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P34931

- HS71L_HUMAN

UniProt

P34931 - HS71L_HUMAN

Protein

Heat shock 70 kDa protein 1-like

Gene

HSPA1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      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 By similarity. Positive regulator of PARK2 translocation to damaged mitochondria.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 174ATP
    Nucleotide bindingi204 – 2063ATP
    Nucleotide bindingi270 – 2778ATP
    Nucleotide bindingi341 – 3444ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. unfolded protein binding Source: UniProt

    GO - Biological processi

    1. binding of sperm to zona pellucida Source: Ensembl
    2. protein refolding Source: UniProt
    3. response to unfolded protein Source: ProtInc

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock 70 kDa protein 1-like
    Short name:
    Heat shock 70 kDa protein 1L
    Alternative name(s):
    Heat shock 70 kDa protein 1-Hom
    Short name:
    HSP70-Hom
    Gene namesi
    Name:HSPA1L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5234. HSPA1L.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell body Source: Ensembl
    3. cytosol Source: UniProt
    4. mitochondrial matrix Source: Ensembl
    5. zona pellucida receptor complex Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731K → E: No rescue of PARK2 translocation deficit in knockout cells. 1 Publication
    Mutagenesisi396 – 3961L → D: No rescue of PARK2 translocation deficit in knockout cells. 1 Publication
    Mutagenesisi638 – 6414Missing: No rescue of PARK2 translocation deficit in knockout cells.

    Organism-specific databases

    PharmGKBiPA29500.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 641641Heat shock 70 kDa protein 1-likePRO_0000078255Add
    BLAST

    Proteomic databases

    MaxQBiP34931.
    PaxDbiP34931.
    PRIDEiP34931.

    2D gel databases

    UCD-2DPAGEP34931.

    PTM databases

    PhosphoSiteiP34931.

    Expressioni

    Tissue specificityi

    Expressed in spermatids.1 Publication

    Inductioni

    Not induced by heat shock.1 Publication

    Gene expression databases

    BgeeiP34931.
    CleanExiHS_HSPA1L.
    GenevestigatoriP34931.

    Organism-specific databases

    HPAiHPA043285.

    Interactioni

    Subunit structurei

    Interacts with PARK2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046372EBI-354912,EBI-366083

    Protein-protein interaction databases

    BioGridi109537. 85 interactions.
    IntActiP34931. 41 interactions.
    MINTiMINT-1136903.
    STRINGi9606.ENSP00000396486.

    Structurei

    Secondary structure

    1
    641
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124
    Beta strandi15 – 2410
    Beta strandi27 – 304
    Beta strandi38 – 414
    Beta strandi44 – 463
    Beta strandi51 – 533
    Helixi55 – 595
    Helixi60 – 634
    Helixi65 – 673
    Helixi72 – 754
    Helixi83 – 897
    Beta strandi93 – 997
    Beta strandi102 – 1098
    Beta strandi112 – 1165
    Helixi118 – 13720
    Beta strandi143 – 1486
    Helixi154 – 16613
    Beta strandi170 – 1767
    Helixi177 – 1848
    Turni185 – 1884
    Beta strandi195 – 2028
    Beta strandi207 – 2159
    Beta strandi218 – 22710
    Helixi232 – 25120
    Helixi255 – 2573
    Helixi259 – 27517
    Turni276 – 2783
    Beta strandi279 – 29012
    Beta strandi293 – 3008
    Helixi301 – 3077
    Helixi309 – 3146
    Helixi316 – 32510
    Helixi330 – 3323
    Beta strandi335 – 3406
    Helixi341 – 3444
    Helixi346 – 35510
    Turni356 – 3583
    Turni367 – 3693
    Helixi370 – 38314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GDQX-ray1.80A1-386[»]
    ProteinModelPortaliP34931.
    SMRiP34931. Positions 4-612.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34931.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOVERGENiHBG051845.
    InParanoidiP34931.
    KOiK03283.
    OMAiNTECESA.
    OrthoDBiEOG7PCJGF.
    PhylomeDBiP34931.
    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]

    Sequencei

    Sequence statusi: Complete.

