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P08107

- HSP71_HUMAN

UniProt

P08107 - HSP71_HUMAN

Protein

Heat shock 70 kDa protein 1A/1B

Gene

HSPA1A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 5 (15 May 2007)
      Previous versions | rss
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    Functioni

    In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154ATP
    Nucleotide bindingi202 – 2043ATP
    Nucleotide bindingi268 – 2758ATP
    Nucleotide bindingi339 – 3424ATP

    GO - Molecular functioni

    1. ATPase activity Source: BHF-UCL
    2. ATPase activity, coupled Source: UniProt
    3. ATP binding Source: BHF-UCL
    4. double-stranded RNA binding Source: MGI
    5. enzyme binding Source: BHF-UCL
    6. heat shock protein binding Source: BHF-UCL
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein binding involved in protein folding Source: BHF-UCL
    10. protein N-terminus binding Source: UniProtKB
    11. ubiquitin protein ligase binding Source: BHF-UCL
    12. unfolded protein binding Source: UniProtKB
    13. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. ATP catabolic process Source: BHF-UCL
    2. cellular heat acclimation Source: UniProt
    3. cellular response to heat Source: UniProt
    4. gene expression Source: Reactome
    5. mRNA catabolic process Source: UniProtKB
    6. mRNA metabolic process Source: Reactome
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of cell death Source: UniProt
    9. negative regulation of cell growth Source: UniProtKB
    10. negative regulation of cell proliferation Source: UniProtKB
    11. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    12. negative regulation of inclusion body assembly Source: BHF-UCL
    13. positive regulation of erythrocyte differentiation Source: UniProtKB
    14. protein refolding Source: BHF-UCL
    15. response to unfolded protein Source: UniProtKB
    16. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Chaperone, Host cell receptor for virus entry, Receptor

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.

    Protein family/group databases

    TCDBi1.A.33.1.3. the cation channel-forming heat shock protein-70 (hsp70) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock 70 kDa protein 1A/1B
    Alternative name(s):
    Heat shock 70 kDa protein 1/2
    Short name:
    HSP70-1/HSP70-2
    Short name:
    HSP70.1/HSP70.2
    Gene namesi
    Name:HSPA1A
    Synonyms:HSPA1, HSX70
    AND
    Name:HSPA1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5232. HSPA1A.
    HGNC:5233. HSPA1B.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. aggresome Source: UniProtKB
    2. blood microparticle Source: UniProt
    3. centriole Source: UniProt
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: UniProt
    6. endoplasmic reticulum Source: UniProtKB
    7. extracellular vesicular exosome Source: UniProt
    8. inclusion body Source: BHF-UCL
    9. mitochondrion Source: UniProtKB
    10. nuclear speck Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. perinuclear region of cytoplasm Source: UniProtKB
    13. ribonucleoprotein complex Source: UniProtKB
    14. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101D → A: Reduces affinity for ADP. 1 Publication
    Mutagenesisi199 – 1991D → A: Reduces affinity for ADP. 1 Publication
    Mutagenesisi561 – 5611K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

    Organism-specific databases

    PharmGKBiPA29499.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 641640Heat shock 70 kDa protein 1A/1BPRO_0000078249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei108 – 1081N6-acetyllysine1 Publication
    Modified residuei246 – 2461N6-acetyllysine1 Publication
    Modified residuei348 – 3481N6-acetyllysine1 Publication
    Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A2 Publications
    Modified residuei631 – 6311Phosphoserine1 Publication
    Modified residuei633 – 6331Phosphoserine1 Publication
    Modified residuei636 – 6361Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP08107.
    PaxDbiP08107.
    PRIDEiP08107.

    2D gel databases

    DOSAC-COBS-2DPAGEP08107.
    OGPiP08107.
    REPRODUCTION-2DPAGEIPI00304925.
    SWISS-2DPAGEP08107.
    UCD-2DPAGEP08107.

    PTM databases

    PhosphoSiteiP08107.

    Expressioni

    Tissue specificityi

    HSPA1B is testis-specific.

    Inductioni

    By heat shock.

    Gene expression databases

    ArrayExpressiP08107.
    BgeeiP08107.
    CleanExiHS_HSPA1A.
    GenevestigatoriP08107.

    Organism-specific databases

    HPAiCAB008640.
    CAB017451.
    CAB032815.
    HPA052504.

