Reviewed, UniProtKB/Swiss-Prot P11142 (HSP7C_HUMAN)

Names and origin

Protein names

Recommended name:
    Heat shock cognate 71 kDa protein
Alternative name(s):
    Heat shock 70 kDa protein 8

Gene names

Name:	HSPA8
Synonyms:	HSC70, HSP73, HSPA10

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones.
Subunit structure	Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 By similarity. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG and TSC2. Interacts with BAG1. Interacts with SV40 VP1. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
Subcellular location	Cytoplasm. Melanosome. 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. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10 Ref.18 Ref.20
Tissue specificity	Ubiquitous.
Induction	Constitutively synthesized.
Domain	The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain. Ref.11
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.15 Ref.17 Ref.19 Ref.21 Ref.22 Ref.24
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Host-virus interaction Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW membrane organization Inferred from Experiment. Source: Reactome post-Golgi vesicle-mediated transport Inferred from Experiment. Source: Reactome response to unfolded protein Ref.2 Non-traceable author statement. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Ref.20 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-351896,EBI-743313
ARRB2	P32121	1	EBI-351896,EBI-714559
GCH1	P30793	2	EBI-351896,EBI-958183
HSPBP1	Q9NZL4	2	EBI-351896,EBI-356763
STUB1	Q9UNE7	2	EBI-351896,EBI-357085

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 646

645

Heat shock cognate 71 kDa protein

PRO_0000078270

Regions

Region

186 – 377

192

Interaction with BAG1

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

15

1

Phosphotyrosine Ref.17

Modified residue

41

1

Phosphotyrosine Ref.19

Modified residue

88

1

N6-acetyllysine Ref.25

Modified residue

107

1

Phosphotyrosine Ref.19

Modified residue

108

1

N6-acetyllysine Ref.25

Modified residue

113

1

Phosphoserine Ref.22

Modified residue

115

1

Phosphotyrosine Ref.22

Modified residue

120

1

Phosphoserine Ref.22

Modified residue

121

1

Phosphoserine Ref.22

Modified residue

153

1

Phosphoserine Ref.21

Modified residue

246

1

N6-acetyllysine Ref.25

Modified residue

319

1

N6-acetyllysine Ref.25

Modified residue

348

1

N6-acetyllysine Ref.25

Modified residue

477

1

Phosphothreonine Ref.15

Modified residue

512

1

N6-acetyllysine Ref.25

Modified residue

524

1

N6-acetyllysine Ref.25

Modified residue

541

1

Phosphoserine Ref.24

Modified residue

589

1

N6-acetyllysine Ref.25

Modified residue

597

1

N6-acetyllysine Ref.25

Modified residue

601

1

N6-acetyllysine Ref.25

Modified residue

637

1

Phosphoserine Ref.24

Modified residue

638

1

Phosphoserine Ref.24

Natural variations

Alternative sequence

464 – 616

153

Missing in isoform 2.

VSP_002427

Natural variant

32

1

D → Y: dbSNP rs11551602.

VAR_049619

Natural variant

459

1

F → L: dbSNP rs11551598.

VAR_049620

Secondary structure

1

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646

Helix Strand Turn

Details...

Beta strand

15 – 17

3

Beta strand

37 – 39

3

Beta strand

42 – 44

3

Helix

54 – 57

4

Turn

58 – 61

4

Helix

70 – 72

3

Helix

81 – 86

6

Helix

87 – 89

3

Beta strand

91 – 96

6

Beta strand

101 – 106

6

Beta strand

111 – 114

4

Helix

116 – 134

19

Beta strand

141 – 146

6

Helix

152 – 160

9

Beta strand

168 – 174

7

Helix

175 – 182

8

Beta strand

193 – 200

8

Beta strand

206 – 212

7

Beta strand

217 – 223

7

Helix

232 – 249

18

Helix

257 – 273

17

Turn

274 – 276

3

Beta strand

277 – 284

8

Beta strand

293 – 298

6

Helix

299 – 305

7

Helix

307 – 310

4

Helix

314 – 323

10

Helix

328 – 330

3

Beta strand

333 – 337

5

Helix

344 – 353

10

Turn

365 – 370

6

Helix

374 – 380

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 9AA27B210730670C	FASTA	646	70,898
	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
	Isoform 2 (HSC54). Checksum: BA2CFBD68F17784E	FASTA	493	53,518
	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 LTGMPGGMPG GFPGGGAPPS 490 GGASSGPTIE EVD