    P34931-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE    50
    RLIGDAAKNQ VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG 100
    GKPKVLVSYK GENKAFYPEE ISSMVLTKLK ETAEAFLGHP VTNAVITVPA 150
    YFNDSQRQAT KDAGVIAGLN VLRIINEPTA AAIAYGLDKG GQGERHVLIF 200
    DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV SHFVEEFKRK 250
    HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT 300
    RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR 350
    LLQDYFNGRD LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP 400
    LSLGLETAGG VMTALIKRNS TIPTKQTQIF TTYSDNQPGV LIQVYEGERA 450
    MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF DIDANGILNV TATDKSTGKV 500
    NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA KNALESYAFN 550
    MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE 600
    LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D 641
    Length:641
    Mass (Da):70,375
    Last modified:October 10, 2002 - v2
    Checksum:iA9339D7657166FF7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti408 – 4081A → V in AAA63228. (PubMed:1700760)Curated
    Sequence conflicti416 – 4161I → M in AAH34483. (PubMed:15489334)Curated
    Sequence conflicti424 – 4241T → P in AAA63228. (PubMed:1700760)Curated
    Sequence conflicti506 – 5061T → A in AAH34483. (PubMed:15489334)Curated
    Sequence conflicti627 – 6271V → M in BAA32521. (PubMed:9685725)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81A → P.1 Publication
    Corresponds to variant rs9469057 [ dbSNP | Ensembl ].
    VAR_025841
    Natural varianti268 – 2681A → T.1 Publication
    Corresponds to variant rs34620296 [ dbSNP | Ensembl ].
    VAR_025842
    Natural varianti294 – 2941D → G.1 Publication
    Corresponds to variant rs34360259 [ dbSNP | Ensembl ].
    VAR_025843
    Natural varianti479 – 4791T → M.1 Publication
    Corresponds to variant rs482145 [ dbSNP | Ensembl ].
    VAR_025844
    Natural varianti493 – 4931T → M.4 Publications
    Corresponds to variant rs2227956 [ dbSNP | Ensembl ].
    VAR_003820
    Natural varianti558 – 5581E → A.1 Publication
    Corresponds to variant rs2227955 [ dbSNP | Ensembl ].
    VAR_025845
    Natural varianti602 – 6021E → K.1 Publication
    Corresponds to variant rs2075800 [ dbSNP | Ensembl ].
    VAR_025846

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59829 Genomic DNA. Translation: AAA63228.1.
    D85730 mRNA. Translation: BAA32521.1.
    AF134726 Genomic DNA. Translation: AAD21817.1.
    BA000025 Genomic DNA. Translation: BAB63301.1.
    DQ383515 Genomic DNA. Translation: ABC88476.1.
    AL662834 Genomic DNA. Translation: CAI17736.1.
    AL671762 Genomic DNA. Translation: CAI18215.1.
    AL929592 Genomic DNA. Translation: CAI18463.1.
    CR388202 Genomic DNA. Translation: CAQ09503.1.
    BC034483 mRNA. Translation: AAH34483.1.
    CCDSiCCDS34413.1.
    PIRiB45871.
    RefSeqiNP_005518.3. NM_005527.3.
    XP_005249128.1. XM_005249071.1.
    XP_005249130.1. XM_005249073.1.
    XP_005272873.1. XM_005272816.1.
    XP_005272874.1. XM_005272817.1.
    XP_005275030.1. XM_005274973.1.
    XP_005275031.1. XM_005274974.1.
    XP_005275458.1. XM_005275401.1.
    XP_005275459.1. XM_005275402.1.
    UniGeneiHs.690634.

    Genome annotation databases

    EnsembliENST00000375654; ENSP00000364805; ENSG00000204390.
    ENST00000383390; ENSP00000372881; ENSG00000206383.
    ENST00000417601; ENSP00000396486; ENSG00000234258.
    ENST00000456772; ENSP00000408347; ENSG00000236251.
    GeneIDi3305.
    KEGGihsa:3305.
    UCSCiuc003nxh.3. human.

