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Protein

60 kDa heat shock protein, mitochondrial

Gene

HSPD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).1 Publication2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei75ATPCombined sources1 Publication1
Binding sitei440ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei520ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi111 – 115ATPCombined sources1 Publication5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase
Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1268020 Mitochondrial protein import
R-HSA-8869496 TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation
SIGNORiP10809

Protein family/group databases

MoonProtiP10809

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial (EC:3.6.4.9)
Alternative name(s):
60 kDa chaperonin
Chaperonin 60
Short name:
CPN60
Heat shock protein 60
Short name:
HSP-60
Short name:
Hsp60
HuCHA60
Mitochondrial matrix protein P1
P60 lymphocyte protein
Gene namesi
Name:HSPD1
Synonyms:HSP60
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000144381.16
HGNCiHGNC:5261 HSPD1
MIMi118190 gene
neXtProtiNX_P10809

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 13, autosomal dominant (SPG13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
See also OMIM:605280
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02674898V → I in SPG13. 1 PublicationCorresponds to variant dbSNP:rs66468541EnsemblClinVar.1
Leukodystrophy, hypomyelinating, 4 (HLD4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life.
See also OMIM:612233
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05478529D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 PublicationCorresponds to variant dbSNP:rs72466451EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Leukodystrophy, Neurodegeneration

Organism-specific databases

DisGeNETi3329
MalaCardsiHSPD1
MIMi605280 phenotype
612233 phenotype
OpenTargetsiENSG00000144381
Orphaneti100994 Autosomal dominant spastic paraplegia type 13
280288 Pelizaeus-Merzbacher-like disease due to HSPD1 mutation
PharmGKBiPA29527

Chemistry databases

ChEMBLiCHEMBL4721

Polymorphism and mutation databases

BioMutaiHSPD1
DMDMi129379

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 26Mitochondrion7 PublicationsAdd BLAST26
ChainiPRO_000000502627 – 57360 kDa heat shock protein, mitochondrialAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei67PhosphoserineCombined sources1
Modified residuei70PhosphoserineCombined sources1
Modified residuei75N6-acetyllysineBy similarity1
Modified residuei82N6-acetyllysine; alternateCombined sources1
Modified residuei82N6-succinyllysine; alternateBy similarity1
Modified residuei87N6-acetyllysineBy similarity1
Modified residuei90PhosphotyrosineCombined sources1
Modified residuei91N6-acetyllysineBy similarity1
Modified residuei125N6-acetyllysine; alternateCombined sources1
Modified residuei125N6-succinyllysine; alternateBy similarity1
Modified residuei130N6-acetyllysineCombined sources1
Modified residuei133N6-acetyllysine; alternateBy similarity1
Modified residuei133N6-malonyllysine; alternate1 Publication1
Modified residuei133N6-succinyllysine; alternateBy similarity1
Modified residuei156N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei202N6-acetyllysine; alternateCombined sources1
Modified residuei202N6-succinyllysine; alternateBy similarity1
Modified residuei205N6-acetyllysine; alternateBy similarity1
Modified residuei205N6-succinyllysine; alternateBy similarity1
Modified residuei218N6-acetyllysine; alternateCombined sources1
Modified residuei218N6-succinyllysine; alternateBy similarity1
Modified residuei236N6-acetyllysine; alternateBy similarity1
Modified residuei236N6-succinyllysine; alternateBy similarity1
Modified residuei249N6-acetyllysineBy similarity1
Modified residuei250N6-acetyllysine; alternateBy similarity1
Modified residuei250N6-succinyllysine; alternateBy similarity1
Modified residuei269N6-acetyllysineCombined sources1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei301N6-succinyllysineBy similarity1
Modified residuei314N6-acetyllysineBy similarity1
Modified residuei352N6-acetyllysine; alternateCombined sources1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei359N6-acetyllysineCombined sources1
Modified residuei389N6-acetyllysineBy similarity1
Modified residuei396N6-acetyllysine; alternateCombined sources1
Modified residuei396N6-succinyllysine; alternateBy similarity1
Modified residuei410PhosphoserineBy similarity1
Modified residuei469N6-acetyllysineCombined sources1
Modified residuei481N6-acetyllysine; alternateBy similarity1
Modified residuei481N6-succinyllysine; alternateBy similarity1
Modified residuei488PhosphoserineCombined sources1
Cross-linki551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP10809
MaxQBiP10809
PaxDbiP10809
PeptideAtlasiP10809
PRIDEiP10809
ProteomicsDBi52653
TopDownProteomicsiP10809-1 [P10809-1]

