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P07901

- HS90A_MOUSE

UniProt

P07901 - HS90A_MOUSE

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Protein
Heat shock protein HSP 90-alpha
Gene
Hsp90aa1, Hsp86, Hsp86-1, Hspca
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATP By similarity
Binding sitei93 – 931ATP By similarity
Binding sitei112 – 1121ATP By similarity
Binding sitei138 – 1381ATP; via amide nitrogen By similarity
Binding sitei401 – 4011ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: Ensembl
  3. TPR domain binding Source: UniProtKB
  4. nitric-oxide synthase regulator activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: MGI
  7. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. chaperone-mediated protein complex assembly Source: Ensembl
  2. nitric oxide biosynthetic process Source: UniProtKB
  3. positive regulation of cytotoxic T cell differentiation Source: UniProtKB
  4. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  5. protein import into mitochondrial outer membrane Source: Ensembl
  6. protein refolding Source: UniProtKB
  7. regulation of catalytic activity Source: GOC
  8. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188191. Signaling by ERBB2.
REACT_196603. Scavenging by Class F Receptors.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_199123. Signaling by constitutively active EGFR.
REACT_213550. HSF1-dependent transactivation.
REACT_221264. eNOS activation.
REACT_223784. Attenuation phase.
REACT_225256. HSF1 activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha
Alternative name(s):
Heat shock 86 kDa
Short name:
HSP 86
Short name:
HSP86
Tumor-specific transplantation 86 kDa antigen
Short name:
TSTA
Gene namesi
Name:Hsp90aa1
Synonyms:Hsp86, Hsp86-1, Hspca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:96250. Hsp90aa1.

Subcellular locationi

Cytoplasm. Melanosome By similarity. Cell membrane By similarity 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. intracellular Source: MGI
  4. melanosome Source: UniProtKB-SubCell
  5. mitochondrion Source: GOC
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 733732Heat shock protein HSP 90-alphaUniRule annotation
PRO_0000062912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine; by PRKDCUniRule annotation
Modified residuei7 – 71Phosphothreonine; by PRKDCUniRule annotation
Modified residuei58 – 581N6-acetyllysine1 Publication
Modified residuei84 – 841N6-acetyllysine1 Publication
Modified residuei231 – 2311Phosphoserine By similarity
Modified residuei252 – 2521Phosphoserine By similarity
Modified residuei263 – 2631Phosphoserine3 Publications
Modified residuei314 – 3141Phosphotyrosine1 Publication
Modified residuei400 – 4001Phosphoserine By similarity
Modified residuei444 – 4441N6-acetyllysine By similarity
Modified residuei459 – 4591N6-acetyllysine By similarity
Modified residuei490 – 4901N6-acetyllysine By similarity
Modified residuei493 – 4931Phosphotyrosine1 Publication
Modified residuei586 – 5861N6-acetyllysine By similarity
Modified residuei599 – 5991S-nitrosocysteine By similarity

Post-translational modificationi

ISGylated.1 Publication
S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1 By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP07901.
PaxDbiP07901.
PRIDEiP07901.

2D gel databases

REPRODUCTION-2DPAGEP07901.

PTM databases

PhosphoSiteiP07901.

Expressioni

Gene expression databases

BgeeiP07901.
GenevestigatoriP07901.

Interactioni

Subunit structurei

Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 By similarity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Akt1P317506EBI-78930,EBI-298707
Itgb1bp2Q9R0005EBI-78930,EBI-7922331

Protein-protein interaction databases

BioGridi200455. 18 interactions.
DIPiDIP-30975N.
IntActiP07901. 25 interactions.
MINTiMINT-152660.

Structurei

3D structure databases

ProteinModelPortaliP07901.
SMRiP07901. Positions 11-700.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni683 – 73351Required for homodimerization By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi729 – 7335TPR repeat-bindingUniRule annotation

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP07901.
KOiK04079.
OMAiKEDQTEF.
OrthoDBiEOG780RM0.
PhylomeDBiP07901.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07901-1 [UniParc]FASTAAdd to Basket

« Hide

MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS    50
NSSDALDKIR YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK 100
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV 150
ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE 200
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE KEEEKEKEEK 250
ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR 300
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF 350
DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS 400
REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI 450
HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK 500
DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL 550
ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI 600
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK 650
AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID 700
EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD 733
Length:733
Mass (Da):84,788
Last modified:January 23, 2007 - v4
Checksum:iD92B8FD38A463B4E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71T → A in AAA37868. 1 Publication
Sequence conflicti242 – 2454Missing in AAA37868. 1 Publication
Sequence conflicti356 – 3561R → K in AAA37868. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04633 mRNA. Translation: AAA53068.1.
M57673 Genomic DNA. Translation: AAA37867.1.
BC046614 mRNA. Translation: AAH46614.1.
M36830 mRNA. Translation: AAA37868.1.
X16857 mRNA. Translation: CAA34748.1.
CCDSiCCDS26172.1.
PIRiB32848. HHMS86.
RefSeqiNP_034610.1. NM_010480.5.
UniGeneiMm.1843.
Mm.315997.
Mm.341186.
Mm.440626.
Mm.486334.

