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Q8BZ21

- KAT6A_MOUSE

UniProt

Q8BZ21 - KAT6A_MOUSE

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Protein

Histone acetyltransferase KAT6A

Gene

Kat6a

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

Functioni

Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2 By similarity. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML By similarity.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei679 – 6791Proton donor/acceptorBy similarity
Binding sitei683 – 6831Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri262 – 31352PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri537 – 55923C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. chromatin binding Source: MGI
  3. DNA binding Source: UniProtKB
  4. histone acetyltransferase activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. aorta morphogenesis Source: MGI
  2. cellular senescence Source: UniProtKB
  3. embryonic hemopoiesis Source: MGI
  4. face morphogenesis Source: MGI
  5. heart morphogenesis Source: MGI
  6. histone acetylation Source: UniProtKB
  7. histone H3 acetylation Source: UniProtKB
  8. myeloid cell differentiation Source: UniProtKB
  9. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. nucleosome assembly Source: InterPro
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. protein acetylation Source: UniProtKB
  14. somatic stem cell maintenance Source: MGI
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6A (EC:2.3.1.48By similarity)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name:
MYST-3
Monocytic leukemia zinc finger homolog
Monocytic leukemia zinc finger protein
Gene namesi
Name:Kat6a
Synonyms:Moz, Myst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2442415. Kat6a.

Subcellular locationi

Nucleus PROSITE-ProRule annotation. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. NucleusPML body By similarity
Note: Recruited into PML body after DNA damage.By similarity

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. nucleosome Source: InterPro
  3. nucleus Source: UniProtKB
  4. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20032003Histone acetyltransferase KAT6APRO_0000051573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei350 – 3501N6-acetyllysineBy similarity
Modified residuei355 – 3551N6-acetyllysineBy similarity
Modified residuei369 – 3691Phosphothreonine; by PKB/AKT1By similarity
Modified residuei472 – 4721PhosphoserineBy similarity
Modified residuei603 – 6031N6-acetyllysine; by autocatalysisBy similarity
Modified residuei813 – 8131N6-acetyllysine1 Publication
Modified residuei816 – 8161N6-acetyllysine1 Publication
Modified residuei901 – 9011PhosphotyrosineBy similarity
Modified residuei1007 – 10071N6-acetyllysineBy similarity
Modified residuei1115 – 11151PhosphoserineBy similarity

Post-translational modificationi

Autoacetylated. Autoacetylation at Lys-603 is required for proper function.By similarity
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BZ21.
PRIDEiQ8BZ21.

PTM databases

PhosphoSiteiQ8BZ21.

Expressioni

Gene expression databases

GenevestigatoriQ8BZ21.

Interactioni

Subunit structurei

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 By similarity. Interacts with RUNX2 By similarity. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with p53/TP53 By similarity. Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53 By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BZ21.
SMRiQ8BZ21. Positions 194-315, 506-778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 17177H15PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 777275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144Required for activation of RUNX1-1By similarityAdd
BLAST
Regioni52 – 166115Required for nuclear localizationBy similarityAdd
BLAST
Regioni144 – 663520Interaction with PMLBy similarityAdd
BLAST
Regioni312 – 663352Interaction with RUNX1-1By similarityAdd
BLAST
Regioni487 – 777291CatalyticBy similarityAdd
BLAST
Regioni506 – 809304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activityBy similarityAdd
BLAST
Regioni644 – 6485Acetyl-CoA bindingBy similarity
Regioni653 – 6597Acetyl-CoA bindingBy similarity
Regioni1511 – 1740230Interaction with PMLBy similarityAdd
BLAST
Regioni1511 – 1636126Interaction with RUNX1-2By similarityAdd
BLAST
Regioni1912 – 194736Required for activation of RUNX1-2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi989 – 9957Poly-Glu
Compositional biasi1019 – 10268Poly-Arg
Compositional biasi1066 – 107914Poly-GluAdd
BLAST
Compositional biasi1107 – 11148Poly-Glu
Compositional biasi1149 – 117628Lys-richAdd
BLAST
Compositional biasi1232 – 12387Poly-Glu
Compositional biasi1405 – 14084Poly-Glu
Compositional biasi1471 – 1591121Ser-richAdd
BLAST
Compositional biasi1601 – 1703103Gln-richAdd
BLAST
Compositional biasi1896 – 197681Met-richAdd
BLAST

