Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10809

- CH60_HUMAN

UniProt

P10809 - CH60_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

60 kDa heat shock protein, mitochondrial

Gene

HSPD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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.

GO - Molecular functioni

  1. ATPase activity Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. chaperone binding Source: UniProtKB
  4. DNA replication origin binding Source: BHF-UCL
  5. double-stranded RNA binding Source: MGI
  6. lipopolysaccharide binding Source: BHF-UCL
  7. p53 binding Source: UniProtKB
  8. poly(A) RNA binding Source: UniProtKB
  9. single-stranded DNA binding Source: BHF-UCL
  10. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' protein folding Source: BHF-UCL
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  3. ATP catabolic process Source: GOC
  4. B cell activation Source: BHF-UCL
  5. B cell cytokine production Source: BHF-UCL
  6. B cell proliferation Source: BHF-UCL
  7. chaperone-mediated protein complex assembly Source: BHF-UCL
  8. isotype switching to IgG isotypes Source: BHF-UCL
  9. MyD88-dependent toll-like receptor signaling pathway Source: BHF-UCL
  10. negative regulation of apoptotic process Source: UniProtKB
  11. positive regulation of apoptotic process Source: BHF-UCL
  12. positive regulation of interferon-alpha production Source: BHF-UCL
  13. positive regulation of interferon-gamma production Source: BHF-UCL
  14. positive regulation of interleukin-10 production Source: BHF-UCL
  15. positive regulation of interleukin-12 production Source: BHF-UCL
  16. positive regulation of interleukin-6 production Source: BHF-UCL
  17. positive regulation of macrophage activation Source: BHF-UCL
  18. positive regulation of T cell activation Source: BHF-UCL
  19. positive regulation of T cell mediated immune response to tumor cell Source: BHF-UCL
  20. protein maturation Source: BHF-UCL
  21. protein refolding Source: UniProtKB
  22. protein stabilization Source: UniProtKB
  23. response to unfolded protein Source: BHF-UCL
  24. T cell activation Source: MGI
  25. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial
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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:5261. HSPD1.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. coated pit Source: BHF-UCL
  3. coated vesicle Source: BHF-UCL
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. early endosome Source: BHF-UCL
  7. extracellular space Source: BHF-UCL
  8. extracellular vesicular exosome Source: UniProtKB
  9. lipopolysaccharide receptor complex Source: BHF-UCL
  10. membrane Source: UniProtKB
  11. mitochondrial inner membrane Source: BHF-UCL
  12. mitochondrial matrix Source: BHF-UCL
  13. mitochondrion Source: UniProtKB
  14. plasma membrane Source: Ensembl
  15. protein complex Source: UniProtKB
  16. secretory granule Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 13, autosomal dominant (SPG13) [MIM:605280]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981V → I in SPG13. 1 Publication
VAR_026748
Leukodystrophy, hypomyelinating, 4 (HLD4) [MIM:612233]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 Publication
VAR_054785

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Leukodystrophy, Neurodegeneration

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Mitochondrion7 PublicationsAdd
BLAST
Chaini27 – 57354760 kDa heat shock protein, mitochondrialPRO_0000005026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311N6-succinyllysineBy similarity
Modified residuei70 – 701Phosphoserine4 Publications
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysine; alternate1 Publication
Modified residuei82 – 821N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei125 – 1251N6-acetyllysine; alternate1 Publication
Modified residuei125 – 1251N6-succinyllysine; alternateBy similarity
Modified residuei130 – 1301N6-acetyllysine1 Publication
Modified residuei133 – 1331N6-acetyllysine; alternateBy similarity
Modified residuei133 – 1331N6-malonyllysine; alternate1 Publication
Modified residuei133 – 1331N6-succinyllysine; alternateBy similarity
Modified residuei156 – 1561N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
Modified residuei205 – 2051N6-acetyllysine; alternateBy similarity
Modified residuei205 – 2051N6-succinyllysine; alternateBy similarity
Modified residuei218 – 2181N6-acetyllysine; alternate1 Publication
Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
Modified residuei236 – 2361N6-acetyllysine; alternateBy similarity
Modified residuei236 – 2361N6-succinyllysine; alternateBy similarity
Modified residuei249 – 2491N6-acetyllysineBy similarity
Modified residuei250 – 2501N6-acetyllysine; alternateBy similarity
Modified residuei250 – 2501N6-succinyllysine; alternateBy similarity
Modified residuei269 – 2691N6-acetyllysine1 Publication
Modified residuei292 – 2921N6-acetyllysineBy similarity
Modified residuei301 – 3011N6-succinyllysineBy similarity
Modified residuei314 – 3141N6-acetyllysineBy similarity
Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
Modified residuei359 – 3591N6-acetyllysine1 Publication
Modified residuei389 – 3891N6-acetyllysineBy similarity
Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
Modified residuei396 – 3961N6-succinyllysine; alternateBy similarity
Modified residuei410 – 4101PhosphoserineBy similarity
Modified residuei469 – 4691N6-acetyllysine1 Publication
Modified residuei481 – 4811N6-acetyllysine; alternateBy similarity
Modified residuei481 – 4811N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP10809.
PaxDbiP10809.
PRIDEiP10809.

2D gel databases

DOSAC-COBS-2DPAGEP10809.
OGPiP10809.
REPRODUCTION-2DPAGEIPI00784154.
P10809.
SWISS-2DPAGEP10809.
UCD-2DPAGEP10809.

PTM databases

PhosphoSiteiP10809.

Expressioni

Gene expression databases

BgeeiP10809.
CleanExiHS_HSPD1.
ExpressionAtlasiP10809. baseline and differential.
GenevestigatoriP10809.

Organism-specific databases

HPAiCAB002775.
HPA001523.
HPA050025.

Interactioni

Subunit structurei

Interacts with HRAS (By similarity). Interacts with HBV protein X and HTLV-1 protein p40tax. Interacts with ATAD3A. Interacts with METTL20 and METTL21B.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383982EBI-352528,EBI-349905
FHITP497895EBI-352528,EBI-741760
MFHAS1Q9Y4C43EBI-352528,EBI-2864441

Protein-protein interaction databases

BioGridi109561. 149 interactions.
DIPiDIP-58N.
IntActiP10809. 67 interactions.
MINTiMINT-1162735.
STRINGi9606.ENSP00000340019.

Structurei

3D structure databases

ProteinModelPortaliP10809.
SMRiP10809. Positions 27-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00390000005727.
HOGENOMiHOG000076290.
HOVERGENiHBG001982.
InParanoidiP10809.
KOiK04077.
OMAiNYKAANE.
OrthoDBiEOG7HTHGJ.
PhylomeDBiP10809.
TreeFamiTF300475.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR017998. Chaperone_TCP-1.
IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
PR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 1 hit.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

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. Align

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671S → G in AAA36022. (PubMed:1980192)Curated
Sequence conflicti111 – 1111D → N in BAG35173. (PubMed:14702039)Curated
Sequence conflicti177 – 1771N → S in BAG35173. (PubMed:14702039)Curated
Sequence conflicti202 – 2021K → KAS in ABB01006. 1 PublicationCurated
Sequence conflicti260 – 2601A → T in BAG35173. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 Publication
VAR_054785
Natural varianti98 – 981V → I in SPG13. 1 Publication
VAR_026748

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei144 – 15815VMLAV…ELKKQ → RNVCCHHSVLNFSVL in isoform 2. 1 PublicationVSP_056144Add
BLAST
Alternative sequencei159 – 573415Missing in isoform 2. 1 PublicationVSP_056145Add
BLAST

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]
XP_005246575.1. XM_005246518.1. [P10809-1]
UniGeneiHs.595053.
Hs.727543.

Genome annotation databases

EnsembliENST00000345042; ENSP00000340019; ENSG00000144381. [P10809-1]
ENST00000388968; ENSP00000373620; ENSG00000144381. [P10809-1]
GeneIDi3329.
KEGGihsa:3329.
UCSCiuc002uui.3. human. [P10809-1]

Polymorphism databases

DMDMi129379.

Keywords - Coding sequence diversityi

Alternative splicing

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 .
CCDSi CCDS33357.1. [P10809-1 ]
PIRi A32800.
RefSeqi NP_002147.2. NM_002156.4. [P10809-1 ]
NP_955472.1. NM_199440.1. [P10809-1 ]
XP_005246575.1. XM_005246518.1. [P10809-1 ]
UniGenei Hs.595053.
Hs.727543.

3D structure databases

ProteinModelPortali P10809.
SMRi P10809. Positions 27-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109561. 149 interactions.
DIPi DIP-58N.
IntActi P10809. 67 interactions.
MINTi MINT-1162735.
STRINGi 9606.ENSP00000340019.

Chemistry

ChEMBLi CHEMBL4721.

PTM databases

PhosphoSitei P10809.

Polymorphism databases

DMDMi 129379.

2D gel databases

DOSAC-COBS-2DPAGE P10809.
OGPi P10809.
REPRODUCTION-2DPAGE IPI00784154.
P10809.
SWISS-2DPAGE P10809.
UCD-2DPAGE P10809.

Proteomic databases

MaxQBi P10809.
PaxDbi P10809.
PRIDEi P10809.

