Q9UNE7 (CHIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase CHIP
EC=6.3.2.-

Alternative name(s):
Antigen NY-CO-7
CLL-associated antigen KW-8
Carboxy terminus of Hsp70-interacting protein
STIP1 homology and U box-containing protein 1

Gene names

Name:	STUB1
Synonyms:	CHIP
ORF Names:	PP1131

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Ref.2 Ref.10 Ref.11 Ref.12 Ref.27 Ref.28 Ref.30
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homodimer By similarity. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W By similarity. Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Ref.2 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.23 Ref.28 Ref.29
Subcellular location	Cytoplasm Ref.2.
Tissue specificity	Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. Ref.2
Domain	The TPR domain is essential for ubiquitination mediated by UBE2D1. Ref.22
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.31 Ref.32 Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 By similarity. Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.
Miscellaneous	Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients.
Sequence similarities	Contains 3 TPR repeats. Contains 1 U-box domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
Molecular function	Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cellular response to misfolded protein Inferred from direct assay PubMed 16831871. Source: BHF-UCL misfolded or incompletely synthesized protein catabolic process Inferred from direct assay PubMed 16831871. Source: BHF-UCL positive regulation of chaperone-mediated protein complex assembly Inferred from direct assay PubMed 16831871. Source: BHF-UCL positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.11. Source: HGNC positive regulation of protein ubiquitination Inferred from direct assay PubMed 16831871. Source: BHF-UCL proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 15781469. Source: HGNC protein K63-linked ubiquitination Inferred from direct assay Ref.16. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.22Ref.16. Source: UniProtKB protein maturation Traceable author statement Ref.16. Source: HGNC regulation of glucocorticoid metabolic process Inferred from direct assay Ref.11. Source: HGNC ubiquitin-dependent SMAD protein catabolic process Inferred from direct assay PubMed 15781469. Source: HGNC
Cellular component	cytosol Traceable author statement. Source: Reactome nuclear inclusion body Inferred from direct assay PubMed 16831871. Source: BHF-UCL ubiquitin conjugating enzyme complex Traceable author statement Ref.16. Source: HGNC ubiquitin ligase complex Inferred from direct assay Ref.16. Source: UniProtKB
Molecular function	Hsp70 protein binding Inferred from direct assay Ref.2. Source: HGNC Hsp90 protein binding Inferred from direct assay Ref.11. Source: BHF-UCL SMAD binding Inferred from direct assay PubMed 15781469. Source: HGNC TPR domain binding Inferred from direct assay Ref.11. Source: HGNC kinase binding Inferred from physical interaction PubMed 17512523. Source: BHF-UCL misfolded protein binding Inferred from direct assay PubMed 16831871. Source: BHF-UCL protein binding, bridging Traceable author statement Ref.16. Source: HGNC protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-ubiquitin ligase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATCAY	Q86WG3	4	EBI-357085,EBI-1783328
HSP90AA1	P07900	9	EBI-357085,EBI-296047
HSPA1B	P08107	3	EBI-357085,EBI-629985
HSPA8	P11142	3	EBI-357085,EBI-351896
MAPT	P10636	2	EBI-357085,EBI-366182
UBE2N	P61088	3	EBI-357085,EBI-1052908
UBE2Q1	Q7Z7E8	3	EBI-357085,EBI-1783287

