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P50502

- F10A1_HUMAN

UniProt

P50502 - F10A1_HUMAN

Protein

Hsc70-interacting protein

Gene

ST13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins By similarity.By similarity

    GO - Molecular functioni

    1. dATP binding Source: Ensembl
    2. protein binding Source: IntAct
    3. protein binding, bridging Source: ProtInc

    GO - Biological processi

    1. chaperone cofactor-dependent protein refolding Source: Ensembl
    2. negative regulation of protein refolding Source: Ensembl
    3. protein folding Source: ProtInc
    4. protein homooligomerization Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hsc70-interacting protein
    Short name:
    Hip
    Alternative name(s):
    Aging-associated protein 2
    Progesterone receptor-associated p48 protein
    Protein FAM10A1
    Putative tumor suppressor ST13
    Renal carcinoma antigen NY-REN-33
    Suppression of tumorigenicity 13 protein
    Gene namesi
    Name:ST13
    Synonyms:AAG2, FAM10A1, HIP, SNC6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11343. ST13.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Hsc70-interacting proteinPRO_0000190811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei346 – 3461Phosphoserine; by GRK51 Publication
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei360 – 3601N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP50502.
    PaxDbiP50502.
    PeptideAtlasiP50502.
    PRIDEiP50502.

    2D gel databases

    OGPiP50502.
    REPRODUCTION-2DPAGEIPI00032826.

    PTM databases

    PhosphoSiteiP50502.

    Miscellaneous databases

    PMAP-CutDBP50502.

    Expressioni

    Gene expression databases

    ArrayExpressiP50502.
    BgeeiP50502.
    CleanExiHS_ST13.
    GenevestigatoriP50502.

    Organism-specific databases

    HPAiHPA043233.
    HPA046412.
    HPA047114.
    HPA047116.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 By similarity. Interacts (via the C-terminus 303- 319 AA) with GRK5.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APOEP026493EBI-357285,EBI-1222467
    NOS3P294743EBI-357285,EBI-1391623
    PSEN1P497683EBI-357285,EBI-297277

    Protein-protein interaction databases

    BioGridi112644. 34 interactions.
    IntActiP50502. 22 interactions.
    MINTiMINT-4999606.
    STRINGi9606.ENSP00000216218.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UZSmodel-A98-244[»]
    ProteinModelPortaliP50502.
    SMRiP50502. Positions 1-44, 78-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati114 – 14734TPR 1Add
    BLAST
    Repeati148 – 18134TPR 2Add
    BLAST
    Repeati182 – 21534TPR 3Add
    BLAST
    Domaini319 – 35840STI1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi279 – 31234Gly/Met/Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FAM10 family.Curated
    Contains 1 STI1 domain.Curated
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG260098.
    HOGENOMiHOG000001586.
    HOVERGENiHBG002482.
    InParanoidiP50502.
    KOiK09560.
    OMAiQANEKKM.
    OrthoDBiEOG77M8P3.
    PhylomeDBiP50502.
    TreeFamiTF313244.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR006636. STI1_HS-bd.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 2 hits.
    [Graphical view]
    SMARTiSM00727. STI1. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50502-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK    50
    SEENTKEEKP DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG 100
    DENAEITEEM MDQANDKKVA AIEALNDGEL QKAIDLFTDA IKLNPRLAIL 150
    YAKRASVFVK LQKPNAAIRD CDRAIEINPD SAQPYKWRGK AHRLLGHWEE 200
    AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER KREEREIKER 250
    IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM 300
    GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS 350
    NPKVMNLISK LSAKFGGQA 369
    Length:369
    Mass (Da):41,332
    Last modified:May 30, 2000 - v2
    Checksum:i98FCC65BEE14CDD7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241H → Y in AAB38382. (PubMed:8721986)Curated
    Sequence conflicti38 – 381M → I in AAB38382. (PubMed:8721986)Curated
    Sequence conflicti50 – 501K → I in AAB38382. (PubMed:8721986)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti297 – 2971M → I.
    Corresponds to variant rs710193 [ dbSNP | Ensembl ].
    VAR_011900

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28918 mRNA. Translation: AAB38382.1.
    U17714 mRNA. Translation: AAC97526.1.
    AY513286 mRNA. Translation: AAT08039.1.
    CR456586 mRNA. Translation: CAG30472.1.
    Z98048 Genomic DNA. Translation: CAB10844.1.
    CH471095 Genomic DNA. Translation: EAW60394.1.
    BC052982 mRNA. Translation: AAH52982.1.
    BC071629 mRNA. Translation: AAH71629.1.
    BC139724 mRNA. Translation: AAI39725.1.
    CCDSiCCDS14006.1.
    RefSeqiNP_003923.2. NM_003932.4.
    UniGeneiHs.712713.

