[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. PubMed=1729596 [NCBI, ExPASy, EBI, Israel, Japan] Matunis M.J., Michael W.M., Dreyfuss G.; "Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein."; Mol. Cell. Biol. 12:164-171(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION. DOI=10.1006/jmbi.1994.1116; PubMed=8107114 [NCBI, ExPASy, EBI, Israel, Japan] Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B., Nielsen H., Celis J.E.; "Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing."; J. Mol. Biol. 236:33-48(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). TISSUE=Brain; Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan] Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.; "DNA sequence and analysis of human chromosome 9."; Nature 429:369-374(2004).
[5]	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.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). TISSUE=Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 1-52; 70-103; 149-163; 192-201; 208-219; 317-325; 378-405 AND 423-456, ACETYLATION AT MET-1, AND MASS SPECTROMETRY. TISSUE=Lung carcinoma; Bienvenut W.V., Vousden K.H., Lukashchuk N.; Submitted (MAR-2008) to UniProtKB.
[8]	PROTEIN SEQUENCE OF 38-46; 149-163; 208-219; 306-316 AND 378-396, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[9]	INTERACTION WITH HCV CORE PROTEIN. DOI=10.1074/jbc.273.28.17651; PubMed=9651361 [NCBI, ExPASy, EBI, Israel, Japan] Hsieh T.-Y., Matsumoto M., Chou H.-C., Schneider R., Hwang S.B., Lee A.S., Lai M.M.C.; "Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K."; J. Biol. Chem. 273:17651-17659(1998).
[10]	MASS SPECTROMETRY. TISSUE=Mammary cancer; DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H; PubMed=11840567 [NCBI, ExPASy, EBI, Israel, Japan] Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.; "Cluster analysis of an extensive human breast cancer cell line protein expression map database."; Proteomics 2:212-223(2002).
[11]	IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX. DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan] Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."; RNA 8:426-439(2002).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS SPECTROMETRY. DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.-E., Tannenbaum S.R., White F.M.; "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; J. Proteome Res. 4:1339-1346(2005).
[13]	INTERACTION WITH ANKRD28, AND PHOSPHORYLATION AT SER-284. DOI=10.1016/j.cellsig.2006.01.019; PubMed=16564677 [NCBI, ExPASy, EBI, Israel, Japan] Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.; "PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K."; Cell. Signal. 18:1769-1778(2006).
[14]	METHYLATION [LARGE SCALE ANALYSIS] AT ARG-296 AND ARG-299, AND MASS SPECTROMETRY. DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan] Ong S.E., Mittler G., Mann M.; "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."; Nat. Methods 1:119-126(2004).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-116 AND SER-284, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-216 AND SER-284, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 AND SER-379, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216 AND SER-379, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-284, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[21]	INTERACTION WITH ASFV PROTEIN P30. DOI=10.1016/j.febslet.2008.08.031; PubMed=18775702 [NCBI, ExPASy, EBI, Israel, Japan] Hernaez B., Escribano J.M., Alonso C.; "African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection."; FEBS Lett. 582:3275-3280(2008).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-284, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND SER-284, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]	STRUCTURE BY NMR OF 375-463. DOI=10.1006/jmbi.1999.2818; PubMed=10369774 [NCBI, ExPASy, EBI, Israel, Japan] Baber J.L., Libutti D., Levens D., Tjandra N.; "High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor."; J. Mol. Biol. 289:949-962(1999).
[25]	STRUCTURE BY NMR OF 379-463 IN COMPLEX WITH SINGLE STRANDED DNA. DOI=10.1093/emboj/cdf352; PubMed=12093748 [NCBI, ExPASy, EBI, Israel, Japan] Braddock D.T., Baber J.L., Levens D., Clore G.M.; "Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA."; EMBO J. 21:3476-3485(2002).

Comments

FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA.
SUBUNIT: Interacts with RBM42 and ZIK1 (By similarity). Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRNPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein.
INTERACTION:
P08631:HCK; NbExp=1; IntAct=EBI-304185, EBI-346340;
Q96PU8:QKI; NbExp=1; IntAct=EBI-304185, EBI-945792;
P50616:TOB1; NbExp=1; IntAct=EBI-304185, EBI-723281;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Note=In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P61978-1, Q07244-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P61978-2, Q07244-2
Features which should be applied to build the isoform sequence: VSP_002822.

Name	3
Isoform ID	P61978-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_021669, VSP_002822.

PTM: Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.
MASS SPECTROMETRY: Mass=50976.25; Method=MALDI; Range=1-463 (P61978-1); Source=PubMed:11840567;.
SIMILARITY: Contains 3 KH domains.

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

S74678; AAB20770.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X72727; CAA51267.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209562; BAD92799.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL354733; CAI16020.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471089; EAW62675.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000355; AAH00355.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014980; AAH14980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00216049; -.
IPI00216746; -.
IPI00807545; -.

PIR

S43363; S43363.

RefSeq

NP_002131.2; -.
NP_112552.1; -.
NP_112553.1; -.

UniGene

Hs.522257

3D structure databases

PDB

1J5K; NMR; -; A=379-463.	[ExPASy / RCSB / EBI]
1KHM; NMR; -; A=379-463.	[ExPASy / RCSB / EBI]
1ZZI; X-ray; 1.80 A; A/B=385-463.	[ExPASy / RCSB / EBI]
1ZZJ; X-ray; 2.30 A; A/B/C=385-463.	[ExPASy / RCSB / EBI]
1ZZK; X-ray; 0.95 A; A=385-463.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1J5K; -.
1KHM; -.
1ZZI; -.
1ZZJ; -.
1ZZK; -.