2D gel databases

DOSAC-COBS-2DPAGEiP10809
OGPiP10809
REPRODUCTION-2DPAGEiIPI00784154
P10809
SWISS-2DPAGEiP10809
UCD-2DPAGEiP10809

PTM databases

CarbonylDBiP10809
iPTMnetiP10809
PhosphoSitePlusiP10809
SwissPalmiP10809

Expressioni

Gene expression databases

BgeeiENSG00000144381 Expressed in 106 organ(s), highest expression level in adrenal tissue
CleanExiHS_HSPD1
ExpressionAtlasiP10809 baseline and differential
GenevisibleiP10809 HS

Organism-specific databases

HPAiCAB002775
CAB072816
HPA001523
HPA050025

Interactioni

Subunit structurei

Homoheptamer arranged in a ring structure (PubMed:1346131, PubMed:11422376, PubMed:25918392). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (PubMed:25918392). Interacts with HRAS (By similarity). Interacts with ATAD3A (PubMed:22664726). Interacts with ETFBKMT and METTL21B (PubMed:23349634). Interacts with MFHAS1 (PubMed:24286120).By similarity6 Publications
(Microbial infection) Interacts with hepatits B virus/HBV protein X.1 Publication
(Microbial infection) Interacts with HTLV-1 protein p40tax.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109561, 301 interactors
CORUMiP10809
DIPiDIP-58N
IntActiP10809, 352 interactors
MINTiP10809
STRINGi9606.ENSP00000340019

Structurei

Secondary structure

1573
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP10809
SMRiP10809
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356 Eukaryota
COG0459 LUCA
GeneTreeiENSGT00390000005727
HOGENOMiHOG000076290
HOVERGENiHBG001982
InParanoidiP10809
KOiK04077
OMAiTDTDKME
OrthoDBiEOG091G04JM
PhylomeDBiP10809
TreeFamiTF300475

Family and domain databases

CDDicd03344 GroEL, 1 hit
Gene3Di1.10.560.10, 2 hits
3.30.260.10, 2 hits
3.50.7.10, 1 hit
HAMAPiMF_00600 CH60, 1 hit
InterProiView protein in InterPro
IPR018370 Chaperonin_Cpn60_CS
IPR001844 Chaprnin_Cpn60
IPR002423 Cpn60/TCP-1
IPR027409 GroEL-like_apical_dom_sf
IPR027413 GROEL-like_equatorial_sf
IPR027410 TCP-1-like_intermed_sf
PfamiView protein in Pfam
PF00118 Cpn60_TCP1, 1 hit
PRINTSiPR00298 CHAPERONIN60
SUPFAMiSSF48592 SSF48592, 2 hits
SSF52029 SSF52029, 1 hit
SSF54849 SSF54849, 1 hit
TIGRFAMsiTIGR02348 GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296 CHAPERONINS_CPN60, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.iShow all

Isoform 1 (identifier: P10809-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA
60 70 80 90 100
VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD
110 120 130 140 150
VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA
160 170 180 190 200
VIAELKKQSK PVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT
210 220 230 240 250
VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK
260 270 280 290 300
ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
310 320 330 340 350
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV
360 370 380 390 400
TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG
410 420 430 440 450
VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA
460 470 480 490 500
LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE
510 520 530 540 550
VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP
560 570
KEEKDPGMGA MGGMGGGMGG GMF
Length:573
Mass (Da):61,055
Last modified:August 1, 1990 - v2
Checksum:iE51E1BAD9615899C
GO
Isoform 2 (identifier: P10809-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     144-158: VMLAVDAVIAELKKQ → RNVCCHHSVLNFSVL
     159-573: Missing.

