Q9UNE7 (CHIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 16, 2012.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||||
| 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 | |
| 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 | |
| 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
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
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References
| « Hide '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. 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. 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. 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 Q9HBT1 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with