    Interactioni

    Subunit structurei

    Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts with METTL21A. Interacts with PARK2.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P298463EBI-629985,EBI-9303040From a different organism.
    BAG5Q9UL156EBI-629985,EBI-356517
    BCL2L12Q9HB09-22EBI-629985,EBI-6969019
    EBNA-LPQ8AZK73EBI-629985,EBI-1185167From a different organism.
    EGFRP005335EBI-629985,EBI-297353
    GATA1P159765EBI-629985,EBI-3909284
    LoxP283016EBI-629985,EBI-642911From a different organism.
    MMEP084733EBI-629985,EBI-353759
    Phlda1Q623922EBI-629985,EBI-309727From a different organism.
    PLK1P533505EBI-629985,EBI-476768
    S100a1P354674EBI-629985,EBI-6477109From a different organism.
    SNCAP378407EBI-629985,EBI-985879
    SSE1P325892EBI-629985,EBI-8648From a different organism.
    STUB1Q9UNE75EBI-629985,EBI-357085

    Protein-protein interaction databases

    BioGridi109535. 148 interactions.
    109536. 52 interactions.
    DIPiDIP-211N.
    IntActiP08107. 115 interactions.
    MINTiMINT-96699.
    STRINGi9606.ENSP00000364802.

    Structurei

    Secondary structure

    1
    641
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi13 – 2210
    Beta strandi25 – 284
    Beta strandi36 – 394
    Beta strandi42 – 443
    Beta strandi49 – 513
    Helixi53 – 564
    Turni57 – 615
    Helixi63 – 653
    Helixi70 – 734
    Helixi81 – 877
    Beta strandi91 – 977
    Beta strandi100 – 1078
    Beta strandi110 – 1145
    Helixi116 – 13520
    Beta strandi141 – 1466
    Helixi152 – 16413
    Beta strandi168 – 1747
    Helixi175 – 1828
    Turni183 – 1864
    Beta strandi190 – 20011
    Beta strandi205 – 2139
    Beta strandi216 – 22510
    Helixi226 – 2283
    Helixi230 – 24920
    Helixi253 – 2553
    Helixi257 – 27317
    Turni274 – 2763
    Beta strandi277 – 28812
    Beta strandi291 – 2988
    Helixi299 – 3057
    Helixi307 – 3115
    Helixi314 – 32310
    Helixi328 – 3303
    Beta strandi333 – 3386
    Helixi339 – 3424
    Helixi344 – 35310
    Turni354 – 3563
    Turni365 – 3673
    Helixi368 – 38114
    Helixi534 – 55320
    Helixi556 – 5583
    Helixi564 – 58320
    Helixi589 – 61224

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HJOX-ray2.30A3-382[»]
    1S3XX-ray1.84A1-382[»]
    1XQSX-ray2.90C/D184-371[»]
    2E88X-ray1.80A1-388[»]
    2E8AX-ray1.77A1-388[»]
    2LMGNMR-A537-610[»]
    3A8YX-ray2.30A/B1-388[»]
    3ATUX-ray1.65A1-388[»]
    3ATVX-ray1.58A1-388[»]
    3AY9X-ray1.75A1-388[»]
    3D2EX-ray2.35B/D1-382[»]
    3D2FX-ray2.30B/D1-382[»]
    3JXUX-ray2.14A1-387[»]
    3LOFX-ray2.40A/B/C/D/E/F534-641[»]
    4IO8X-ray2.58A1-382[»]
    4J8FX-ray2.70A1-382[»]
    ProteinModelPortaliP08107.
    SMRiP08107. Positions 1-613.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08107.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP08107.
    KOiK03283.
    OMAiIRSSARC.
    OrthoDBiEOG7PCJGF.
    PhylomeDBiP08107.
    TreeFamiTF105042.

    Family and domain databases

    Gene3Di1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProiIPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view]
    PfamiPF00012. HSP70. 1 hit.
    [Graphical view]
    PRINTSiPR00301. HEATSHOCK70.
    SUPFAMiSSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08107-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL    50
    IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK 100
    PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF 150
    NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL 200
    GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK 250
    KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 300
    RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL 350
    QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS 400
    LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT 450
    KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK 500
    ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK 550
    SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE 600
    QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D 641
    Length:641
    Mass (Da):70,052
    Last modified:May 15, 2007 - v5
    Checksum:i78F513118C96DE66
    GO
    Isoform 2 (identifier: P08107-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         96-150: Missing.