    Polymorphism databases

    DMDMi23831140.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59829 Genomic DNA. Translation: AAA63228.1 .
    D85730 mRNA. Translation: BAA32521.1 .
    AF134726 Genomic DNA. Translation: AAD21817.1 .
    BA000025 Genomic DNA. Translation: BAB63301.1 .
    DQ383515 Genomic DNA. Translation: ABC88476.1 .
    AL662834 Genomic DNA. Translation: CAI17736.1 .
    AL671762 Genomic DNA. Translation: CAI18215.1 .
    AL929592 Genomic DNA. Translation: CAI18463.1 .
    CR388202 Genomic DNA. Translation: CAQ09503.1 .
    BC034483 mRNA. Translation: AAH34483.1 .
    CCDSi CCDS34413.1.
    PIRi B45871.
    RefSeqi NP_005518.3. NM_005527.3.
    XP_005249128.1. XM_005249071.1.
    XP_005249130.1. XM_005249073.1.
    XP_005272873.1. XM_005272816.1.
    XP_005272874.1. XM_005272817.1.
    XP_005275030.1. XM_005274973.1.
    XP_005275031.1. XM_005274974.1.
    XP_005275458.1. XM_005275401.1.
    XP_005275459.1. XM_005275402.1.
    UniGenei Hs.690634.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GDQ X-ray 1.80 A 1-386 [» ]
    ProteinModelPortali P34931.
    SMRi P34931. Positions 4-612.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109537. 85 interactions.
    IntActi P34931. 41 interactions.
    MINTi MINT-1136903.
    STRINGi 9606.ENSP00000396486.

    PTM databases

    PhosphoSitei P34931.

    Polymorphism databases

    DMDMi 23831140.

    2D gel databases

    UCD-2DPAGE P34931.

    Proteomic databases

    MaxQBi P34931.
    PaxDbi P34931.
    PRIDEi P34931.

    Protocols and materials databases

    DNASUi 3305.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375654 ; ENSP00000364805 ; ENSG00000204390 .
    ENST00000383390 ; ENSP00000372881 ; ENSG00000206383 .
    ENST00000417601 ; ENSP00000396486 ; ENSG00000234258 .
    ENST00000456772 ; ENSP00000408347 ; ENSG00000236251 .
    GeneIDi 3305.
    KEGGi hsa:3305.
    UCSCi uc003nxh.3. human.

    Organism-specific databases

    CTDi 3305.
    GeneCardsi GC06M031777.
    GC06Mj31764.
    GC06Mk31759.
    GC06Mn31767.
    H-InvDB HIX0165969.
    HIX0166127.
    HIX0166446.
    HIX0167182.
    HIX0184230.
    HGNCi HGNC:5234. HSPA1L.
    HPAi HPA043285.
    MIMi 140559. gene.
    neXtProti NX_P34931.
    PharmGKBi PA29500.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOVERGENi HBG051845.
    InParanoidi P34931.
    KOi K03283.
    OMAi NTECESA.
    OrthoDBi EOG7PCJGF.
    PhylomeDBi P34931.
    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.

    Miscellaneous databases

    EvolutionaryTracei P34931.
    GeneWikii HSPA1L.
    GenomeRNAii 3305.
    NextBioi 13111.
    PROi P34931.
    SOURCEi Search...

    Gene expression databases

    Bgeei P34931.
    CleanExi HS_HSPA1L.
    Genevestigatori P34931.

    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], INDUCTION.
    2. "Genomic structure of the spermatid-specific HSP70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man."
      Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.
      J. Biochem. 124:347-353(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Tissue: Testis.
    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].
    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].
    5. NIEHS SNPs program
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-8; THR-268; GLY-294; MET-479; MET-493; ALA-558 AND LYS-602.
    6. "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 MET-493.
    7. "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], VARIANT MET-493.
      Tissue: Testis.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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: FUNCTION IN PARK2 TRANSLOCATION, INTERACTION WITH PARK2, MUTAGENESIS OF LYS-73; LEU-396 AND 638-GLU--ASP-641.
    10. "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 (1.80 ANGSTROMS) OF 2-386 IN COMPLEX WITH ADP AND PHOSPHATE.
    11. "Polymorphic analysis of the three MHC-linked HSP70 genes."
      Milner C.M., Campbell R.D.
      Immunogenetics 36:357-362(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MET-493.

    Entry informationi

    Entry nameiHS71L_HUMAN
    AccessioniPrimary (citable) accession number: P34931
    Secondary accession number(s): A6NNB0
    , B0UXW8, O75634, Q2HXR3, Q8NE72, Q96QC9, Q9UQM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 136 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, 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

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