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Reviewed, UniProtKB/Swiss-Prot Q9UNE7 (STUB1_HUMAN)

Last modified February 9, 2010. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    STIP1 homology and U box-containing protein 1
    EC=6.3.2.-
Alternative name(s):
    Carboxy terminus of Hsp70-interacting protein
    E3 ubiquitin-protein ligase CHIP
    CLL-associated antigen KW-8
    Antigen NY-CO-7
Gene names
Name: STUB1
Synonyms: CHIP
ORF Names: PP1131
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Has E3 ubiquitin-protein ligase activity and targets misfolded chaperone substrates towards proteasomal degradation. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Ref.2 Ref.10 Ref.11

Subunit structure

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. Ref.2 Ref.10 Ref.11 Ref.12 Ref.14

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

Post-translational modification

Auto-ubiquitinated (in vitro).

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25

Involvement in disease

Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients. Ref.1 Ref.3

Sequence similarities

Contains 3 TPR repeats.

Contains 1 U-box domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
TPR repeat
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcellular response to misfolded protein

Inferred from direct assay. Source: UniProtKB

misfolded or incompletely synthesized protein catabolic process

Inferred from direct assay. Source: UniProtKB

positive regulation of cellular chaperone-mediated protein complex assembly

Inferred from direct assay. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process Ref.11

Inferred from direct assay. Source: HGNC

positive regulation of protein ubiquitination Ref.11

Inferred from direct assay. Source: UniProtKB

proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay. Source: HGNC

protein maturation

Traceable author statement. Source: HGNC

protein polyubiquitination

Inferred from direct assay. Source: HGNC

regulation of glucocorticoid metabolic process Ref.11

Inferred from direct assay. Source: HGNC

ubiquitin-dependent SMAD protein catabolic process

Inferred from direct assay. Source: HGNC

   Cellular componentcytoplasm Ref.2

Inferred from direct assay. Source: UniProtKB

nuclear inclusion body

Inferred from direct assay. Source: UniProtKB

ubiquitin conjugating enzyme complex

Traceable author statement. Source: HGNC

ubiquitin ligase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionHsp70 protein binding Ref.2

Inferred from direct assay. Source: HGNC

Hsp90 protein binding Ref.11

Inferred from direct assay. Source: UniProtKB

SMAD binding

Inferred from direct assay. Source: HGNC

TPR domain binding Ref.11

Inferred from direct assay. Source: HGNC

kinase binding

Inferred from physical interaction. Source: UniProtKB

misfolded protein binding

Inferred from direct assay. Source: UniProtKB

protein binding, bridging

Traceable author statement. 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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303STIP1 homology and U box-containing protein 1
PRO_0000106329

Regions

Repeat26 – 5934TPR 1
Repeat60 – 9334TPR 2
Repeat95 – 12733TPR 3
Domain226 – 30075U-box

Amino acid modifications

Modified residue191Phosphoserine Ref.9 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25
Modified residue231Phosphoserine Ref.13 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25
Modified residue251Phosphoserine By similarity
Modified residue2731Phosphoserine Ref.21
Modified residue2761Phosphothreonine Ref.18

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_015947

Experimental info

Sequence conflict521A → V in AAD33400. Ref.2
Sequence conflict2721R → G in AAC18038. Ref.1
Sequence conflict2801L → F in AAC18038. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 7E7D6568B17070BF

FASTA30334,856
        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 

« Hide

Isoform 2.

Checksum: BA7782D3C2F9E1F9
Show »

FASTA23127,067

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), DISEASE.
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), DISEASE.
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[13]"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: Epithelium.
[14]"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.
[15]"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: Epithelium.
[16]"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: Epithelium.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]"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.
[24]"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.
[25]"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: T-cell.
+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.
IPIIPI00025156.
IPI00645380.
RefSeqNP_005852.2.
UniGeneHs.592081

3D structure databases

SMRQ9UNE7. Positions 23-303.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29752N.
IntActQ9UNE7. 12 interactions.
STRINGQ9UNE7.

PTM databases

PhosphoSiteQ9UNE7.

Proteomic databases

PRIDEQ9UNE7.

Genome annotation databases

EnsemblENST00000219548; ENSP00000219548; ENSG00000103266; Homo sapiens. [Genome view]
GeneID10273.
KEGGhsa:10273.
UCSCuc002cit.1. human.
uc002ciu.1. human.

Organism-specific databases

CTD10273.
GeneCardsGC16P000670.
H-InvDBHIX0012661.
HGNCHGNC:11427. STUB1.
MIM607207. gene.
PharmGKBPA36227.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG378130.
HOVERGENQ9UNE7.
InParanoidQ9UNE7.
OMALHSYLTR.
OrthoDBEOG9JQ6HS.
PhylomeDBQ9UNE7.

Enzyme and pathway databases

Pathway_Interaction_DBalphasynuclein_pathway. Alpha-synuclein signaling.

Gene expression databases

ArrayExpressQ9UNE7.
BgeeQ9UNE7.
CleanExHS_STUB1.
GenevestigatorQ9UNE7.
GermOnlineENSG00000103266. Homo sapiens.

Family and domain databases

InterProIPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
IPR003613. Ubox_domain.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF04564. U-box. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
SM00504. Ubox. 1 hit.
[Graphical view]
PROSITEPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio38918.
SOURCESearch...

Entry information

Entry nameSTUB1_HUMAN
AccessionPrimary (citable) accession number: Q9UNE7
Secondary accession number(s): A2IDB9 expand/collapse secondary AC list , O60526, Q969U2, Q9HBT1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: February 9, 2010
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents