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P19120

- HSP7C_BOVIN

UniProt

P19120 - HSP7C_BOVIN

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Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP (By similarity).By similarity

Sites

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

Regions

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

GO - Molecular functioni

  1. ATPase activity, coupled Source: Ensembl
  2. ATP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. chaperone mediated protein folding requiring cofactor Source: Ensembl
  2. clathrin coat disassembly Source: Ensembl
  3. mRNA processing Source: UniProtKB-KW
  4. negative regulation of fibril organization Source: Ensembl
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. protein refolding Source: Ensembl
  7. regulation of cell cycle Source: Ensembl
  8. response to stress Source: UniProtKB-KW
  9. RNA splicing Source: UniProtKB-KW
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_205580. HSF1-dependent transactivation.
REACT_211255. GABA synthesis, release, reuptake and degradation.
REACT_213591. Attenuation phase.
REACT_214880. CHL1 interactions.
REACT_218726. Regulation of HSF1-mediated heat shock response.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Gene namesi
Name:HSPA8
Synonyms:HSC70
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 15

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity. Nucleusnucleolus By similarity. Cell membrane By similarity
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 (By similarity).By similarity

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleolus Source: Ensembl
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB-KW
  7. Prp19 complex Source: UniProtKB
  8. ribonucleoprotein complex Source: UniProtKB
  9. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 650649Heat shock cognate 71 kDa proteinPRO_0000078268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity
Modified residuei246 – 2461N6-acetyllysineBy similarity
Modified residuei319 – 3191N6-acetyllysine; alternateBy similarity
Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity
Modified residuei328 – 3281N6-acetyllysineBy similarity
Modified residuei362 – 3621PhosphoserineBy similarity
Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
Modified residuei524 – 5241N6-acetyllysineBy similarity
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21ABy similarity
Modified residuei589 – 5891N6-acetyllysineBy similarity
Modified residuei597 – 5971N6-acetyllysineBy similarity
Modified residuei601 – 6011N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated.By similarity
ISGylated.By similarity
Trimethylation at Lys-561 reduces fibrillar SNCA binding.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19120.
PRIDEiP19120.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Constitutively synthesized.

Gene expression databases

ExpressionAtlasiP19120. baseline.

Interactioni

Subunit structurei

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 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. 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 TRIM5 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 (By similarity). Interacts with PARK2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CFTRP135692EBI-907802,EBI-349854From a different organism.
CftrP263615EBI-907802,EBI-6115317From a different organism.

Protein-protein interaction databases

BioGridi159144. 2 interactions.
DIPiDIP-35481N.
IntActiP19120. 6 interactions.
MINTiMINT-157582.
STRINGi9913.ENSBTAP00000017497.

Structurei

Secondary structure

1
650
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104
Beta strandi13 – 2210
Beta strandi25 – 284
Beta strandi36 – 394
Beta strandi42 – 443
Beta strandi49 – 513
Helixi53 – 564
Turni57 – 615
Helixi63 – 653
Beta strandi66 – 683
Helixi70 – 723
Turni73 – 753
Helixi81 – 877
Beta strandi91 – 977
Beta strandi100 – 1078
Beta strandi110 – 1145
Helixi116 – 13520
Beta strandi141 – 1466
Helixi152 – 16413
Beta strandi168 – 1747
Helixi175 – 1828
Turni183 – 1864
Beta strandi187 – 1915
Beta strandi193 – 2008
Beta strandi205 – 2139
Beta strandi216 – 22510
Helixi230 – 24920
Helixi253 – 2553
Helixi257 – 27317
Turni274 – 2763
Beta strandi277 – 28812
Beta strandi291 – 2988
Helixi299 – 31214
Helixi314 – 32310
Helixi328 – 3303
Beta strandi333 – 3386
Helixi339 – 3424
Helixi344 – 35310
Turni354 – 3563
Helixi365 – 3673
Helixi368 – 38013
Beta strandi386 – 3883
Beta strandi392 – 3965
Beta strandi401 – 4055
Turni406 – 4083
Beta strandi409 – 4146
Beta strandi419 – 43214
Beta strandi438 – 4469
Helixi450 – 4523
Beta strandi453 – 4619
Beta strandi474 – 4807
Beta strandi486 – 4927
Turni493 – 4953
Beta strandi498 – 5036
Helixi512 – 52413
Helixi526 – 5349
Beta strandi539 – 5424
Helixi547 – 5493

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATRX-ray2.34A1-386[»]
1ATSX-ray2.43A1-386[»]
1BA0X-ray1.90A1-386[»]
1BA1X-ray1.70A1-386[»]
1BUPX-ray1.70A1-386[»]
1HPMX-ray1.70A1-386[»]
1HX1X-ray1.90A4-381[»]
1KAXX-ray1.70A1-381[»]
1KAYX-ray1.70A1-381[»]
1KAZX-ray1.70A1-381[»]
1NGAX-ray2.18A1-386[»]
1NGBX-ray2.18A1-386[»]
1NGCX-ray2.20A1-386[»]
1NGDX-ray2.18A1-386[»]
1NGEX-ray2.05A1-386[»]
1NGFX-ray2.17A1-386[»]
1NGGX-ray2.19A1-386[»]
1NGHX-ray2.23A1-386[»]
1NGIX-ray2.15A1-386[»]
1NGJX-ray2.10A1-386[»]
1Q2Gmodel-B4-381[»]
1QQMX-ray1.90A4-381[»]
1QQNX-ray1.90A4-381[»]
1QQOX-ray1.90A4-381[»]
1YUWX-ray2.60A1-554[»]
2BUPX-ray1.70A1-381[»]
2QW9X-ray1.85A/B1-394[»]
2QWLX-ray1.75A/B1-394[»]
2QWMX-ray1.86A/B1-394[»]
2QWNX-ray2.40A1-394[»]
2QWOX-ray1.70A1-394[»]
2QWPX-ray1.75A1-394[»]
2QWQX-ray2.21A1-394[»]
2QWRX-ray2.21A1-394[»]
3C7NX-ray3.12B1-554[»]
3HSCX-ray1.93A1-386[»]
4FL9X-ray1.90A1-554[»]
ProteinModelPortaliP19120.
SMRiP19120. Positions 1-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19120.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 377192Interaction with BAG1By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP19120.
KOiK03283.
OMAiGENKIFT.
OrthoDBiEOG7PCJGF.
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.

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

P19120-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK
510 520 530 540 550
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK
560 570 580 590 600
ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
610 620 630 640 650
KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD
Length:650
Mass (Da):71,241
Last modified:May 29, 2007 - v2
Checksum:iFBE109C14A28B925
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801A → T in AAI05183. 1 PublicationCurated
Sequence conflicti543 – 5431E → K in CAA37422. (PubMed:2216746)Curated
Sequence conflicti543 – 5431E → K in CAA37823. (PubMed:2216746)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53827 mRNA. Translation: CAA37823.1.
X53335 mRNA. Translation: CAA37422.1.
BT030487 mRNA. Translation: ABQ12927.1.
BC105182 mRNA. Translation: AAI05183.1.
PIRiS11456.
RefSeqiNP_776770.2. NM_174345.4.
UniGeneiBt.12309.

