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Q6NZM9

- HDAC4_MOUSE

UniProt

Q6NZM9 - HDAC4_MOUSE

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Protein

Histone deacetylase 4

Gene

Hdac4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D By similarity.By similarity

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi664 – 6641ZincBy similarity
Metal bindingi666 – 6661ZincBy similarity
Metal bindingi672 – 6721ZincBy similarity
Metal bindingi743 – 7431ZincBy similarity
Active sitei795 – 7951By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  7. protein deacetylase activity Source: MGI
  8. protein kinase binding Source: UniProtKB
  9. transcription corepressor activity Source: MGI
  10. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of cell proliferation Source: MGI
  2. negative regulation of glycolytic process Source: BHF-UCL
  3. negative regulation of osteoblast differentiation Source: MGI
  4. negative regulation of transcription, DNA-templated Source: MGI
  5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  6. osteoblast development Source: MGI
  7. positive regulation of protein sumoylation Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: BHF-UCL
  9. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  10. protein deacetylation Source: GOC
  11. regulation of cardiac muscle contraction by calcium ion signaling Source: MGI
  12. regulation of skeletal muscle fiber development Source: MGI
  13. regulation of striated muscle cell differentiation Source: MGI
  14. response to denervation involved in regulation of muscle adaptation Source: BHF-UCL
  15. skeletal system development Source: MGI
  16. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 4 (EC:3.5.1.98)
Short name:
HD4
Gene namesi
Name:Hdac4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:3036234. Hdac4.

Subcellular locationi

Nucleus. Cytoplasm
Note: Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-245, Ser-465 and Ser-629 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation By similarity.By similarity

GO - Cellular componenti

  1. actomyosin Source: MGI
  2. cytoplasm Source: BHF-UCL
  3. cytosol Source: MGI
  4. histone deacetylase complex Source: InterPro
  5. neuromuscular junction Source: MGI
  6. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10761076Histone deacetylase 4PRO_0000281033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451Phosphoserine; by CaMK4 and SIK11 Publication
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei465 – 4651Phosphoserine; by CaMK4 and SIK12 Publications
Cross-linki556 – 556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei629 – 6291Phosphoserine; by CaMK4By similarity
Modified residuei630 – 6301PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-349 impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3 By similarity.By similarity
Sumoylation on Lys-556 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6NZM9.
PaxDbiQ6NZM9.
PRIDEiQ6NZM9.

PTM databases

PhosphoSiteiQ6NZM9.

Expressioni

Gene expression databases

BgeeiQ6NZM9.
CleanExiMM_HDAC4.
GenevestigatoriQ6NZM9.

Interactioni

Subunit structurei

Interacts with HDAC7. Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B. Interacts with KDM5B. Interacts with ANKRA2. Interacts with EP300 in the presence of TFAP2C By similarity. Interacts with AHRR. Interacts with MYOCD.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Runx2Q087753EBI-646397,EBI-903354

Protein-protein interaction databases

BioGridi229009. 14 interactions.
DIPiDIP-36317N.
IntActiQ6NZM9. 6 interactions.
MINTiMINT-5183788.

Structurei

3D structure databases

ProteinModelPortaliQ6NZM9.
SMRiQ6NZM9. Positions 62-128, 649-1023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 312196Interaction with MEF2ABy similarityAdd
BLAST
Regioni652 – 1076425Histone deacetylaseBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 169104Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1043 – 107634Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi464 – 49936Gln-richAdd
BLAST
Compositional biasi561 – 5688Poly-Glu

Domaini

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ6NZM9.
KOiK11406.
OMAiVSFGGHR.
OrthoDBiEOG7RFTH5.
PhylomeDBiQ6NZM9.
TreeFamiTF106174.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6NZM9-1) [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
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPTAVPMD
60 70 80 90 100
LRLDHQFSLP LEPALREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS
110 120 130 140 150
RQHEAQLHEH IKQQQEMLAM KHQQELLEHQ RKLERHRQEQ ELEKQHREQK
160 170 180 190 200
LQQLKNKEKG KESAVASTEV KMKLQEFVLN KKKALAHRNL NHCISSDPRY
210 220 230 240 250
WYGKTQHSSL DQSSPPQSGV SASYNHPVLG MYDAKDDFPL RKTASEPNLK
260 270 280 290 300
LRSRLKQKVA ERRSSPLLRR KDGPVATALK KRPLDVTDSA CSSAPGSGPS
310 320 330 340 350
SPNSSSGNVS TENGIAPTVP SAPAETSLAH RLVTREGSVA PLPLYTSPSL
360 370 380 390 400
PNITLGLPAT GPAAGAAGQQ DAERLALPAL QQRILFPGTH LTPYLSTSPL
410 420 430 440 450
ERDGAAAHNP LLQHMVLLEQ PPTQTPLVTG LGALPLHSQS LVGADRVSPS
460 470 480 490 500
IHKLRQHRPL GRTQSAPLPQ NAQALQHLVI QQQHQQFLEK HKQQFQQQQL
510 520 530 540 550
HLSKIISKPS EPPRQPESHP EETEEELREH QALLDEPYLD RLPGQKEPSL
560 570 580 590 600
AGVQVKQEPI ESEEEEAEAT RETEPGQRPA TEQELLFRQQ ALLLEQQRIH
610 620 630 640 650
QLRNYQASME AAGIPVSFGS HRPLSRAQSS PASATFPMSV QEPPTKPRFT
660 670 680 690 700
TGLVYDTLML KHQCTCGNTN SHPEHAGRIQ SIWSRLQETG LRGKCECIRG
710 720 730 740 750
RKATLEELQT VHSEAHTLLY GTNPLNRQKL DSSLTSVFVR LPCGGVGVDS
760 770 780 790 800
DTIWNEVHSS GAARLAVGCV VELVFKVATG ELKNGFAVVR PPGHHAEEST
810 820 830 840 850
PMGFCYFNSV AVAAKLLQQR LNVSKILIVD WDVHHGNGTQ QAFYNDPNVL
860 870 880 890 900
YMSLHRYDDG NFFPGSGAPD EVGTGPGVGF NVNMAFTGGL EPPMGDAEYL
910 920 930 940 950
AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK
960 970 980 990 1000
QLMGLAGGRL VLALEGGHDL TAICDASEAC VSALLGNELE PLPEKVLHQR
1010 1020 1030 1040 1050
PNANAVHSME KVMDIHSKYW RCLQRLSSTV GHSLIEAQKC EKEEAETVTA
1060 1070
MASLSVGVKP AEKRSEEEPM EEEPPL
Length:1,076
Mass (Da):118,562
Last modified:July 5, 2004 - v1
Checksum:iA3CCC3CCCBB903A0
GO
Isoform 2 (identifier: Q6NZM9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: Missing.
     732-732: S → SKKLLG

Note: No experimental confirmation available.

Show »
Length:910
Mass (Da):99,124
Checksum:i80C1A8CA5567EE19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti569 – 5691A → S in BAE33147. (PubMed:16141072)Curated
Sequence conflicti904 – 9041R → K in BAE33147. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 171171Missing in isoform 2. 1 PublicationVSP_023952Add
BLAST
Alternative sequencei732 – 7321S → SKKLLG in isoform 2. 1 PublicationVSP_023953

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK029933 mRNA. Translation: BAE43272.1.
AK155250 mRNA. Translation: BAE33147.1.
AK162369 mRNA. Translation: BAE36877.1.
BC066052 mRNA. Translation: AAH66052.1.
CCDSiCCDS48324.1. [Q6NZM9-1]
RefSeqiNP_997108.1. NM_207225.1. [Q6NZM9-1]
UniGeneiMm.318567.

Genome annotation databases

EnsembliENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313. [Q6NZM9-1]
ENSMUST00000097644; ENSMUSP00000095249; ENSMUSG00000026313. [Q6NZM9-1]
GeneIDi208727.
KEGGimmu:208727.
UCSCiuc007cbe.2. mouse. [Q6NZM9-2]
uc007cbf.2. mouse. [Q6NZM9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK029933 mRNA. Translation: BAE43272.1 .
AK155250 mRNA. Translation: BAE33147.1 .
AK162369 mRNA. Translation: BAE36877.1 .
BC066052 mRNA. Translation: AAH66052.1 .
CCDSi CCDS48324.1. [Q6NZM9-1 ]
RefSeqi NP_997108.1. NM_207225.1. [Q6NZM9-1 ]
UniGenei Mm.318567.

3D structure databases

ProteinModelPortali Q6NZM9.
SMRi Q6NZM9. Positions 62-128, 649-1023.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229009. 14 interactions.
DIPi DIP-36317N.
IntActi Q6NZM9. 6 interactions.
MINTi MINT-5183788.

PTM databases

PhosphoSitei Q6NZM9.

Proteomic databases

MaxQBi Q6NZM9.
PaxDbi Q6NZM9.
PRIDEi Q6NZM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000008995 ; ENSMUSP00000008995 ; ENSMUSG00000026313 . [Q6NZM9-1 ]
ENSMUST00000097644 ; ENSMUSP00000095249 ; ENSMUSG00000026313 . [Q6NZM9-1 ]
GeneIDi 208727.
KEGGi mmu:208727.
UCSCi uc007cbe.2. mouse. [Q6NZM9-2 ]
uc007cbf.2. mouse. [Q6NZM9-1 ]

Organism-specific databases

CTDi 9759.
MGIi MGI:3036234. Hdac4.

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062809.
HOGENOMi HOG000232065.
HOVERGENi HBG057100.
InParanoidi Q6NZM9.
KOi K11406.
OMAi VSFGGHR.
OrthoDBi EOG7RFTH5.
PhylomeDBi Q6NZM9.
TreeFami TF106174.

Miscellaneous databases

NextBioi 372399.
PROi Q6NZM9.
SOURCEi Search...

Gene expression databases

Bgeei Q6NZM9.
CleanExi MM_HDAC4.
Genevestigatori Q6NZM9.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell, Epididymis and Testis.
  2. "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).
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin."
    Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N.
    Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYOCD.
  4. "Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5."
    Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.
    Biochem. Biophys. Res. Commun. 364:276-282(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHRR.
  5. "CaMKIIdelta isoforms differentially affect calcium handling but similarly regulate HDAC/MEF2 transcriptional responses."
    Zhang T., Kohlhaas M., Backs J., Mishra S., Phillips W., Dybkova N., Chang S., Ling H., Bers D.M., Maier L.S., Olson E.N., Brown J.H.
    J. Biol. Chem. 282:35078-35087(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMK2D.
  6. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
    Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
    Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-465 AND SER-465.
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHDAC4_MOUSE
AccessioniPrimary (citable) accession number: Q6NZM9
Secondary accession number(s): Q3TRZ9, Q3U2J3, Q3V3Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 93 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, 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