Note: No experimental confirmation available.
Show »
Length:158
Mass (Da):17,100
Checksum:i9FC1907D8E2C1ECE
GO

Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JL25C9JL25_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
175Annotation score:
E7EXB4E7EXB4_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
221Annotation score:
E7ESH4E7ESH4_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
234Annotation score:
C9JL19C9JL19_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
83Annotation score:
C9JCQ4C9JCQ4_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
94Annotation score:
C9J0S9C9J0S9_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
58Annotation score:
F8WBB1F8WBB1_HUMAN
60 kDa heat shock protein, mitochon...
HSPD1
48Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti67S → G in AAA36022 (PubMed:1980192).Curated1
Sequence conflicti111D → N in BAG35173 (PubMed:14702039).Curated1
Sequence conflicti177N → S in BAG35173 (PubMed:14702039).Curated1
Sequence conflicti202K → KAS in ABB01006 (Ref. 4) Curated1
Sequence conflicti260A → T in BAG35173 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05478529D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 PublicationCorresponds to variant dbSNP:rs72466451EnsemblClinVar.1
Natural variantiVAR_02674898V → I in SPG13. 1 PublicationCorresponds to variant dbSNP:rs66468541EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056144144 – 158VMLAV…ELKKQ → RNVCCHHSVLNFSVL in isoform 2. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_056145159 – 573Missing in isoform 2. 1 PublicationAdd BLAST415

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22382 mRNA Translation: AAA60127.1
M34664 mRNA Translation: AAA36022.1
AJ250915 Genomic DNA Translation: CAB75426.1
DQ217936 Genomic DNA Translation: ABB01006.1
AK301276 mRNA Translation: BAH13448.1
AK312240 mRNA Translation: BAG35173.1
AC010746 Genomic DNA No translation available.
AC020550 Genomic DNA No translation available.
AC114809 Genomic DNA No translation available.
BC002676 mRNA Translation: AAH02676.1
BC003030 mRNA Translation: AAH03030.1
BC067082 mRNA Translation: AAH67082.1
BC073746 mRNA Translation: AAH73746.1
CCDSiCCDS33357.1 [P10809-1]
PIRiA32800
RefSeqiNP_002147.2, NM_002156.4 [P10809-1]
NP_955472.1, NM_199440.1 [P10809-1]
UniGeneiHs.595053
Hs.727543

Genome annotation databases

EnsembliENST00000345042; ENSP00000340019; ENSG00000144381 [P10809-1]
ENST00000388968; ENSP00000373620; ENSG00000144381 [P10809-1]
GeneIDi3329
KEGGihsa:3329
UCSCiuc002uui.4 human [P10809-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22382 mRNA Translation: AAA60127.1
M34664 mRNA Translation: AAA36022.1
AJ250915 Genomic DNA Translation: CAB75426.1
DQ217936 Genomic DNA Translation: ABB01006.1
AK301276 mRNA Translation: BAH13448.1
AK312240 mRNA Translation: BAG35173.1
AC010746 Genomic DNA No translation available.
AC020550 Genomic DNA No translation available.
AC114809 Genomic DNA No translation available.
BC002676 mRNA Translation: AAH02676.1
BC003030 mRNA Translation: AAH03030.1
BC067082 mRNA Translation: AAH67082.1
BC073746 mRNA Translation: AAH73746.1
CCDSiCCDS33357.1 [P10809-1]
PIRiA32800
RefSeqiNP_002147.2, NM_002156.4 [P10809-1]
NP_955472.1, NM_199440.1 [P10809-1]
UniGeneiHs.595053
Hs.727543