    Show »
    Length:586
    Mass (Da):63,937
    Checksum:i6FBA863FEACE9DF1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71I → V in AAA52697. (PubMed:3931075)Curated
    Sequence conflicti7 – 71I → V in CAA28381. (PubMed:3786141)Curated
    Sequence conflicti355 – 3551N → D in BAG65428. (PubMed:14702039)Curated
    Sequence conflicti370 – 3701A → G in AAA52697. (PubMed:3931075)Curated
    Sequence conflicti469 – 4691Missing in AAA52697. (PubMed:3931075)Curated
    Sequence conflicti497 – 4971K → N in BAG65428. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951I → V.1 Publication
    VAR_032152
    Natural varianti110 – 1101E → D.3 Publications
    Corresponds to variant rs562047 [ dbSNP | Ensembl ].
    VAR_029053
    Natural varianti467 – 4671A → V.1 Publication
    VAR_032153
    Natural varianti499 – 4991N → S.2 Publications
    Corresponds to variant rs483638 [ dbSNP | Ensembl ].
    VAR_029054

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei96 – 15055Missing in isoform 2. 1 PublicationVSP_044427Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59828 Genomic DNA. Translation: AAA63226.1.
    M59830 Genomic DNA. Translation: AAA63227.1.
    M11717 Genomic DNA. Translation: AAA52697.1.
    AF134726 Genomic DNA. Translation: AAD21815.1.
    AF134726 Genomic DNA. Translation: AAD21816.1.
    BA000025 Genomic DNA. Translation: BAB63299.1.
    BA000025 Genomic DNA. Translation: BAB63300.1.
    AK304652 mRNA. Translation: BAG65428.1.
    DQ388429 Genomic DNA. Translation: ABD48956.1.
    DQ451402 Genomic DNA. Translation: ABD96830.1.
    AL662834 Genomic DNA. Translation: CAI17737.1.
    AL662834 Genomic DNA. Translation: CAI17738.1.
    AL671762 Genomic DNA. Translation: CAI18216.1.
    AL671762 Genomic DNA. Translation: CAI18217.1.
    AL929592 Genomic DNA. Translation: CAI18464.1.
    AL929592 Genomic DNA. Translation: CAI18466.1.
    BC002453 mRNA. Translation: AAH02453.1.
    BC009322 mRNA. Translation: AAH09322.1.
    BC018740 mRNA. Translation: AAH18740.1.
    BC057397 mRNA. Translation: AAH57397.1.
    BC063507 mRNA. Translation: AAH63507.1.
    M24743 Genomic DNA. Translation: AAA59844.1.
    M24744 Genomic DNA. Translation: AAA59845.1.
    X04676 Genomic DNA. Translation: CAA28381.1.
    X04677 Genomic DNA. Translation: CAA28382.1.
    CCDSiCCDS34414.1. [P08107-1]
    CCDS34415.1. [P08107-1]
    PIRiA29160.
    A45871.
    I59139.
    I79540.
    RefSeqiNP_005336.3. NM_005345.5. [P08107-1]
    NP_005337.2. NM_005346.4. [P08107-1]
    UniGeneiHs.274402.
    Hs.702139.
    Hs.719966.

    Genome annotation databases

    EnsembliENST00000375650; ENSP00000364801; ENSG00000204388. [P08107-1]
    ENST00000375651; ENSP00000364802; ENSG00000204389. [P08107-1]
    ENST00000391548; ENSP00000375391; ENSG00000224501. [P08107-1]
    ENST00000391555; ENSP00000375399; ENSG00000212866. [P08107-1]
    ENST00000400040; ENSP00000382915; ENSG00000215328.
    ENST00000430065; ENSP00000404524; ENSG00000235941. [P08107-1]
    ENST00000433487; ENSP00000408907; ENSG00000234475. [P08107-1]
    ENST00000441618; ENSP00000406359; ENSG00000237724. [P08107-1]
    ENST00000445736; ENSP00000403530; ENSG00000231555. [P08107-1]
    ENST00000450744; ENSP00000393087; ENSG00000232804. [P08107-1]
    GeneIDi3303.
    3304.
    KEGGihsa:3303.
    hsa:3304.
    UCSCiuc003nxj.3. human. [P08107-1]

