgestimate.
DB00506; Norgestrel.
DB00396; Progesterone.

20248; -.

PGR; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Steroid-binding; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 933`	`933`	`Progesterone receptor.`	`PRO_0000053693`
`DNA_BIND`	`567 639`	`73`	`Nuclear receptor.`
`ZN_FING`	`567 587`	`21`	`NR C4-type.`
`ZN_FING`	`603 627`	`25`	`NR C4-type.`
`REGION`	`1 566`	`566`	`Modulating, Pro-Rich.`
`REGION`	`681 933`	`253`	`Steroid-binding.`
`MOTIF`	`183 187`	`5`	`Nuclear localization signal (Potential).`
`MOD_RES`	`20 20`		`Phosphoserine.`
`MOD_RES`	`81 81`		`Phosphoserine.`
`MOD_RES`	`102 102`		`Phosphoserine.`
`MOD_RES`	`130 130`		`Phosphoserine.`
`MOD_RES`	`162 162`		`Phosphoserine.`
`MOD_RES`	`190 190`		`Phosphoserine.`
`MOD_RES`	`213 213`		`Phosphoserine.`
`MOD_RES`	`294 294`		`Phosphoserine; by MAPK1.`
`MOD_RES`	`345 345`		`Phosphoserine; by MAPK.`
`MOD_RES`	`400 400`		`Phosphoserine; by CDK2.`
`MOD_RES`	`676 676`		`Phosphoserine.`
`CROSSLNK`	`7 7`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).`
`CROSSLNK`	`388 388`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate.`
`CROSSLNK`	`388 388`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate.`
`CROSSLNK`	`531 531`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).`
`VAR_SEQ`	`1 164`		`Missing (in isoform A).`	`VSP_003706`
`VARIANT`	`50 50`	`1`	`A -> T.`	`VAR_019221`
`VARIANT`	`120 120`	`1`	`A -> V.`	`VAR_019222`
`VARIANT`	`186 186`	`1`	`P -> L.`	`VAR_019223`
`VARIANT`	`301 301`	`1`	`M -> R.`	`VAR_019224`
`VARIANT`	`344 344`	`1`	`S -> T (in dbSNP:rs3740753 [NCBI]).`	`VAR_016117`
`VARIANT`	`347 347`	`1`	`C -> S (in dbSNP:rs11571147 [NCBI]).`	`VAR_025555`
`VARIANT`	`444 444`	`1`	`A -> S (in dbSNP:rs11571150 [NCBI]).`	`VAR_019225`
`VARIANT`	`529 529`	`1`	`V -> L.`	`VAR_019226`
`VARIANT`	`536 536`	`1`	`Q -> P.`	`VAR_019227`
`VARIANT`	`625 625`	`1`	`R -> I (in dbSNP:rs2020874 [NCBI]).`	`VAR_014627`
`VARIANT`	`651 651`	`1`	`L -> V (in dbSNP:rs11571222 [NCBI]).`	`VAR_019228`
`VARIANT`	`660 660`	`1`	`V -> L (in dbSNP:rs1042838 [NCBI]).`	`VAR_016118`
`VARIANT`	`865 865`	`1`	`S -> L (in dbSNP:rs2020880 [NCBI]).`	`VAR_014628 [3D]`
`MUTAGEN`	`7 7`		`K->R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531.`
`MUTAGEN`	`294 294`		`S->A: No effect on interaction with CUEDC2. Impaired progesterone-induced transciptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation; when associated with A-344 and A-345.`
`MUTAGEN`	`294 294`		`S->D: Decreases protein stability and increases progesterone-induced transcriptional activity.`
`MUTAGEN`	`344 344`		`S->A: No interaction with SP1. No change in progestin-induced protein degradation; when associated with A-345. No change in sumoylation; when associated with A-294 and A-345.`
`MUTAGEN`	`345 345`		`S->A: No change in progestin-induced protein degradation; when associated with A-344. No change in sumoylation; when associated with A-294 and A-344.`
`MUTAGEN`	`388 388`		`K->R: Great loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity.`
`MUTAGEN`	`400 400`		`S->A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin.`
`MUTAGEN`	`531 531`		`K->R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388.`
`CONFLICT`	`226 226`		`G -> S (in Ref. 1; CAA36018).`
`CONFLICT`	`256 256`		`V -> S (in Ref. 1; CAA36018).`
`TURN`	`568 570`	`3`
`STRAND`	`576 578`	`3`
`STRAND`	`581 583`	`3`
`HELIX`	`585 596`	`12`
`TURN`	`613 618`	`6`
`HELIX`	`620 630`	`11`
`HELIX`	`686 694`	`9`
`HELIX`	`711 735`	`25`
`HELIX`	`739 741`	`3`
`HELIX`	`744 771`	`28`
`STRAND`	`774 779`	`6`
`STRAND`	`782 784`	`3`
`HELIX`	`786 788`	`3`
`HELIX`	`792 811`	`20`
`HELIX`	`815 826`	`12`
`STRAND`	`828 830`	`3`
`HELIX`	`838 857`	`20`
`HELIX`	`863 896`	`34`
`HELIX`	`898 901`	`4`
`HELIX`	`907 921`	`15`
`STRAND`	`925 927`	`3`

Sequence information

Length: 933 AA [This is the length of the unprocessed precursor]

Molecular weight: 98981 Da [This is the MW of the unprocessed precursor]

CRC64: 80452E54FF3A0454 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA IPISLDGLLF 

        70         80         90        100        110        120 
PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS SSPPEKDSGL LDSVLDTLLA 

       130        140        150        160        170        180 
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGC KVGDSSGTAA 

       190        200        210        220        230        240 
AHKVLPRGLS PARQLLLPAS ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK 

       250        260        270        280        290        300 
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV 

       310        320        330        340        350        360 
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS TPVAVGDFPD 

       370        380        390        400        410        420 
CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS PRSYLVAGAN PAAFPDFPLG 

       430        440        450        460        470        480 
PPPPLPPRAT PSRPGEAAVT AAPASASVSS ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC 

       490        500        510        520        530        540 
KAPGASGCLL PRDGLPSTSA SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP 

       550        560        570        580        590        600 
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 

       610        620        630        640        650        660 
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA LDAVALPQPV 

       670        680        690        700        710        720 
GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY AGHDNTKPDT SSSLLTSLNQ 

       730        740        750        760        770        780 
LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP 

       790        800        810        820        830        840 
DLILNEQRMK ESSFYSLCLT MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ 

       850        860        870        880        890        900 
FEEMRSSYIR ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 

       910        920        930 
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK

P06401 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools