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Protein

60 kDa heat shock protein, mitochondrial

Gene

Hspd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial
Alternative name(s):
60 kDa chaperonin
Chaperonin 60
Short name:
CPN60
HSP-65
Heat shock protein 60
Short name:
HSP-60
Short name:
Hsp60
Mitochondrial matrix protein P1
Gene namesi
Name:Hspd1
Synonyms:Hsp60
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:96242. Hspd1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • coated pit Source: MGI
  • coated vesicle Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • early endosome Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • Golgi apparatus Source: Ensembl
  • intracellular membrane-bounded organelle Source: MGI
  • lipopolysaccharide receptor complex Source: MGI
  • membrane Source: ParkinsonsUK-UCL
  • membrane raft Source: Ensembl
  • mitochondrial crista Source: Ensembl
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • plasma membrane Source: MGI
  • protein complex Source: UniProtKB
  • rough endoplasmic reticulum Source: Ensembl
  • secretory granule Source: MGI
  • zymogen granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Mitochondrion1 PublicationAdd
BLAST
Chaini27 – 57354760 kDa heat shock protein, mitochondrialPRO_0000005027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311N6-succinyllysineCombined sources
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei70 – 701PhosphoserineCombined sources
Modified residuei75 – 751N6-acetyllysineCombined sources
Modified residuei82 – 821N6-acetyllysine; alternateBy similarity
Modified residuei82 – 821N6-succinyllysine; alternateCombined sources
Modified residuei87 – 871N6-acetyllysineCombined sources
Modified residuei90 – 901PhosphotyrosineBy similarity
Modified residuei91 – 911N6-acetyllysineCombined sources
Modified residuei125 – 1251N6-acetyllysine; alternateCombined sources
Modified residuei125 – 1251N6-succinyllysine; alternateCombined sources
Modified residuei130 – 1301N6-acetyllysineCombined sources
Modified residuei133 – 1331N6-acetyllysine; alternateCombined sources
Modified residuei133 – 1331N6-malonyllysine; alternateBy similarity
Modified residuei133 – 1331N6-succinyllysine; alternateCombined sources
Modified residuei156 – 1561N6-acetyllysineCombined sources
Modified residuei191 – 1911N6-acetyllysine; alternateCombined sources
Modified residuei191 – 1911N6-succinyllysine; alternateCombined sources
Modified residuei202 – 2021N6-acetyllysine; alternateCombined sources
Modified residuei202 – 2021N6-succinyllysine; alternateCombined sources
Modified residuei205 – 2051N6-acetyllysine; alternateCombined sources
Modified residuei205 – 2051N6-succinyllysine; alternateCombined sources
Modified residuei218 – 2181N6-acetyllysine; alternateCombined sources
Modified residuei218 – 2181N6-succinyllysine; alternateCombined sources
Modified residuei236 – 2361N6-acetyllysine; alternateCombined sources
Modified residuei236 – 2361N6-succinyllysine; alternateCombined sources
Modified residuei249 – 2491N6-acetyllysineCombined sources
Modified residuei250 – 2501N6-acetyllysine; alternateCombined sources
Modified residuei250 – 2501N6-succinyllysine; alternateCombined sources
Modified residuei269 – 2691N6-acetyllysineCombined sources
Modified residuei292 – 2921N6-acetyllysineCombined sources
Modified residuei301 – 3011N6-succinyllysineCombined sources
Modified residuei314 – 3141N6-acetyllysineCombined sources
Modified residuei352 – 3521N6-acetyllysine; alternateCombined sources
Modified residuei352 – 3521N6-succinyllysine; alternateCombined sources
Modified residuei359 – 3591N6-acetyllysineCombined sources
Modified residuei389 – 3891N6-acetyllysineCombined sources
Modified residuei396 – 3961N6-acetyllysine; alternateBy similarity
Modified residuei396 – 3961N6-succinyllysine; alternateCombined sources
Modified residuei410 – 4101PhosphoserineCombined sources
Modified residuei455 – 4551N6-acetyllysine; alternateCombined sources
Modified residuei455 – 4551N6-succinyllysine; alternateCombined sources
Modified residuei469 – 4691N6-acetyllysineCombined sources
Modified residuei481 – 4811N6-acetyllysine; alternateCombined sources
Modified residuei481 – 4811N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63038.
MaxQBiP63038.
PaxDbiP63038.
PRIDEiP63038.
TopDownProteomicsiP63038-1. [P63038-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00308885.
P63038.
SWISS-2DPAGEP63038.
UCD-2DPAGEP19227.
P63038.