    Polymorphism databases

    DMDMi147744565.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59828 Genomic DNA. Translation: AAA63226.1 .
    M59830 Genomic DNA. Translation: AAA63227.1 .
    M11717 Genomic DNA. Translation: AAA52697.1 .
    AF134726 Genomic DNA. Translation: AAD21815.1 .
    AF134726 Genomic DNA. Translation: AAD21816.1 .
    BA000025 Genomic DNA. Translation: BAB63299.1 .
    BA000025 Genomic DNA. Translation: BAB63300.1 .
    AK304652 mRNA. Translation: BAG65428.1 .
    DQ388429 Genomic DNA. Translation: ABD48956.1 .
    DQ451402 Genomic DNA. Translation: ABD96830.1 .
    AL662834 Genomic DNA. Translation: CAI17737.1 .
    AL662834 Genomic DNA. Translation: CAI17738.1 .
    AL671762 Genomic DNA. Translation: CAI18216.1 .
    AL671762 Genomic DNA. Translation: CAI18217.1 .
    AL929592 Genomic DNA. Translation: CAI18464.1 .
    AL929592 Genomic DNA. Translation: CAI18466.1 .
    BC002453 mRNA. Translation: AAH02453.1 .
    BC009322 mRNA. Translation: AAH09322.1 .
    BC018740 mRNA. Translation: AAH18740.1 .
    BC057397 mRNA. Translation: AAH57397.1 .
    BC063507 mRNA. Translation: AAH63507.1 .
    M24743 Genomic DNA. Translation: AAA59844.1 .
    M24744 Genomic DNA. Translation: AAA59845.1 .
    X04676 Genomic DNA. Translation: CAA28381.1 .
    X04677 Genomic DNA. Translation: CAA28382.1 .
    CCDSi CCDS34414.1. [P08107-1 ]
    CCDS34415.1. [P08107-1 ]
    PIRi A29160.
    A45871.
    I59139.
    I79540.
    RefSeqi NP_005336.3. NM_005345.5. [P08107-1 ]
    NP_005337.2. NM_005346.4. [P08107-1 ]
    UniGenei Hs.274402.
    Hs.702139.
    Hs.719966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HJO X-ray 2.30 A 3-382 [» ]
    1S3X X-ray 1.84 A 1-382 [» ]
    1XQS X-ray 2.90 C/D 184-371 [» ]
    2E88 X-ray 1.80 A 1-388 [» ]
    2E8A X-ray 1.77 A 1-388 [» ]
    2LMG NMR - A 537-610 [» ]
    3A8Y X-ray 2.30 A/B 1-388 [» ]
    3ATU X-ray 1.65 A 1-388 [» ]
    3ATV X-ray 1.58 A 1-388 [» ]
    3AY9 X-ray 1.75 A 1-388 [» ]
    3D2E X-ray 2.35 B/D 1-382 [» ]
    3D2F X-ray 2.30 B/D 1-382 [» ]
    3JXU X-ray 2.14 A 1-387 [» ]
    3LOF X-ray 2.40 A/B/C/D/E/F 534-641 [» ]
    4IO8 X-ray 2.58 A 1-382 [» ]
    4J8F X-ray 2.70 A 1-382 [» ]
    ProteinModelPortali P08107.
    SMRi P08107. Positions 1-613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109535. 148 interactions.
    109536. 52 interactions.
    DIPi DIP-211N.
    IntActi P08107. 115 interactions.
    MINTi MINT-96699.
    STRINGi 9606.ENSP00000364802.

    Chemistry

    BindingDBi P08107.
    ChEMBLi CHEMBL5460.

    Protein family/group databases

    TCDBi 1.A.33.1.3. the cation channel-forming heat shock protein-70 (hsp70) family.

    PTM databases

    PhosphoSitei P08107.

    Polymorphism databases

    DMDMi 147744565.

    2D gel databases

    DOSAC-COBS-2DPAGE P08107.
    OGPi P08107.
    REPRODUCTION-2DPAGE IPI00304925.
    SWISS-2DPAGE P08107.
    UCD-2DPAGE P08107.

    Proteomic databases

    MaxQBi P08107.
    PaxDbi P08107.
    PRIDEi P08107.

    Protocols and materials databases

    DNASUi 3303.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375650 ; ENSP00000364801 ; ENSG00000204388 . [P08107-1 ]
    ENST00000375651 ; ENSP00000364802 ; ENSG00000204389 . [P08107-1 ]
    ENST00000391548 ; ENSP00000375391 ; ENSG00000224501 . [P08107-1 ]
    ENST00000391555 ; ENSP00000375399 ; ENSG00000212866 . [P08107-1 ]
    ENST00000400040 ; ENSP00000382915 ; ENSG00000215328 .
    ENST00000430065 ; ENSP00000404524 ; ENSG00000235941 . [P08107-1 ]
    ENST00000433487 ; ENSP00000408907 ; ENSG00000234475 . [P08107-1 ]
    ENST00000441618 ; ENSP00000406359 ; ENSG00000237724 . [P08107-1 ]
    ENST00000445736 ; ENSP00000403530 ; ENSG00000231555 . [P08107-1 ]
    ENST00000450744 ; ENSP00000393087 ; ENSG00000232804 . [P08107-1 ]
    GeneIDi 3303.
    3304.
    KEGGi hsa:3303.
    hsa:3304.
    UCSCi uc003nxj.3. human. [P08107-1 ]