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UNE7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UNE7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	E3 ubiquitin-protein ligase CHIP		PRO_0000106329
Regions
	Repeat	26 – 59	34	TPR 1
	Repeat	60 – 93	34	TPR 2
	Repeat	95 – 127	33	TPR 3
	Domain	226 – 300	75	U-box
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.9 Ref.14 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.25 Ref.26 Ref.31 Ref.32
	Modified residue	23	1	Phosphoserine Ref.14 Ref.17 Ref.18 Ref.21 Ref.24 Ref.25 Ref.26 Ref.32
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	273	1	Phosphoserine Ref.25
	Modified residue	276	1	Phosphothreonine Ref.20
	Cross-link	2		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	22		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22
	Cross-link	221		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22
	Cross-link	255		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22
Natural variations
	Alternative sequence	1 – 72	72	Missing in isoform 2.		VSP_015947
Experimental info
	Sequence conflict	52	1	A → V in AAD33400. Ref.2
	Sequence conflict	272	1	R → G in AAC18038. Ref.1
	Sequence conflict	280	1	L → F in AAC18038. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 25, 2005. Version 2. Checksum: 7E7D6568B17070BF	FASTA	303	34,856
	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
	Isoform 2 [UniParc]. Checksum: BA7782D3C2F9E1F9	FASTA	231	27,067
	10 20 30 40 50 60 MQQHEQALAD CRRALELDGQ SVKAHFFLGQ CQLEMESYDE AIANLQRAYS LAKEQRLNFG 70 80 90 100 110 120 DDIPSALRIA KKKRWNSIEE RRIHQESELH SYLSRLIAAE RERELEECQR NHEGDEDDSH 130 140 150 160 170 180 VRAQQACIEA KHDKYMADMD ELFSQVDEKR KKRDIPDYLC GKISFELMRE PCITPSGITY 190 200 210 220 230 DRKDIEEHLQ RVGHFDPVTR SPLTQEQLIP NLAMKEVIDA FISENGWVED Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human colon cancer antigens recognized by autologous antibodies." 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. Int. J. Cancer 76:652-658(1998) [PubMed: 9610721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN. Tissue: Colon carcinoma.
[2]	"Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions." Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C. Mol. Cell. Biol. 19:4535-4545(1999) [PubMed: 10330192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HSPA8 AND HSPA1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Heart.
[3]	"Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX." Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G. Blood 100:2123-2131(2002) [PubMed: 12200376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN.
[4]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." 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. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." 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. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed: 15498874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon and Skin.
[9]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 13-30; 56-66; 86-119; 129-140; 155-167; 235-241; 256-263 AND 273-287, PHOSPHORYLATION AT SER-19, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation." Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J., Patterson C. J. Biol. Chem. 276:42938-42944(2001) [PubMed: 11557750] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3.
[11]	"The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins." Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hoehfeld J., Patterson C. Nat. Cell Biol. 3:93-96(2001) [PubMed: 11146632] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP90.
[12]	"Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase." Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C., Pratt W.B., Osawa Y. J. Biol. Chem. 279:52970-52977(2004) [PubMed: 15466472] [Abstract] Cited for: FUNCTION.
[13]	"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator." Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J. Mol. Biol. Cell 15:4003-4010(2004) [PubMed: 15215316] [Abstract] Cited for: INTERACTION WITH HSPA1A AND HSPBP1.
[14]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Regulation of the cytoplasmic quality control protein degradation pathway by BAG2." 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. J. Biol. Chem. 280:38673-38681(2005) [PubMed: 16169850] [Abstract] Cited for: INTERACTION WITH BAG2.
[16]	"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex." Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H. Mol. Cell 20:525-538(2005) [PubMed: 16307917] [Abstract] Cited for: INTERACTION WITH UBE2N AND UBE2V1.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology." Windheim M., Peggie M., Cohen P. Biochem. J. 409:723-729(2008) [PubMed: 18042044] [Abstract] Cited for: POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255, DOMAIN TPR.
[23]	"MKKS is a centrosome-shuttling protein degraded by disease-causing mutations via CHIP-mediated ubiquitination." Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K., Kimura H., Cyr D.M., Kubota H., Nagata K. Mol. Biol. Cell 19:899-911(2008) [PubMed: 18094050] [Abstract] Cited for: INTERACTION WITH MKKS.
[24]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[27]	"CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases." Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A. Arch. Biochem. Biophys. 483:66-74(2009) [PubMed: 19103148] [Abstract] Cited for: FUNCTION.
[28]	"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair." Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J., Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L. EMBO J. 28:3207-3215(2009) [PubMed: 19713937] [Abstract] Cited for: FUNCTION, INTERACTION WITH POLB.
[29]	"Functional interaction of DYX1C1 with estrogen receptors suggests involvement of hormonal pathways in dyslexia." Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E., Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E., Kere J. Hum. Mol. Genet. 18:2802-2812(2009) [PubMed: 19423554] [Abstract] Cited for: INTERACTION WITH DYX1C1.
[30]	"Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis." Annamalai B., Liu X., Gopal U., Isaacs J.S. Mol. Cancer Res. 7:1021-1032(2009) [PubMed: 19567782] [Abstract] Cited for: FUNCTION.
[31]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY.
[32]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[33]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF039689 mRNA. Translation: AAC18038.1. AF129085 mRNA. Translation: AAD33400.1. AF432221 mRNA. Translation: AAL99927.1. AF217968 mRNA. Translation: AAG17211.1. AE006464 Genomic DNA. Translation: AAK61242.1. Z92544 Genomic DNA. Translation: CAM26348.1. CH471112 Genomic DNA. Translation: EAW85758.1. BC007545 mRNA. Translation: AAH07545.1. BC017178 mRNA. Translation: AAH17178.1. BC022788 mRNA. Translation: AAH22788.1. BC063617 mRNA. Translation: AAH63617.1.
IPI	IPI00025156. IPI00645380.
RefSeq	NP_005852.2. NM_005861.2.
UniGene	Hs.592081.
3D structure databases
ProteinModelPortal	Q9UNE7.
SMR	Q9UNE7. Positions 23-303.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29752N.
IntAct	Q9UNE7. 24 interactions.
MINT	MINT-1132706.
STRING	Q9UNE7.
PTM databases
PhosphoSite	Q9UNE7.
Polymorphism databases
DMDM	78099173.
Proteomic databases
PRIDE	Q9UNE7.
Protocols and materials databases
DNASU	10273.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219548; ENSP00000219548; ENSG00000103266.
GeneID	10273.
KEGG	hsa:10273.
UCSC	uc002cit.3. human.
Organism-specific databases
CTD	10273.
GeneCards	GC16P000735.
H-InvDB	HIX0012661.
HGNC	HGNC:11427. STUB1.
MIM	607207. gene.
neXtProt	NX_Q9UNE7.
PharmGKB	PA36227.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5113.
GeneTree	ENSGT00650000093277.
HOGENOM	HOG000163725.
HOVERGEN	HBG053046.
InParanoid	Q9UNE7.
KO	K09561.
OMA	LHSYLTR.
OrthoDB	EOG4Z36F9.
PhylomeDB	Q9UNE7.
Enzyme and pathway databases
Pathway_Interaction_DB	alphasynuclein_pathway. Alpha-synuclein signaling.
Reactome	REACT_111102. Signal Transduction. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9UNE7.
Bgee	Q9UNE7.
CleanEx	HS_STUB1.
Genevestigator	Q9UNE7.
GermOnline	ENSG00000103266. Homo sapiens.
Family and domain databases
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit. G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
InterPro	IPR001440. TPR-1. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. IPR003613. Ubox_domain. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00515. TPR_1. 2 hits. PF04564. U-box. 1 hit. [Graphical view]
SMART	SM00028. TPR. 3 hits. SM00504. Ubox. 1 hit. [Graphical view]
PROSITE	PS50005. TPR. 3 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	38918.
SOURCE	Search...

Entry information

Entry name

CHIP_HUMAN

Accession

Primary (citable) accession number: Q9UNE7
Secondary accession number(s): A2IDB9 , O60526, Q969U2, Q9HBT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 16, 2012
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.