ModBase

P61978.

Protein-protein interaction databases

IntAct

P61978; 28.

PTM databases

PhosphoSite

P61978; -.

Enzyme and pathway databases

Reactome

REACT_1675; mRNA Processing.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.

2D gel databases

SWISS-2DPAGE

P61978; -.

Organism-specific databases

GC09M085775; -.

HIX0008131; -.

HGNC:5044; HNRNPK.

CAB004435; -.
CAB016225; -.
HPA007644; -.

MIM

600712; gene. [NCBI / EBI]

PharmGKB

PA29368; -.

Gene expression databases

P61978; -.

P61978; -.

HS_HNRNPK; -.

ENSG00000165119; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0030530;	Cellular component: heterogeneous nuclear ribonucleoprotein complex (traceable author statement from ProtInc).
GO:0005654;	Cellular component: nucleoplasm (traceable author statement from ProtInc).
GO:0005681;	Cellular component: spliceosome (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723;	Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0000398;	Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
GO:0007165;	Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR004087; KH.
IPR004088; KH_type_1.
IPR018111; KH_type_1_subgr.
IPR012987; ROK_N.
Graphical view of domain structure.

Pfam

PF00013; KH_1; 3.
PF08067; ROKNT; 1.
Pfam graphical view of domain structure.

SMART

SM00322; KH; 3.
SMART graphical view of domain structure.

PROSITE

PS50084; KH_TYPE_1; 3.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P61978; -.

Genome annotation databases

Ensembl

ENSG00000165119; Homo sapiens. [Contig view]

GeneID

3190; -.

KEGG

hsa:3190; -.

Phylogenomic databases

HOVERGEN

P61978; -.

OMA

P61978; XGLQLPS.

Other

NextBio

12686; -.

PMAP-CutDB

P61978; -.

SOURCE

HNRNPK; Homo sapiens.

ProtoNet

P61978.

UniRef

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

Keywords

3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; DNA-binding; Host-virus interaction; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 463`	`463`	`Heterogeneous nuclear ribonucleoprotein K.`	`PRO_0000050096`
`DOMAIN`	`42 104`	`63`	`KH 1.`
`REPEAT`	`54 76`	`23`	`1-1.`
`REPEAT`	`59 62`	`4`	`3-1.`
`DOMAIN`	`144 209`	`66`	`KH 2.`
`REPEAT`	`245 250`	`6`	`2-1.`
`REPEAT`	`257 260`	`4`	`3-2.`
`REPEAT`	`267 270`	`4`	`3-3.`
`REPEAT`	`295 298`	`4`	`3-4.`
`REPEAT`	`324 329`	`6`	`2-2.`
`DOMAIN`	`387 451`	`65`	`KH 3.`
`REPEAT`	`399 421`	`23`	`1-2.`
`REPEAT`	`404 407`	`4`	`3-5.`
`REGION`	`35 197`	`163`	`Interaction with ASFV p30.`
`REGION`	`54 421`	`368`	`2 X 22 AA approximate repeats.`
`REGION`	`59 407`	`349`	`5 X 4 AA repeats of G-X-G-G.`
`REGION`	`209 337`	`129`	`Interaction with ZIK1 (By similarity).`
`REGION`	`236 273`	`38`	`RNA-binding RGG-box.`
`REGION`	`245 329`	`85`	`2 X 6 AA approximate repeats.`
`COMPBIAS`	`289 294`	`6`	`Poly-Pro.`
`COMPBIAS`	`310 315`	`6`	`Poly-Pro.`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`MOD_RES`	`3 3`		`Phosphothreonine.`
`MOD_RES`	`36 36`		`Phosphoserine.`
`MOD_RES`	`116 116`		`Phosphoserine.`
`MOD_RES`	`214 214`		`Phosphoserine.`
`MOD_RES`	`216 216`		`Phosphoserine.`
`MOD_RES`	`284 284`		`Phosphoserine.`
`MOD_RES`	`296 296`		`Omega-N-methylated arginine.`
`MOD_RES`	`299 299`		`Omega-N-methylated arginine.`
`MOD_RES`	`379 379`		`Phosphoserine.`
`VAR_SEQ`	`111 134`		`Missing (in isoform 3).`	`VSP_021669`
`VAR_SEQ`	`459 463`		`SGKFF -> ADVEGF (in isoform 2 and isoform 3).`	`VSP_002822`
`CONFLICT`	`32 32`		`A -> D (in Ref. 2; CAA51267).`
`STRAND`	`388 395`	`8`
`TURN`	`396 398`	`3`
`HELIX`	`399 402`	`4`
`HELIX`	`405 407`	`3`
`HELIX`	`408 417`	`10`
`STRAND`	`420 423`	`4`
`STRAND`	`430 439`	`10`
`HELIX`	`441 459`	`19`

Sequence information

Length: 463 AA [This is the length of the unprocessed precursor]

Molecular weight: 50976 Da [This is the MW of the unprocessed precursor]

CRC64: 0F70EE169B2A064A [This is a checksum on the sequence]

        10         20         30         40         50         60 
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK 

        70         80         90        100        110        120 
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT 

       130        140        150        160        170        180 
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL 

       190        200        210        220        230        240 
FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT 

       250        260        270        280        290        300 
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 

       310        320        330        340        350        360 
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA 

       370        380        390        400        410        420 
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS 

       430        440        450        460 
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF

P61978 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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