P11142 (HSP7C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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. Ref.14
Subunit structure	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. 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.24
Subcellular location	Cytoplasm. Melanosome. Nucleus › nucleolus. 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.10 Ref.18 Ref.20 Ref.25
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	Acetylated. ISGylated. Ref.16 Ref.19
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Host-virus interaction Stress response Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cellular membrane organization Traceable author statement. Source: Reactome chaperone mediated protein folding requiring cofactor Inferred from electronic annotation. Source: Compara gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.14. 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 regulation of cell cycle Inferred from electronic annotation. Source: Compara response to unfolded protein Non-traceable author statement Ref.2. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Prp19 complex Inferred from direct assay Ref.25. Source: UniProtKB cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Traceable author statement. Source: Reactome cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay PubMed 92266438. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.20. Source: UniProtKB spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Non-traceable author statement PubMed 8530083. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTB	P60709	2	EBI-351896,EBI-353944
ARRB1	P49407	4	EBI-351896,EBI-743313
ARRB2	P32121	4	EBI-351896,EBI-714559
ATP13A2	Q9NQ11	2	EBI-351896,EBI-6308763
STUB1	Q9UNE7	3	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 Ref.6

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 Ref.6

Modified residue

15

1

Phosphotyrosine By similarity

Modified residue

41

1

Phosphotyrosine By similarity

Modified residue

153

1

Phosphoserine Ref.21

Modified residue

246

1

N6-acetyllysine Ref.23

Modified residue

319

1

N6-acetyllysine Ref.23

Modified residue

362

1

Phosphoserine Ref.26

Modified residue

589

1

N6-acetyllysine Ref.23

Modified residue

597

1

N6-acetyllysine Ref.23

Modified residue

601

1

N6-acetyllysine Ref.23

Natural variations

Alternative sequence

464 – 616

153

Missing in isoform 2.

VSP_002427

Natural variant

32

1

D → Y.
Corresponds to variant rs11551602 [ dbSNP | Ensembl ].

VAR_049619

Natural variant

459

1

F → L.
Corresponds to variant rs11551598 [ dbSNP | Ensembl ].

VAR_049620

Secondary structure

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646

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Beta strand

13 – 22

10

Beta strand

25 – 28

4

Beta strand

36 – 39

4

Beta strand

42 – 44

3

Beta strand

49 – 51

3

Helix

53 – 57

5

Turn

58 – 61

4

Beta strand

65 – 67

3

Helix

70 – 72

3

Turn

73 – 75

3

Helix

81 – 87

7

Beta strand

91 – 97

7

Beta strand

100 – 107

8

Beta strand

110 – 114

5

Helix

116 – 135

20

Beta strand

141 – 146

6

Helix

152 – 164

13

Beta strand

168 – 174

7

Helix

175 – 182

8

Helix

185 – 187

3

Beta strand

193 – 200

8

Beta strand

205 – 213

9

Beta strand

216 – 225

10

Helix

230 – 249

20

Helix

253 – 255

3

Helix

257 – 273

17

Turn

274 – 276

3

Beta strand

277 – 288

12

Beta strand

291 – 298

8

Helix

299 – 305

7

Helix

307 – 312

6

Helix

314 – 323

10

Helix

328 – 330

3

Beta strand

333 – 338

6

Helix

339 – 342

4

Helix

344 – 353

10

Turn

354 – 356

3

Beta strand

357 – 360

4

Turn

365 – 367

3

Helix

368 – 380

13

Beta strand

641 – 644

4

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) [UniParc]. 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] [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, 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, 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, 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]	"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.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SV40 VP1.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"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.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[22]	"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.
[23]	"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, MASS SPECTROMETRY.
[24]	"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.
[25]	"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.
[26]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
+	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.
IPI00037070.

PIR

A27077.

RefSeq

NP_006588.1. NM_006597.4.
NP_694881.1. NM_153201.2.

UniGene

Hs.180414.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AGY	X-ray	1.85	C/D/F	639-646	[»]
3AGZ	X-ray	2.51	C/D/E/F	639-646	[»]
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	[»]
3LDQ	X-ray	1.90	A	4-381	[»]
3M3Z	X-ray	2.10	A	4-381	[»]

ProteinModelPortal

P11142.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11142. 61 interactions.

MINT

MINT-4998609.

STRING

9606.ENSP00000227378.

PTM databases

PhosphoSite

P11142.

Polymorphism databases

DMDM

123648.

2D gel databases

DOSAC-COBS-2DPAGE

P11142.

OGP

P11142.

REPRODUCTION-2DPAGE

IPI00003865.

SWISS-2DPAGE

P11142.

UCD-2DPAGE

P11142.

Proteomic databases

PaxDb

P11142.

PeptideAtlas

P11142.

PRIDE

P11142.

Protocols and materials databases

DNASU

3312.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227378; ENSP00000227378; ENSG00000109971.
ENST00000453788; ENSP00000404372; ENSG00000109971.
ENST00000532636; ENSP00000437125; ENSG00000109971.
ENST00000534624; ENSP00000432083; ENSG00000109971.

GeneID

3312.

KEGG

hsa:3312.

UCSC

uc001pyo.3. human.
uc001pyp.3. human.

Organism-specific databases

CTD

3312.

GeneCards

GC11M122952.

H-InvDB

HIX0033867.

HGNC

HGNC:5241. HSPA8.

HPA

CAB002056.

MIM

600816. gene.

neXtProt

NX_P11142.

PharmGKB

PA29507.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0443.

HOGENOM

HOG000228135.

HOVERGEN

HBG051845.

InParanoid

P11142.

KO

K03283.

OMA

FNVINDN.

OrthoDB

EOG4W6NVK.

PhylomeDB

P11142.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_11123. Membrane Trafficking.
REACT_13685. Neuronal System.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P11142.

Bgee

P11142.

CleanEx

HS_HSPA8.

Genevestigator

P11142.

GermOnline

ENSG00000109971. Homo sapiens.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]

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

BindingDB

P11142.

ChEMBL

CHEMBL1275223.

ChiTaRS

HSPA8. human.

EvolutionaryTrace

P11142.

GenomeRNAi

3312.

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:	May 1, 2013
This is version 168 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.