    Genome annotation databases

    EnsembliENST00000216218; ENSP00000216218; ENSG00000100380.
    GeneIDi6767.
    KEGGihsa:6767.
    UCSCiuc003aze.3. human.

    Polymorphism databases

    DMDMi6686278.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28918 mRNA. Translation: AAB38382.1 .
    U17714 mRNA. Translation: AAC97526.1 .
    AY513286 mRNA. Translation: AAT08039.1 .
    CR456586 mRNA. Translation: CAG30472.1 .
    Z98048 Genomic DNA. Translation: CAB10844.1 .
    CH471095 Genomic DNA. Translation: EAW60394.1 .
    BC052982 mRNA. Translation: AAH52982.1 .
    BC071629 mRNA. Translation: AAH71629.1 .
    BC139724 mRNA. Translation: AAI39725.1 .
    CCDSi CCDS14006.1.
    RefSeqi NP_003923.2. NM_003932.4.
    UniGenei Hs.712713.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UZS model - A 98-244 [» ]
    ProteinModelPortali P50502.
    SMRi P50502. Positions 1-44, 78-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112644. 34 interactions.
    IntActi P50502. 22 interactions.
    MINTi MINT-4999606.
    STRINGi 9606.ENSP00000216218.

    PTM databases

    PhosphoSitei P50502.

    Polymorphism databases

    DMDMi 6686278.

    2D gel databases

    OGPi P50502.
    REPRODUCTION-2DPAGE IPI00032826.

    Proteomic databases

    MaxQBi P50502.
    PaxDbi P50502.
    PeptideAtlasi P50502.
    PRIDEi P50502.

    Protocols and materials databases

    DNASUi 6767.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216218 ; ENSP00000216218 ; ENSG00000100380 .
    GeneIDi 6767.
    KEGGi hsa:6767.
    UCSCi uc003aze.3. human.

    Organism-specific databases

    CTDi 6767.
    GeneCardsi GC22M041220.
    HGNCi HGNC:11343. ST13.
    HPAi HPA043233.
    HPA046412.
    HPA047114.
    HPA047116.
    MIMi 606796. gene.
    neXtProti NX_P50502.
    PharmGKBi PA36167.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260098.
    HOGENOMi HOG000001586.
    HOVERGENi HBG002482.
    InParanoidi P50502.
    KOi K09560.
    OMAi QANEKKM.
    OrthoDBi EOG77M8P3.
    PhylomeDBi P50502.
    TreeFami TF313244.

    Miscellaneous databases

    ChiTaRSi ST13. human.
    GeneWikii ST13.
    GenomeRNAii 6767.
    NextBioi 26408.
    PMAP-CutDB P50502.
    PROi P50502.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50502.
    Bgeei P50502.
    CleanExi HS_ST13.
    Genevestigatori P50502.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR006636. STI1_HS-bd.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 2 hits.
    [Graphical view ]
    SMARTi SM00727. STI1. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein."
      Prapapanich V., Chen S., Nair S.C., Rimerman R.A., Smith D.F.
      Mol. Endocrinol. 10:420-431(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa."
      Mo Y., Zheng S., Shen D.
      Zhonghua Zhong Liu Za Zhi 18:241-243(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon mucosa.
    3. "Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening."
      Cao J., Cai X., Zheng L., Geng L., Shi Z., Pao C.C., Zheng S.
      J. Cancer Res. Clin. Oncol. 123:447-451(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon mucosa.
    4. "Identification of human aging-associated gene."
      Kim J.W.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin and Testis.
    9. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 119-142; 147-153; 174-186 AND 211-222, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "G protein-coupled receptor kinase 5 phosphorylation of Hip regulates internalization of the chemokine receptor CXCR4."
      Barker B.L., Benovic J.L.
      Biochemistry 50:6933-6941(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-346, INTERACTION WITH GRK5.

    Entry informationi

    Entry nameiF10A1_HUMAN
    AccessioniPrimary (citable) accession number: P50502
    Secondary accession number(s): O14999, Q2TU77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3