Genome annotation databases

EnsembliENSMUST00000021698; ENSMUSP00000021698; ENSMUSG00000021270.
ENSMUST00000094361; ENSMUSP00000091921; ENSMUSG00000021270.
GeneIDi15519.
KEGGimmu:15519.
UCSCiuc007pbq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04633 mRNA. Translation: AAA53068.1 .
M57673 Genomic DNA. Translation: AAA37867.1 .
BC046614 mRNA. Translation: AAH46614.1 .
M36830 mRNA. Translation: AAA37868.1 .
X16857 mRNA. Translation: CAA34748.1 .
CCDSi CCDS26172.1.
PIRi B32848. HHMS86.
RefSeqi NP_034610.1. NM_010480.5.
UniGenei Mm.1843.
Mm.315997.
Mm.341186.
Mm.440626.
Mm.486334.

3D structure databases

ProteinModelPortali P07901.
SMRi P07901. Positions 11-700.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200455. 18 interactions.
DIPi DIP-30975N.
IntActi P07901. 25 interactions.
MINTi MINT-152660.

Chemistry

BindingDBi P07901.
ChEMBLi CHEMBL4197.

PTM databases

PhosphoSitei P07901.

2D gel databases

REPRODUCTION-2DPAGE P07901.

Proteomic databases

MaxQBi P07901.
PaxDbi P07901.
PRIDEi P07901.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021698 ; ENSMUSP00000021698 ; ENSMUSG00000021270 .
ENSMUST00000094361 ; ENSMUSP00000091921 ; ENSMUSG00000021270 .
GeneIDi 15519.
KEGGi mmu:15519.
UCSCi uc007pbq.1. mouse.

Organism-specific databases

CTDi 3320.
MGIi MGI:96250. Hsp90aa1.

Phylogenomic databases

eggNOGi COG0326.
HOGENOMi HOG000031988.
HOVERGENi HBG007374.
InParanoidi P07901.
KOi K04079.
OMAi KEDQTEF.
OrthoDBi EOG780RM0.
PhylomeDBi P07901.
TreeFami TF300686.

Enzyme and pathway databases

Reactomei REACT_188191. Signaling by ERBB2.
REACT_196603. Scavenging by Class F Receptors.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_199123. Signaling by constitutively active EGFR.
REACT_213550. HSF1-dependent transactivation.
REACT_221264. eNOS activation.
REACT_223784. Attenuation phase.
REACT_225256. HSF1 activation.

Miscellaneous databases

NextBioi 288436.
PROi P07901.
SOURCEi Search...

Gene expression databases

Bgeei P07901.
Genevestigatori P07901.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins."
    Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.
    J. Biol. Chem. 264:5343-5351(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Mapping of the mouse 86-kDa heat-shock protein expressed gene (Hsp86-1) on chromosome 12 and related genes on chromosomes 3, 4, 9, and 11."
    Moore S.K., Appella E., Villar C.J., Kozak C.A.
    Genomics 10:1019-1029(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
  3. "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].
    Tissue: Retina.
  4. "A mouse tumor-specific transplantation antigen is a heat shock-related protein."
    Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.
    Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31.
  5. "The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
    Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
    Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, HOMODIMERIZATION.
  6. "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."
    Hoffmann T., Hovemann B.
    Gene 74:491-501(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-356.
  7. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  8. "High constitutive transcription of HSP86 gene in murine embryonal carcinoma cells."
    Legagneux V., Mezger V., Quelard C., Barnier J.V., Bensaude O., Morange M.
    Differentiation 41:42-48(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 460-733.
  9. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
    Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
    J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
  10. "Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus."
    Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.
    J. Biol. Chem. 276:14884-14889(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4.
  11. "A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins."
    Davies T.H., Ning Y.M., Sanchez E.R.
    J. Biol. Chem. 277:4597-4600(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A HETEROMULTIMERIC COMPLEX WITH NR3C1 AND FKBP4 OR FKBP5, SUBCELLULAR LOCATION.
  12. "The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."
    Lees-Miller S.P., Anderson C.W.
    J. Biol. Chem. 264:17275-17280(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PRKDC AT THR-5 AND THR-7.
  13. Cited for: ISGYLATION.
  14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  17. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHS90A_MOUSE
AccessioniPrimary (citable) accession number: P07901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 160 of the entry and version 4 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

External Data

Dasty 3

Similar proteinsi