Genome annotation databases

EnsembliENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
GeneIDi281831.
KEGGibta:281831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53827 mRNA. Translation: CAA37823.1 .
X53335 mRNA. Translation: CAA37422.1 .
BT030487 mRNA. Translation: ABQ12927.1 .
BC105182 mRNA. Translation: AAI05183.1 .
PIRi S11456.
RefSeqi NP_776770.2. NM_174345.4.
UniGenei Bt.12309.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ATR X-ray 2.34 A 1-386 [» ]
1ATS X-ray 2.43 A 1-386 [» ]
1BA0 X-ray 1.90 A 1-386 [» ]
1BA1 X-ray 1.70 A 1-386 [» ]
1BUP X-ray 1.70 A 1-386 [» ]
1HPM X-ray 1.70 A 1-386 [» ]
1HX1 X-ray 1.90 A 4-381 [» ]
1KAX X-ray 1.70 A 1-381 [» ]
1KAY X-ray 1.70 A 1-381 [» ]
1KAZ X-ray 1.70 A 1-381 [» ]
1NGA X-ray 2.18 A 1-386 [» ]
1NGB X-ray 2.18 A 1-386 [» ]
1NGC X-ray 2.20 A 1-386 [» ]
1NGD X-ray 2.18 A 1-386 [» ]
1NGE X-ray 2.05 A 1-386 [» ]
1NGF X-ray 2.17 A 1-386 [» ]
1NGG X-ray 2.19 A 1-386 [» ]
1NGH X-ray 2.23 A 1-386 [» ]
1NGI X-ray 2.15 A 1-386 [» ]
1NGJ X-ray 2.10 A 1-386 [» ]
1Q2G model - B 4-381 [» ]
1QQM X-ray 1.90 A 4-381 [» ]
1QQN X-ray 1.90 A 4-381 [» ]
1QQO X-ray 1.90 A 4-381 [» ]
1YUW X-ray 2.60 A 1-554 [» ]
2BUP X-ray 1.70 A 1-381 [» ]
2QW9 X-ray 1.85 A/B 1-394 [» ]
2QWL X-ray 1.75 A/B 1-394 [» ]
2QWM X-ray 1.86 A/B 1-394 [» ]
2QWN X-ray 2.40 A 1-394 [» ]
2QWO X-ray 1.70 A 1-394 [» ]
2QWP X-ray 1.75 A 1-394 [» ]
2QWQ X-ray 2.21 A 1-394 [» ]
2QWR X-ray 2.21 A 1-394 [» ]
3C7N X-ray 3.12 B 1-554 [» ]
3HSC X-ray 1.93 A 1-386 [» ]
4FL9 X-ray 1.90 A 1-554 [» ]
ProteinModelPortali P19120.
SMRi P19120. Positions 1-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 159144. 2 interactions.
DIPi DIP-35481N.
IntActi P19120. 6 interactions.
MINTi MINT-157582.
STRINGi 9913.ENSBTAP00000017497.

Chemistry

BindingDBi P19120.
ChEMBLi CHEMBL1275213.

Proteomic databases

PaxDbi P19120.
PRIDEi P19120.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000017497 ; ENSBTAP00000017497 ; ENSBTAG00000013162 .
GeneIDi 281831.
KEGGi bta:281831.

Organism-specific databases

CTDi 3312.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P19120.
KOi K03283.
OMAi GENKIFT.
OrthoDBi EOG7PCJGF.
TreeFami TF105042.

Enzyme and pathway databases

Reactomei REACT_205580. HSF1-dependent transactivation.
REACT_211255. GABA synthesis, release, reuptake and degradation.
REACT_213591. Attenuation phase.
REACT_214880. CHL1 interactions.
REACT_218726. Regulation of HSF1-mediated heat shock response.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei P19120.
NextBioi 20805740.
PROi P19120.

Gene expression databases

ExpressionAtlasi P19120. baseline.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein."
    Deluca-Flaherty C., McKay D.B.
    Nucleic Acids Res. 18:5569-5569(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain cortex.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  4. "Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein."
    Flaherty K.M., de Luca-Flaherty C., McKay D.B.
    Nature 346:623-628(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
  5. "Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment."
    Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B.
    J. Biol. Chem. 269:12899-12907(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385 IN COMPLEXES WITH ADP AND ATP.
  6. "Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70."
    Wilbanks S.M., McKay D.B.
    Biochemistry 37:7456-7462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
  7. "The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change."
    Sousa M.C., McKay D.B.
    Biochemistry 37:15392-15399(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381 IN COMPLEX WITH ADP.
  8. "Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein."
    Johnson E.R., McKay D.B.
    Biochemistry 38:10823-10830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 2-554 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiHSP7C_BOVIN
AccessioniPrimary (citable) accession number: P19120
Secondary accession number(s): A5D968, Q3MHM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3