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PJ1X-ray3.15A/B/C/D/E/F/G/H/I/J/K/L/M/N27-556[»]
ProteinModelPortaliP10809
SMRiP10809
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109561, 301 interactors
CORUMiP10809
DIPiDIP-58N
IntActiP10809, 352 interactors
MINTiP10809
STRINGi9606.ENSP00000340019

Chemistry databases

ChEMBLiCHEMBL4721

Protein family/group databases

MoonProtiP10809

PTM databases

CarbonylDBiP10809
iPTMnetiP10809
PhosphoSitePlusiP10809
SwissPalmiP10809

Polymorphism and mutation databases

BioMutaiHSPD1
DMDMi129379

2D gel databases

DOSAC-COBS-2DPAGEiP10809
OGPiP10809
REPRODUCTION-2DPAGEiIPI00784154
P10809
SWISS-2DPAGEiP10809
UCD-2DPAGEiP10809

Proteomic databases

EPDiP10809
MaxQBiP10809
PaxDbiP10809
PeptideAtlasiP10809
PRIDEiP10809
ProteomicsDBi52653
TopDownProteomicsiP10809-1 [P10809-1]

Protocols and materials databases

DNASUi3329
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345042; ENSP00000340019; ENSG00000144381 [P10809-1]
ENST00000388968; ENSP00000373620; ENSG00000144381 [P10809-1]
GeneIDi3329
KEGGihsa:3329
UCSCiuc002uui.4 human [P10809-1]

Organism-specific databases

CTDi3329
DisGeNETi3329
EuPathDBiHostDB:ENSG00000144381.16
GeneCardsiHSPD1
HGNCiHGNC:5261 HSPD1
HPAiCAB002775
CAB072816
HPA001523
HPA050025
MalaCardsiHSPD1
MIMi118190 gene
605280 phenotype
612233 phenotype
neXtProtiNX_P10809
OpenTargetsiENSG00000144381
Orphaneti100994 Autosomal dominant spastic paraplegia type 13
280288 Pelizaeus-Merzbacher-like disease due to HSPD1 mutation
PharmGKBiPA29527
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0356 Eukaryota
COG0459 LUCA
GeneTreeiENSGT00390000005727
HOGENOMiHOG000076290
HOVERGENiHBG001982
InParanoidiP10809
KOiK04077
OMAiTDTDKME
OrthoDBiEOG091G04JM
PhylomeDBiP10809
TreeFamiTF300475

Enzyme and pathway databases

ReactomeiR-HSA-1268020 Mitochondrial protein import
R-HSA-8869496 TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation
SIGNORiP10809

Miscellaneous databases

ChiTaRSiHSPD1 human
GeneWikiiGroEL
GenomeRNAii3329
PROiPR:P10809
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000144381 Expressed in 106 organ(s), highest expression level in adrenal tissue
CleanExiHS_HSPD1
ExpressionAtlasiP10809 baseline and differential
GenevisibleiP10809 HS

Family and domain databases

CDDicd03344 GroEL, 1 hit
Gene3Di1.10.560.10, 2 hits
3.30.260.10, 2 hits
3.50.7.10, 1 hit
HAMAPiMF_00600 CH60, 1 hit
InterProiView protein in InterPro
IPR018370 Chaperonin_Cpn60_CS
IPR001844 Chaprnin_Cpn60
IPR002423 Cpn60/TCP-1
IPR027409 GroEL-like_apical_dom_sf
IPR027413 GROEL-like_equatorial_sf
IPR027410 TCP-1-like_intermed_sf
PfamiView protein in Pfam
PF00118 Cpn60_TCP1, 1 hit
PRINTSiPR00298 CHAPERONIN60
SUPFAMiSSF48592 SSF48592, 2 hits
SSF52029 SSF52029, 1 hit
SSF54849 SSF54849, 1 hit
TIGRFAMsiTIGR02348 GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296 CHAPERONINS_CPN60, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCH60_HUMAN
AccessioniPrimary (citable) accession number: P10809
Secondary accession number(s): B2R5M6
, B7Z712, Q38L19, Q9UCR6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1990
Last modified: September 12, 2018
This is version 224 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health

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