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P11142 (HSP7C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Lipopolysaccharide-associated protein 1
Short name=LAP-1
Short name=LPS-associated protein 1
Gene names
Name:HSPA8
Synonyms:HSC70, HSP73, HSPA10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Ref.15 Ref.16

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with SV40 VP1. Interacts with TRIM5. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PARK2. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.25 Ref.28 Ref.33 Ref.34

Subcellular location

Cytoplasm. Melanosome. Nucleusnucleolus. Cell membrane. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. Ref.11 Ref.16 Ref.20 Ref.22 Ref.29

Tissue specificity

Ubiquitous. Ref.16

Induction

Constitutively synthesized.

Domain

The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain. Ref.12

Post-translational modification

Acetylated. Ref.5 Ref.6

ISGylated. Ref.18 Ref.21

Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
Stress response
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.33. Source: BHF-UCL

RNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

membrane organization

Traceable author statement. Source: Reactome

negative regulation of fibril organization

Inferred from direct assay Ref.33. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.15. Source: UniProtKB

neurotransmitter secretion

Traceable author statement. Source: Reactome

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

protein folding

Non-traceable author statement PubMed 8530083. Source: UniProtKB

protein refolding

Inferred from direct assay PubMed 21231916. Source: UniProt

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Non-traceable author statement Ref.2. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPrp19 complex

Inferred from direct assay Ref.29. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Inferred from direct assay PubMed 21231916. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

intracellular

Non-traceable author statement Ref.9. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay PubMed 92266438. Source: UniProtKB

nucleus

Inferred from direct assay Ref.29. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from direct assay Ref.22. Source: UniProtKB

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from direct assay Ref.33. Source: BHF-UCL

ATPase activity

Inferred from direct assay Ref.33. Source: BHF-UCL

ATPase activity, coupled

Non-traceable author statement PubMed 8530083. Source: UniProtKB

MHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

enzyme binding

Inferred from physical interaction Ref.33. Source: BHF-UCL

heat shock protein binding

Inferred from physical interaction Ref.33. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15PubMed 10954706PubMed 16531398Ref.12. Source: UniProtKB

unfolded protein binding

Inferred from direct assay PubMed 21231916. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11142-1)

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: P11142-2)

Also known as: HSC54;

The sequence of this isoform differs from the canonical sequence as follows:
     464-616: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 646645Heat shock cognate 71 kDa protein
PRO_0000078270

Regions

Nucleotide binding12 – 154ATP
Nucleotide binding202 – 2043ATP
Nucleotide binding268 – 2758ATP
Nucleotide binding339 – 3424ATP
Region186 – 377192Interaction with BAG1

Sites

Binding site711ATP

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.6 Ref.24
Modified residue1081N6-acetyllysine By similarity
Modified residue1531Phosphoserine Ref.23
Modified residue2461N6-acetyllysine Ref.27
Modified residue3191N6-acetyllysine; alternate Ref.27
Modified residue3191N6-succinyllysine; alternate By similarity
Modified residue3281N6-acetyllysine By similarity
Modified residue3621Phosphoserine Ref.30
Modified residue5121N6-acetyllysine; alternate By similarity
Modified residue5121N6-succinyllysine; alternate By similarity
Modified residue5241N6-acetyllysine By similarity
Modified residue5611N6,N6,N6-trimethyllysine; by METTL21A Ref.10 Ref.33
Modified residue5891N6-acetyllysine Ref.27
Modified residue5971N6-acetyllysine Ref.27
Modified residue6011N6-acetyllysine Ref.27

Natural variations

Alternative sequence464 – 616153Missing in isoform 2.
VSP_002427
Natural variant321D → Y.
Corresponds to variant rs11551602 [ dbSNP | Ensembl ].
VAR_049619
Natural variant4591F → L.
Corresponds to variant rs11551598 [ dbSNP | Ensembl ].
VAR_049620

Experimental info

Mutagenesis5611K → R: Complete loss of in vitro methylation by METTL21A. Ref.10 Ref.33

Secondary structure

.......................................................................... 646
Helix Strand Turn

Details...

Sequences

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

Last modified July 1, 1989. Version 1.
Checksum: 9AA27B210730670C

FASTA64670,898
        10         20         30         40         50         60 
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 

        70         80         90        100        110        120 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 

       130        140        150        160        170        180 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 

       190        200        210        220        230        240 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 

       250        260        270        280        290        300 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 

       310        320        330        340        350        360 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 

       370        380        390        400        410        420 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 

       430        440        450        460        470        480 
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 

       490        500        510        520        530        540 
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 

       550        560        570        580        590        600 
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 

       610        620        630        640 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 

« Hide

Isoform 2 (HSC54) [UniParc].

Checksum: BA2CFBD68F17784E
Show »