Domaini

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri262 – 31352PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri537 – 55923C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BZ21.
PhylomeDBiQ8BZ21.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BZ21-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ
60 70 80 90 100
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN
110 120 130 140 150
KLLKRAFEGL AETGGSTLKS IERFLKSQKD VSAACGGSAA PGFHQQLRLA
160 170 180 190 200
IKRAVGHGRL LKDGPLYRLN TKAASAEGKE GCESLSCLPP VSLLPHEKDK
210 220 230 240 250
PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS CLKFSPELTV
260 270 280 290 300
RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
310 320 330 340 350
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK
360 370 380 390 400
GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK
410 420 430 440 450
FNKKTKGLID GLTKFFTPSP DGRKARGEVV DYSEQYRIRK KGNRKSSTSD
460 470 480 490 500
WPTDNQDGWE SKQENEERLF GSQEIMTERD MELFRDIQEQ ALQKVGVTGP
510 520 530 540 550
PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE FCLKYMKSRT
560 570 580 590 600
ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL
610 620 630 640 650
DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP
660 670 680 690 700
QYQRKGYGRF LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE
710 720 730 740 750
CLYHQNDKQI SIKKLSKLTG VCPQDITSTL HHLRMLDFRS DQFVIIRREK
760 770 780 790 800
LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV SNSVVSEDED EEADEGEKEE
810 820 830 840 850
PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK ELASSSRLSK
860 870 880 890 900
QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ
910 920 930 940 950
YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ
960 970 980 990 1000
LKKSPETLKC RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN
1010 1020 1030 1040 1050
SPPILTKPTL KRKKPILHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE
1060 1070 1080 1090 1100
DSDSERPMPR LEPTFEMEEE EEEEEEESEL FPRGYFHCLS SQDILRCQSS
1110 1120 1130 1140 1150
SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL EPDTSTPMKK
1160 1170 1180 1190 1200
KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG
1210 1220 1230 1240 1250
RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP
1260 1270 1280 1290 1300
LDSSNSPEAE PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT
1310 1320 1330 1340 1350
EANQNEDHDA DDEDEGHLDS LKTKEPEEQP AREDDKEEPG IQGSFLAANM
1360 1370 1380 1390 1400
QDSRENTKDK DEAEPDSEED QPSHEASVVS ETMPGSEEDH EEDSNTKEEL
1410 1420 1430 1440 1450
IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC EETLAACQTL
1460 1470 1480 1490 1500
QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE
1510 1520 1530 1540 1550
SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI
1560 1570 1580 1590 1600
ESTTENYENP SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT
1610 1620 1630 1640 1650
QQMANMGNSC SMLQQNTVQP AANCNIKSPQ TCVVERPPSN QQPPPPPPPP
1660 1670 1680 1690 1700
PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ QQPPPPQQQP QPPPPQQQPP
1710 1720 1730 1740 1750
LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA GSYSQPSATF
1760 1770 1780 1790 1800
SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA
1810 1820 1830 1840 1850
GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV
1860 1870 1880 1890 1900
KGHISIRSKS APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV
1910 1920 1930 1940 1950
NLMPTPAYNV NSMNMNTLNA MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM
1960 1970 1980 1990 2000
QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP SHHSYMNAAG VPKQSLNGPY

MRR
Length:2,003
Mass (Da):224,919
Last modified:July 5, 2005 - v2
Checksum:i93D0D687A1621B31
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC115361 Genomic DNA. No translation available.
AK028058 mRNA. Translation: BAC25728.1.
AK036885 mRNA. Translation: BAC29621.1.
AK039615 mRNA. Translation: BAC30401.1.
AK054322 mRNA. Translation: BAC35729.1.
CCDSiCCDS40294.1.
UniGeneiMm.182776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC115361 Genomic DNA. No translation available.
AK028058 mRNA. Translation: BAC25728.1 .
AK036885 mRNA. Translation: BAC29621.1 .
AK039615 mRNA. Translation: BAC30401.1 .
AK054322 mRNA. Translation: BAC35729.1 .
CCDSi CCDS40294.1.
UniGenei Mm.182776.

3D structure databases

ProteinModelPortali Q8BZ21.
SMRi Q8BZ21. Positions 194-315, 506-778.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BZ21.

Proteomic databases

MaxQBi Q8BZ21.
PRIDEi Q8BZ21.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:2442415. Kat6a.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q8BZ21.
PhylomeDBi Q8BZ21.

Miscellaneous databases

ChiTaRSi KAT6A. mouse.
PROi Q8BZ21.
SOURCEi Search...

Gene expression databases

Genevestigatori Q8BZ21.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEi PS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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] OF 1-1010.
    Strain: C57BL/6J.
    Tissue: Cerebellum, Ovary, Spinal cord and Vagina.
  3. "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
    Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
    EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUNX1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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-172; LYS-813 AND LYS-816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKAT6A_MOUSE
AccessioniPrimary (citable) accession number: Q8BZ21
Secondary accession number(s): Q8BW52, Q8BYH1, Q8C1F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 109 of the entry and version 2 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