PTM databases

iPTMnetiP63038.
SwissPalmiP63038.

Miscellaneous databases

PMAP-CutDBP63038.

Expressioni

Gene expression databases

BgeeiP63038.
CleanExiMM_HSPD1.
ExpressionAtlasiP63038. baseline and differential.
GenevisibleiP63038. MM.

Interactioni

Subunit structurei

Interacts with ATAD3A (By similarity). Interacts with ETFBKMT and METTL21B (By similarity). Interacts with HRAS.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200451. 14 interactions.
DIPiDIP-31396N.
IntActiP63038. 21 interactions.
MINTiMINT-1860238.
STRINGi10090.ENSMUSP00000027123.

Structurei

3D structure databases

ProteinModelPortaliP63038.
SMRiP63038. Positions 27-550.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
HOVERGENiHBG001982.
InParanoidiP63038.
KOiK04077.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiP63038.
TreeFamiTF300475.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. 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. AlignAdd to basket

Isoform 1 (identifier: P63038-1) [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
MLRLPTVLRQ MRPVSRALAP 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 DIGNIISDAM KKVGRKGVIT
210 220 230 240 250
VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK
260 270 280 290 300
ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
310 320 330 340 350
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV
360 370 380 390 400
TKDDAMLLKG KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG
410 420 430 440 450
VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA
460 470 480 490 500
LDSLKPANED QKIGIEIIKR ALKIPAMTIA KNAGVEGSLI VEKILQSSSE
510 520 530 540 550
VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEAVVTEIP
560 570
KEEKDPGMGA MGGMGGGMGG GMF
Length:573
Mass (Da):60,955
Last modified:August 31, 2004 - v1
Checksum:i0014B58B77D0127B
GO
Isoform 2 (identifier: P63038-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Note: No experimental confirmation available.
Show »
Length:258
Mass (Da):27,015
Checksum:iDD79DC2838C3771B
GO

Sequence cautioni

The sequence AAI06113.1 differs from that shown.. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → H AA sequence (PubMed:1347942).Curated
Sequence conflicti139 – 1391E → K AA sequence (PubMed:1347942).Curated
Sequence conflicti251 – 2511I → F in CAA37653 (PubMed:1979012).Curated
Sequence conflicti364 – 3641K → E in BAC40607 (PubMed:16141072).Curated
Sequence conflicti518 – 5181I → V in CAA38762 (PubMed:2263486).Curated
Sequence conflicti527 – 5271T → Q AA sequence (PubMed:1347942).Curated
Sequence conflicti547 – 5471T → V AA sequence (PubMed:1347942).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 315315Missing in isoform 2. 1 PublicationVSP_025020Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55023 mRNA. Translation: CAA38762.1.
AK088844 mRNA. Translation: BAC40607.1.
AK143882 mRNA. Translation: BAE25581.1.
AK146831 mRNA. Translation: BAE27466.1.
BC016400 mRNA. Translation: AAH16400.1.
BC018545 mRNA. Translation: AAH18545.1.
BC106112 mRNA. Translation: AAI06113.1. Sequence problems.
X53584 mRNA. Translation: CAA37653.1.
CCDSiCCDS35569.1. [P63038-1]
PIRiS13084. HHMS60.
RefSeqiNP_034607.3. NM_010477.4. [P63038-1]
XP_006495769.1. XM_006495706.1. [P63038-1]
UniGeneiMm.1777.
Mm.439809.

