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UniProtKB/Swiss-Prot entry Q9UNE7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name STUB1_HUMAN
Primary accession number Q9UNE7
Secondary accession numbers O60526 Q969U2 Q9HBT1
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 25, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 69)
Name and origin of the protein
Protein name STIP1 homology and U box-containing protein 1
Synonyms EC 6.3.2.-
Carboxy terminus of Hsp70-interacting protein
E3 ubiquitin-protein ligase CHIP
CLL-associated antigen KW-8
Antigen NY-CO-7
Gene name
Name: STUB1
Synonyms: CHIP
ORFNames: PP1131
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
TISSUE=Colon carcinoma;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P; PubMed=9610721 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HSPA8 AND HSPA1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=10330192 [NCBI, ExPASy, EBI, Israel, Japan]
Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.;
"Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.";
Mol. Cell. Biol. 19:4535-4545(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
DOI=10.1182/blood-2002-02-0513; PubMed=12200376 [NCBI, ExPASy, EBI, Israel, Japan]
Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.;
"Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX.";
Blood 100:2123-2131(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/hmg/10.4.339; PubMed=11157797 [NCBI, ExPASy, EBI, Israel, Japan]
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1073/pnas.0404089101; PubMed=15498874 [NCBI, ExPASy, EBI, Israel, Japan]
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Skin;
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 13-30; 56-66; 86-119; 129-140; 155-167; 235-241; 256-263 AND 273-287, PHOSPHORYLATION AT SER-19, AND MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[8]
FUNCTION, AND INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3.
DOI=10.1074/jbc.M101968200; PubMed=11557750 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J., Patterson C.;
"CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation.";
J. Biol. Chem. 276:42938-42944(2001).
[9]
FUNCTION, AND INTERACTION WITH HSP90.
DOI=10.1038/35050618; PubMed=11146632 [NCBI, ExPASy, EBI, Israel, Japan]
Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hoehfeld J., Patterson C.;
"The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.";
Nat. Cell Biol. 3:93-96(2001).
[10]
INTERACTION WITH HSPA1A AND HSPBP1.
DOI=10.1091/mbc.E04-04-0293; PubMed=15215316 [NCBI, ExPASy, EBI, Israel, Japan]
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.";
Mol. Biol. Cell 15:4003-4010(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, 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).
[12]
INTERACTION WITH BAG2.
DOI=10.1074/jbc.M507986200; PubMed=16169850 [NCBI, ExPASy, EBI, Israel, Japan]
Dai Q., Qian S.B., Li H.-H., McDonough H., Borchers C., Huang D., Takayama S., Younger J.M., Ren H.Y., Cyr D.M., Patterson C.;
"Regulation of the cytoplasmic quality control protein degradation pathway by BAG2.";
J. Biol. Chem. 280:38673-38681(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, 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).
[20]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
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
AF039689; AAC18038.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF129085; AAD33400.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF432221; AAL99927.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF217968; AAG17211.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006464; AAK61242.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007545; AAH07545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017178; AAH17178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022788; AAH22788.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063617; AAH63617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00025156; -.
IPI00645380; -.
RefSeq NP_005852.2; -.
UniGene Hs.592081
3D structure databases
SMR Q9UNE7; 23-303.
ModBase Q9UNE7.
Protein-protein interaction databases
IntAct Q9UNE7; 12.
PTM databases
PhosphoSite Q9UNE7; -.
Enzyme and pathway databases
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
Organism-specific databases
GeneCards GC16P000670; -.
H-InvDB HIX0012661; -.
HGNC HGNC:11427; STUB1.
GenAtlas STUB1.
MIM 607207; gene. [NCBI / EBI]
PharmGKB PA36227; -.
Gene expression databases
Bgee Q9UNE7; -.
CleanEx HS_STUB1; -.
GermOnline ENSG00000103266; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HGNC).
GO:0031371; Cellular component: ubiquitin conjugating enzyme complex (traceable author statement from HGNC).
GO:0000151; Cellular component: ubiquitin ligase complex (inferred from electronic annotation from InterPro).
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0030544; Molecular function: Hsp70 protein binding (inferred from direct assay from HGNC).
GO:0030191; Molecular function: Hsp70/Hsc70 protein inhibitor activity (inferred from direct assay from HGNC).
GO:0051879; Molecular function: Hsp90 protein binding (inferred from direct assay from HGNC).
GO:0010546; Molecular function: Hsp90 protein inhibitor activity (inferred from direct assay from UniProtKB).
GO:0030674; Molecular function: protein binding, bridging (traceable author statement from HGNC).
GO:0046332; Molecular function: SMAD binding (inferred from direct assay from HGNC).
GO:0030911; Molecular function: TPR domain binding (inferred from direct assay from HGNC).
GO:0032436; Biological process: positive regulation of proteasomal ubiquitin-dependent protein catabolic process (inferred from direct assay from HGNC).
GO:0031398; Biological process: positive regulation of protein ubiquitination (inferred from direct assay from HGNC).
GO:0043161; Biological process: proteasomal ubiquitin-dependent protein catabolic process (inferred from direct assay from HGNC).
GO:0006457; Biological process: protein folding (traceable author statement from HGNC).
GO:0051604; Biological process: protein maturation (traceable author statement from HGNC).
GO:0000209; Biological process: protein polyubiquitination (inferred from direct assay from HGNC).
GO:0031943; Biological process: regulation of glucocorticoid metabolic process (inferred from direct assay from HGNC).
GO:0030579; Biological process: ubiquitin-dependent SMAD protein catabolic process (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
IPR019734; TPR_repeat.
IPR003613; Ubox_domain.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF00515; TPR_1; 3.
PF04564; U-box; 1.
Pfam graphical view of domain structure.
SMART SM00028; TPR; 3.
SM00504; Ubox; 1.
SMART graphical view of domain structure.
PROSITE PS50005; TPR; 3.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9UNE7; -.
Genome annotation databases
Ensembl ENSG00000103266; Homo sapiens. [Contig view]
GeneID 10273; -.
KEGG hsa:10273; -.
Phylogenomic databases
HOGENOM Q9UNE7; -.
HOVERGEN Q9UNE7; -.
OMA Q9UNE7; LHSYLTR.
Other
NextBio 38918; -.
SOURCE STUB1; Homo sapiens.
ProtoNet Q9UNE7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; Direct protein sequencing; Ligase; Phosphoprotein; Repeat; TPR repeat; Ubl conjugation; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   303  303     STIP1 homology and U box-containing protein 1. PRO_0000106329
REPEAT   26    59  34     TPR 1. 
REPEAT   60    93  34     TPR 2. 
REPEAT   95   127  33     TPR 3. 
DOMAIN   226   300  75     U-box. 
MOD_RES   19    19        Phosphoserine. 
MOD_RES   23    23        Phosphoserine. 
MOD_RES   25    25        Phosphoserine (By similarity). 
MOD_RES   273   273        Phosphoserine. 
MOD_RES   276   276        Phosphothreonine. 
VAR_SEQ   1    72        Missing (in isoform 2). VSP_015947
CONFLICT   52    52        A -> V (in Ref. 2; AAD33400). 
CONFLICT   272   272        R -> G (in Ref. 1; AAC18038). 
CONFLICT   280   280        L -> F (in Ref. 1; AAC18038). 
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 34856 Da [This is the MW of the unprocessed precursor] CRC64: 7E7D6568B17070BF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA 

        70         80         90        100        110        120 
VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA 

       130        140        150        160        170        180 
YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC 

       190        200        210        220        230        240 
QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM 

       250        260        270        280        290        300 
REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV 


EDY 

Q9UNE7 in FASTA format

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