References

	« Hide 'large scale' referencesShow '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: 3037489] [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: 11093761] [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: 15489334] [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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 78-88; 113-155; 160-188; 221-246; 300-319; 329-342; 349-357; 362-384; 459-469; 510-517; 540-550; 584-597 AND 602-609, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[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: 1286667] [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: 8713105] [Abstract] Cited for: PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
[10]	"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: 1586970] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"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: 9305631] [Abstract] Cited for: INTERACTION WITH BAG1, DOMAIN.
[12]	"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: 9679980] [Abstract] Cited for: INTERACTION WITH BAG1.
[13]	"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: 11147964] [Abstract] Cited for: INTERACTION WITH SV40 VP1.
[14]	"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: 14532270] [Abstract] Cited for: INTERACTION WITH PACRG.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-477, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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: 15963462] [Abstract] Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
[17]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, MASS SPECTROMETRY.
[18]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41 AND TYR-107, MASS SPECTROMETRY.
[20]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[21]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, MASS SPECTROMETRY.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; TYR-115; SER-120 AND SER-121, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-637 AND SER-638, MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-108; LYS-246; LYS-319; LYS-348; LYS-512; LYS-524; LYS-589; LYS-597 AND LYS-601, MASS SPECTROMETRY.
+	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.

IPI

IPI00003865.
IPI00939595.

PIR

A27077.

RefSeq

NP_006588.1.
NP_694881.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ESK	X-ray	2.05	B	635-646	[»]
3FZF	X-ray	2.20	A	4-381	[»]
3FZH	X-ray	2.00	A	4-381	[»]
3FZK	X-ray	2.10	A	4-381	[»]
3FZL	X-ray	2.20	A	4-381	[»]
3FZM	X-ray	2.30	A	4-381	[»]

SMR

P11142. Positions 1-554, 542-621.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11142. 60 interactions.

STRING

P11142.

PTM databases

PhosphoSite

P11142.

2-D gel databases

SWISS-2DPAGE

P11142.

Aarhus/Ghent-2DPAGE

6504. IEF.

Cornea-2DPAGE

P11142.

DOSAC-COBS-2DPAGE

P11142.

HSC-2DPAGE

P11142.

OGP

P11142.

PHCI-2DPAGE

P11142.

REPRODUCTION-2DPAGE

IPI00003865.

Proteomic databases

PeptideAtlas

P11142.

PRIDE

P11142.

Genome annotation databases

Ensembl

ENST00000227378; ENSP00000227378; ENSG00000109971; Homo sapiens. [Genome view]

GeneID

3312.

KEGG

hsa:3312.

UCSC

uc001pyo.1. human.
uc001pyp.1. human.

Organism-specific databases

CTD

3312.

GeneCards

GC11M122460.

H-InvDB

HIX0010213.

HGNC

HGNC:5241. HSPA8.

HPA

CAB002056.

MIM

600816. gene.

PharmGKB

PA29507.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17884.

HOGENOM

HBG334976.

HOVERGEN

P11142.

InParanoid

P11142.

OMA

EKYKADD.

OrthoDB

EOG9TQPV5.

PhylomeDB

P11142.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

P11142.

CleanEx

HS_HSPA8.

Genevestigator

P11142.

GermOnline

ENSG00000109971. Homo sapiens.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13136.

PMAP-CutDB

P11142.

SOURCE

Search...

Entry information

Entry name

HSP7C_HUMAN

Accession

Primary (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:	January 19, 2010
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.