Genome annotation databases

EnsembliENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980. [P63038-1]
GeneIDi15510.
KEGGimmu:15510.
UCSCiuc007bab.2. mouse. [P63038-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55023 mRNA. Translation: CAA38762.1.
AK088844 mRNA. Translation: BAC40607.1.
AK143882 mRNA. Translation: BAE25581.1.
AK146831 mRNA. Translation: BAE27466.1.
BC016400 mRNA. Translation: AAH16400.1.
BC018545 mRNA. Translation: AAH18545.1.
BC106112 mRNA. Translation: AAI06113.1. Sequence problems.
X53584 mRNA. Translation: CAA37653.1.
CCDSiCCDS35569.1. [P63038-1]
PIRiS13084. HHMS60.
RefSeqiNP_034607.3. NM_010477.4. [P63038-1]
XP_006495769.1. XM_006495706.1. [P63038-1]
UniGeneiMm.1777.
Mm.439809.

3D structure databases

ProteinModelPortaliP63038.
SMRiP63038. Positions 27-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200451. 14 interactions.
DIPiDIP-31396N.
IntActiP63038. 21 interactions.
MINTiMINT-1860238.
STRINGi10090.ENSMUSP00000027123.

PTM databases

iPTMnetiP63038.
SwissPalmiP63038.

2D gel databases

REPRODUCTION-2DPAGEIPI00308885.
P63038.
SWISS-2DPAGEP63038.
UCD-2DPAGEP19227.
P63038.

Proteomic databases

EPDiP63038.
MaxQBiP63038.
PaxDbiP63038.
PRIDEiP63038.
TopDownProteomicsiP63038-1. [P63038-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980. [P63038-1]
GeneIDi15510.
KEGGimmu:15510.
UCSCiuc007bab.2. mouse. [P63038-1]

Organism-specific databases

CTDi3329.
MGIiMGI:96242. Hspd1.

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
HOVERGENiHBG001982.
InParanoidiP63038.
KOiK04077.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiP63038.
TreeFamiTF300475.

Miscellaneous databases

ChiTaRSiHspd1. mouse.
NextBioi288418.
PMAP-CutDBP63038.
PROiP63038.
SOURCEiSearch...

Gene expression databases

BgeeiP63038.
CleanExiMM_HSPD1.
ExpressionAtlasiP63038. baseline and differential.
GenevisibleiP63038. MM.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of a murine cDNA clone encoding one member of the hsp65 multigene family."
    Loetscher E., Allison J.P.
    Nucleic Acids Res. 18:7153-7153(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Thymus.
  2. "An interaction between p21ras and heat shock protein hsp60, a chaperonin."
    Ikawa S., Weinberg R.A.
    Proc. Natl. Acad. Sci. U.S.A. 89:2012-2016(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 527-548, INTERACTION WITH HRAS.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Heart, Kidney and Thymus.
  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] (ISOFORMS 1 AND 2).
    Strain: 129 and FVB/N.
    Tissue: Mammary tumor.
  5. "Nucleotide sequence of mouse HSP60 (chaperonin, GroEL homolog) cDNA."
    Venner T.J., Gupta R.S.
    Biochim. Biophys. Acta 1087:336-338(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-573 (ISOFORM 1).
    Strain: BALB/cJ.
    Tissue: Fibroblast.
  6. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
    Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
    Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-47.
    Tissue: Fibroblast.
  7. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Strain: C57BL/6J and OF1.
    Tissue: Brain and Hippocampus.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-82; LYS-125; LYS-133; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-250; LYS-301; LYS-352; LYS-396; LYS-455 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  11. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-87; LYS-91; LYS-125; LYS-130; LYS-133; LYS-156; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-249; LYS-250; LYS-269; LYS-292; LYS-314; LYS-352; LYS-359; LYS-389; LYS-455; LYS-469 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCH60_MOUSE
AccessioniPrimary (citable) accession number: P63038
Secondary accession number(s): P19226
, P19227, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.