Protocols and materials databases

DNASUi 3329.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345042 ; ENSP00000340019 ; ENSG00000144381 . [P10809-1 ]
ENST00000388968 ; ENSP00000373620 ; ENSG00000144381 . [P10809-1 ]
GeneIDi 3329.
KEGGi hsa:3329.
UCSCi uc002uui.3. human. [P10809-1 ]

Organism-specific databases

CTDi 3329.
GeneCardsi GC02M198315.
HGNCi HGNC:5261. HSPD1.
HPAi CAB002775.
HPA001523.
HPA050025.
MIMi 118190. gene.
605280. phenotype.
612233. phenotype.
neXtProti NX_P10809.
Orphaneti 100994. Autosomal dominant spastic paraplegia type 13.
280288. Pelizaeus-Merzbacher-like disease due to HSPD1 mutation.
PharmGKBi PA29527.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
GeneTreei ENSGT00390000005727.
HOGENOMi HOG000076290.
HOVERGENi HBG001982.
InParanoidi P10809.
KOi K04077.
OMAi NYKAANE.
OrthoDBi EOG7HTHGJ.
PhylomeDBi P10809.
TreeFami TF300475.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSi HSPD1. human.
GeneWikii GroEL.
GenomeRNAii 3329.
NextBioi 13188.
PROi P10809.
SOURCEi Search...

Gene expression databases

Bgeei P10809.
CleanExi HS_HSPD1.
ExpressionAtlasi P10809. baseline and differential.
Genevestigatori P10809.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPi MF_00600. CH60.
InterProi IPR017998. Chaperone_TCP-1.
IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00298. CHAPERONIN60.
PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 1 hit.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02348. GroEL. 1 hit.
PROSITEi PS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen."
    Jindal S., Dudani A.K., Singh B., Harley C.B., Gupta R.S.
    Mol. Cell. Biol. 9:2279-2283(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families."
    Venner T.J., Singh B., Gupta R.S.
    DNA Cell Biol. 9:545-552(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter."
    Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H., Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.
    Hum. Genet. 112:71-77(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Genetic variation in immune response genes."
    Tan J., Ong R., Hibberd M.L., Seielstad M.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Adrenal gland and Spleen.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung, Skin and Uterus.
  8. "Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein)."
    Waldinger D., Eckerskorn C., Lottspeich F., Cleve H.
    Biol. Chem. Hoppe-Seyler 369:1185-1189(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-573.
  9. "Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis."
    Ward L.D., Hong J., Whitehead R.H., Simpson R.J.
    Electrophoresis 11:883-891(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-55.
    Tissue: Colon carcinoma.
  10. "Complex formation of human T-cell leukemia virus type I p40tax transactivator with cellular polypeptides."
    Nagata K., Ide Y., Takagi T., Ohtani K., Aoshima M., Tozawa H., Nakamura M., Sugamura K.
    J. Virol. 66:1040-1049(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-55, INTERACTION WITH HTLV-1 P40TAX.
  11. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
    Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
    Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-50.
    Tissue: Mammary carcinoma.
  12. "The human myocardial two-dimensional gel protein database: update 1994."
    Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
    Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46.
    Tissue: Heart.
  13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-37.
    Tissue: Platelet.
  14. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-35.
    Tissue: Liver.
  15. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 61-72, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 61-72; 206-218; 237-249; 251-290; 430-446 AND 463-469, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  17. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-121; 251-268 AND 430-446.
    Tissue: Adipocyte.
  18. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Colon carcinoma.
  19. Cited for: MITOCHONDRIAL IMPORT.
  20. "Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis."
    Tanaka Y., Kanai F., Kawakami T., Tateishi K., Ijichi H., Kawabe T., Arakawa Y., Kawakami T., Nishimura T., Shirakata Y., Koike K., Omata M.
    Biochem. Biophys. Res. Commun. 318:461-469(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV PROTEIN X.
  21. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "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.
  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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-125; LYS-130; LYS-202; LYS-218; LYS-269; LYS-352; LYS-359; LYS-396 AND LYS-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: MALONYLATION AT LYS-133.
  29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-expressed in cancer cells, that functions as dominant negative for the ubiquitous ATAD3A."
    Merle N., Feraud O., Gilquin B., Hubstenberger A., Kieffer-Jacquinot S., Assard N., Bennaceur-Griscelli A., Honnorat J., Baudier J.
    Mitochondrion 12:441-448(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATAD3A.
  31. "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: INTERACTION WITH METTL20 AND METTL21B.
  32. "Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60."
    Hansen J.J., Durr A., Cournu-Rebeix I., Georgopoulos C., Ang D., Nielsen M.N., Davoine C.-S., Brice A., Fontaine B., Gregersen N., Bross P.
    Am. J. Hum. Genet. 70:1328-1332(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG13 ILE-98.
  33. "Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy."
    Magen D., Georgopoulos C., Bross P., Ang D., Segev Y., Goldsher D., Nemirovski A., Shahar E., Ravid S., Luder A., Heno B., Gershoni-Baruch R., Skorecki K., Mandel H.
    Am. J. Hum. Genet. 83:30-42(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HLD4 GLY-29, CHARACTERIZATION OF VARIANT HLD4 GLY-29.

Entry informationi

Entry nameiCH60_HUMAN
AccessioniPrimary (citable) accession number: P10809
Secondary accession number(s): B2R5M6
, B7Z712, Q38L19, Q9UCR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 183 of the entry and version 2 of the sequence. [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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3