    Organism-specific databases

    CTDi 3303.
    3304.
    GeneCardsi GC06P031823.
    GC06P031824.
    GC06Pi31794.
    GC06Pi31806.
    GC06Pj31770.
    GC06Pj31782.
    GC06Pk31765.
    GC06Pk31777.
    GC06Pn31773.
    GC06Pn31785.
    H-InvDB HIX0058169.
    HIX0058187.
    HIX0166160.
    HGNCi HGNC:5232. HSPA1A.
    HGNC:5233. HSPA1B.
    HPAi CAB008640.
    CAB017451.
    CAB032815.
    HPA052504.
    MIMi 140550. gene.
    603012. gene.
    neXtProti NX_P08107.
    PharmGKBi PA29499.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P08107.
    KOi K03283.
    OMAi IRSSARC.
    OrthoDBi EOG7PCJGF.
    PhylomeDBi P08107.
    TreeFami TF105042.

    Enzyme and pathway databases

    Reactomei REACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.

    Miscellaneous databases

    ChiTaRSi HSPA1A. human.
    EvolutionaryTracei P08107.
    GeneWikii HSPA1A.
    NextBioi 13103.
    PROi P08107.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08107.
    Bgeei P08107.
    CleanExi HS_HSPA1A.
    Genevestigatori P08107.

    Family and domain databases

    Gene3Di 1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProi IPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view ]
    Pfami PF00012. HSP70. 1 hit.
    [Graphical view ]
    PRINTSi PR00301. HEATSHOCK70.
    SUPFAMi SSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the three MHC-linked HSP70 genes."
      Milner C.M., Campbell R.D.
      Immunogenetics 32:242-251(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70."
      Hunt C., Morimoto R.I.
      Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B), VARIANTS ASP-110 AND SER-499.
    4. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Uterus.
    6. NIEHS SNPs program
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-95; ASP-110; VAL-467 AND SER-499.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110.
    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] (ISOFORM 1).
      Tissue: Brain, Muscle, Pancreas, PNS and Skin.
    9. "Human major histocompatibility complex contains genes for the major heat shock protein HSP70."
      Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.
      Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36 AND 360-424.
    10. "In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells."
      Drabent B., Genthe A., Benecke B.-J.
      Nucleic Acids Res. 14:8933-8948(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
    11. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-155; 160-187; 221-247; 273-311; 326-342; 349-357; 362-416; 424-447; 459-469; 510-517; 540-550; 574-595 AND 598-641, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    12. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 37-49; 57-71; 78-88; 113-126; 160-187; 221-247; 302-311; 329-342; 349-357; 362-384; 540-550 AND 574-589, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    13. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
      Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
      J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TERT.
    15. "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
      Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
      EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC7.
    16. Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
      Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
      Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, IDENTIFICATION BY MASS SPECTROMETRY.
    18. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family."
      Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.
      DNA Cell Biol. 25:704-714(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK1BP1, IDENTIFICATION BY MASS SPECTROMETRY.
    20. "The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity."
      Perez-Vargas J., Romero P., Lopez S., Arias C.F.
      J. Virol. 80:3322-3331(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
    21. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    22. Cited for: INTERACTION WITH DNAJC7.
    23. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
      Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
      J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5.
    27. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-633 AND THR-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function."
      Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S.
      J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHCHD3.
    30. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
      Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
      J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, INTERACTION WITH METTL21A.
    31. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
      Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
      Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARK2.
    32. "Structure of a new crystal form of human hsp70 ATPase domain."
      Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.
      Acta Crystallogr. D 55:1105-1107(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP, ATP-BINDING.
    33. "Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state."
      Shida M., Arakawa A., Ishii R., Kishishita S., Takagi T., Kukimoto-Niino M., Sugano S., Tanaka A., Shirouzu M., Yokoyama S.
      Acta Crystallogr. D 66:223-232(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 389-641 IN COMPLEX WITH ATP ANALOG, ATP-BINDING.
    34. "Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
      Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
      PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP, ATP-BINDING.
    35. "The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange."
      Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F., Shirouzu M., Yokoyama S.
      Structure 18:309-319(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
    36. "Biochemical and structural studies on the high affinity of Hsp70 for ADP."
      Arakawa A., Handa N., Shirouzu M., Yokoyama S.
      Protein Sci. 20:1367-1379(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-388, ATP-BINDING, MUTAGENESIS OF ASP-10 AND ASP-199.

    Entry informationi

    Entry nameiHSP71_HUMAN
    AccessioniPrimary (citable) accession number: P08107
    Secondary accession number(s): B4E3B6
    , P19790, Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 184 of the entry and version 5 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 6
      Human chromosome 6: 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