FASTA49353,518

References

« Hide 'large scale' references
[1]"Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein."
Dworniczak B.P., Mirault M.-E.
Nucleic Acids Res. 15:5181-5197(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70."
Tsukahara F., Yoshioka T., Muraki T.
Mol. Pharmacol. 58:1257-1263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Complete coding sequence of human HSC70."
Niswonger M.L., Berk L.R., Srivastava P.K.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"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: Placenta and Skin.
[5]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-49; 57-71; 77-102; 103-155; 160-188; 221-247; 273-311; 326-342; 349-416; 424-447; 452-493; 510-517; 540-550; 570-597 AND 602-646, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Bilsland A.E., Keith W.N.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-49; 57-72; 78-88; 113-188; 221-247; 300-319; 326-342; 349-357; 362-384; 424-447; 452-469; 510-517; 540-550 AND 584-609, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[7]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-88; 113-126; 129-155; 160-187; 221-246; 300-311; 329-342; 362-384; 424-447; 540-550 AND 574-583, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 50-55; 103-107 AND 580-596.
[9]"Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
[10]"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.
[11]"Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."
Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.
Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"BAG-1 modulates the chaperone activity of Hsp70/Hsc70."
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C., Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.
EMBO J. 16:4887-4896(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG1, DOMAIN.
[13]"Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
Cancer Res. 58:3116-3131(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG1.
[14]"HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells."
Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.
Cell Stress Chaperones 5:132-138(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 VP1.
[15]"The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CITED1.
[16]"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[17]"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACRG.
[18]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[19]"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.
Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[21]"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HERC5, ISGYLATION.
[22]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; C11ORF30; MATR3; ZNF335; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
[26]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"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-246; LYS-319; LYS-589; LYS-597 AND LYS-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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.
[29]"Molecular architecture of the human Prp19/CDC5L complex."
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., Fischle W., Urlaub H., Luhrmann R.
Mol. Cell. Biol. 30:2105-2119(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR LOCATION.
[30]"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-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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.
[34]"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.
[35]"Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering."
Kajander T., Sachs J.N., Goldman A., Regan L.
J. Biol. Chem. 284:25364-25374(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-634.
[36]"Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design."
Williamson D.S., Borgognoni J., Clay A., Daniels Z., Dokurno P., Drysdale M.J., Foloppe N., Francis G.L., Graham C.J., Howes R., Macias A.T., Murray J.B., Parsons R., Shaw T., Surgenor A.E., Terry L., Wang Y., Wood M., Massey A.J.
J. Med. Chem. 52:1510-1513(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP AND ATP ANALOGS.
[37]"Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity."
Macias A.T., Williamson D.S., Allen N., Borgognoni J., Clay A., Daniels Z., Dokurno P., Drysdale M.J., Francis G.L., Graham C.J., Howes R., Matassova N., Murray J.B., Parsons R., Shaw T., Surgenor A.E., Terry L., Wang Y., Wood M., Massey A.J.
J. Med. Chem. 54:4034-4041(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP ANALOGS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00371 Genomic DNA. Translation: CAA68445.1.
AB034951 mRNA. Translation: BAB18615.1.
AF352832 mRNA. Translation: AAK17898.1.
BC016179 mRNA. Translation: AAH16179.1.
BC016660 mRNA. Translation: AAH16660.1.
BC019816 mRNA. Translation: AAH19816.1.
CCDSCCDS44754.1. [P11142-2]
CCDS8440.1. [P11142-1]
PIRA27077.
RefSeqNP_006588.1. NM_006597.5. [P11142-1]
NP_694881.1. NM_153201.3. [P11142-2]
XP_006718894.1. XM_006718831.1. [P11142-1]
UniGeneHs.180414.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AGYX-ray1.85C/D/F639-646[»]
3AGZX-ray2.51C/D/E/F639-646[»]
3ESKX-ray2.05B635-646[»]
3FZFX-ray2.20A4-381[»]
3FZHX-ray2.00A4-381[»]
3FZKX-ray2.10A4-381[»]
3FZLX-ray2.20A4-381[»]
3FZMX-ray2.30A4-381[»]
3LDQX-ray1.90A4-381[»]
3M3ZX-ray2.10A4-381[»]
4H5NX-ray1.86A/B2-384[»]
4H5RX-ray1.64A/B2-384[»]
4H5TX-ray1.90A2-384[»]
4H5VX-ray1.75A2-384[»]
4H5WX-ray1.94A/B2-384[»]
4HWIX-ray2.27A5-381[»]
ProteinModelPortalP11142.
SMRP11142. Positions 1-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109544. 283 interactions.
IntActP11142. 86 interactions.
MINTMINT-4998609.
STRING9606.ENSP00000227378.

Chemistry

BindingDBP11142.
ChEMBLCHEMBL1275223.

PTM databases

PhosphoSiteP11142.

Polymorphism databases

DMDM123648.

2D gel databases

DOSAC-COBS-2DPAGEP11142.
OGPP11142.
REPRODUCTION-2DPAGEIPI00003865.
SWISS-2DPAGEP11142.
UCD-2DPAGEP11142.

Proteomic databases

MaxQBP11142.
PaxDbP11142.
PeptideAtlasP11142.
PRIDEP11142.

Protocols and materials databases

DNASU3312.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]
ENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]
ENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]
ENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]
GeneID3312.
KEGGhsa:3312.
UCSCuc001pyo.3. human. [P11142-1]
uc001pyp.3. human. [P11142-2]

Organism-specific databases

CTD3312.
GeneCardsGC11M122969.
H-InvDBHIX0033867.
HGNCHGNC:5241. HSPA8.
HPACAB002056.
MIM600816. gene.
neXtProtNX_P11142.
PharmGKBPA29507.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP11142.
KOK03283.
OMAGENKIFT.
OrthoDBEOG7PCJGF.
PhylomeDBP11142.
TreeFamTF105042.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_11123. Membrane Trafficking.
REACT_120956. Cellular responses to stress.
REACT_13685. Neuronal System.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP11142.
BgeeP11142.
CleanExHS_HSPA8.
GenevestigatorP11142.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA8. human.
EvolutionaryTraceP11142.
GeneWikiHSPA8.
GenomeRNAi3312.
NextBio13136.
PMAP-CutDBP11142.
PROP11142.
SOURCESearch...

Entry information

Entry nameHSP7C_HUMAN
AccessionPrimary (citable) accession number: P11142
Secondary accession number(s): Q9H3R6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 180 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM