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Q5TKR9

- KAT6A_RAT

UniProt

Q5TKR9 - KAT6A_RAT

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Protein

Histone acetyltransferase KAT6A

Gene

Kat6a

Organism
Rattus norvegicus (Rat)
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 sitei678 – 6781Proton donor/acceptorBy similarity
Binding sitei682 – 6821Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri199 – 25860PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri255 – 30652PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri536 – 55823C2HC-typeAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. cellular senescence Source: UniProtKB
  2. histone acetylation Source: UniProtKB
  3. histone H3 acetylation Source: UniProtKB
  4. myeloid cell differentiation Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. nucleosome assembly Source: InterPro
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. protein acetylation Source: UniProtKB
  9. 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

Enzyme and pathway databases

ReactomeiREACT_198384. HATs acetylate histones.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1304892. 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 – 19981998Histone acetyltransferase KAT6APRO_0000051574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysineBy similarity
Modified residuei350 – 3501N6-acetyllysineBy similarity
Modified residuei355 – 3551N6-acetyllysineBy similarity
Modified residuei369 – 3691Phosphothreonine; by PKB/AKT1By similarity
Modified residuei471 – 4711PhosphoserineBy similarity
Modified residuei602 – 6021N6-acetyllysine; by autocatalysisBy similarity
Modified residuei815 – 8151N6-acetyllysineBy similarity
Modified residuei900 – 9001Phosphotyrosine1 Publication
Modified residuei1006 – 10061N6-acetyllysineBy similarity
Modified residuei1114 – 11141PhosphoserineBy similarity

Post-translational modificationi

Autoacetylated. Autoacetylation at Lys-602 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

PaxDbiQ5TKR9.
PRIDEiQ5TKR9.

PTM databases

PhosphoSiteiQ5TKR9.

Expressioni

Gene expression databases

GenevestigatoriQ5TKR9.

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. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037279.

Structurei

3D structure databases

ProteinModelPortaliQ5TKR9.
SMRiQ5TKR9. Positions 505-777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 17177H15PROSITE-ProRule annotationAdd
BLAST
Domaini502 – 776275MYST-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 – 662519Interaction with PMLBy similarityAdd
BLAST
Regioni312 – 662351Interaction with RUNX1-1By similarityAdd
BLAST
Regioni486 – 776291CatalyticBy similarityAdd
BLAST
Regioni505 – 808304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activityBy similarityAdd
BLAST
Regioni643 – 6475Acetyl-CoA bindingBy similarity
Regioni652 – 6587Acetyl-CoA bindingBy similarity
Regioni1510 – 1735226Interaction with PMLBy similarityAdd
BLAST
Regioni1510 – 1635126Interaction with RUNX1-2By similarityAdd
BLAST
Regioni1907 – 194236Required for activation of RUNX1-2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi988 – 9947Poly-Glu
Compositional biasi1018 – 10258Poly-Arg
Compositional biasi1028 – 110679Glu-richAdd
BLAST
Compositional biasi1107 – 11137Poly-Glu
Compositional biasi1141 – 116828Lys-richAdd
BLAST
Compositional biasi1231 – 12377Poly-Glu
Compositional biasi1262 – 12709Poly-Glu
Compositional biasi1463 – 1583121Ser-richAdd
BLAST
Compositional biasi1586 – 15905Poly-Ser
Compositional biasi1593 – 169199Gln-richAdd
BLAST
Compositional biasi1665 – 16728Poly-Pro
Compositional biasi1676 – 16805Poly-Pro
Compositional biasi1684 – 16907Poly-Pro
Compositional biasi1884 – 196481Met-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 fingeri199 – 25860PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri255 – 30652PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri536 – 55823C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ5TKR9.
KOiK11305.
OrthoDBiEOG7WHH8N.
PhylomeDBiQ5TKR9.
TreeFamiTF106483.

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.

Q5TKR9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ
60 70 80 90 100
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN
110 120 130 140 150
KLLKRAFEGL AESGGSTLKS IERFLKSQKD VSAACGGTAA SGFHQQLRLA
160 170 180 190 200
IKRAVGHGRL LKDGPLYRLN TKAANAEGKE GCESLSCLPP VSLLPHEKDK
210 220 230 240 250
PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS CLKFSPELTV
260 270 280 290 300
RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
310 320 330 340 350
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK
360 370 380 390 400
GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK
410 420 430 440 450
FNKKTKGLID GLTKFFTPSP DGRKARGEAV DYSELRIRKK GNRKSSTSHW
460 470 480 490 500
PTDNQDGWES KQESEERLFG SQEIMTERDM ELFRDIQEQA LQKVGVTGPP
510 520 530 540 550
DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF CLKYMKSRTI
560 570 580 590 600
LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD
610 620 630 640 650
HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ
660 670 680 690 700
YQRKGYGRFL IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC
710 720 730 740 750
LYHQNDKQIS IKKLSKLTGV CPQDITSTLH HLRMLDFRSD QFVIIRREKL
760 770 780 790 800
IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS NSVVSEEEDE EADDGEKEEP
810 820 830 840 850
QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE LASSSRLSKQ
860 870 880 890 900
ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY
910 920 930 940 950
GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL
960 970 980 990 1000
KKSPETLKCR LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS
1010 1020 1030 1040 1050
PPVLTKPTLK RKKPILHRRR RVRKRKHHNS SVVTETISET TEVLDEPFED
1060 1070 1080 1090 1100
SDSERPMPRL EPTFEIEEEE EEEDENELFP RGYFHCLSSQ DILRCQASSK
1110 1120 1130 1140 1150
RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE PDTSTPMKKK
1160 1170 1180 1190 1200
KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR
1210 1220 1230 1240 1250
KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL
1260 1270 1280 1290 1300
DSSNSPDADP KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE
1310 1320 1330 1340 1350
ANQNEDHDAD DEDDGHLDSL KTKEPEGQPA REDGTEEPGT QESFLDASIQ
1360 1370 1380 1390 1400
DSRENAKDKD ETEADSEEEQ PSHEASVGSE TMPGSEEDHE EDSNTKEELI
1410 1420 1430 1440 1450
ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE ETLAACQTLQ
1460 1470 1480 1490 1500
SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES
1510 1520 1530 1540 1550
GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE
1560 1570 1580 1590 1600
STTENYENPS SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ
1610 1620 1630 1640 1650
QMASMGNSCS MLQQNSVQPA TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP
1660 1670 1680 1690 1700
PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP QQQPQPPPPP QQQPPLSQCS
1710 1720 1730 1740 1750
MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ PSATFSLAKL
1760 1770 1780 1790 1800
QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA
1810 1820 1830 1840 1850
QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS
1860 1870 1880 1890 1900
IRSKSAPLPS ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT
1910 1920 1930 1940 1950
PAYNVNSMNM NTLNAMNSYR MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG
1960 1970 1980 1990
MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY MNAAGVPKQS LNGPYMRR
Length:1,998
Mass (Da):223,331
Last modified:July 5, 2005 - v2
Checksum:i37092EED5475855D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03100194 Genomic DNA. No translation available.
AB195309 mRNA. Translation: BAD72833.1.
RefSeqiNP_001094040.1. NM_001100570.1.
UniGeneiRn.33802.

Genome annotation databases

GeneIDi306571.
KEGGirno:306571.
UCSCiRGD:1304892. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03100194 Genomic DNA. No translation available.
AB195309 mRNA. Translation: BAD72833.1 .
RefSeqi NP_001094040.1. NM_001100570.1.
UniGenei Rn.33802.

3D structure databases

ProteinModelPortali Q5TKR9.
SMRi Q5TKR9. Positions 505-777.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000037279.

PTM databases

PhosphoSitei Q5TKR9.

Proteomic databases

PaxDbi Q5TKR9.
PRIDEi Q5TKR9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 306571.
KEGGi rno:306571.
UCSCi RGD:1304892. rat.

Organism-specific databases

CTDi 7994.
RGDi 1304892. Kat6a.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q5TKR9.
KOi K11305.
OrthoDBi EOG7WHH8N.
PhylomeDBi Q5TKR9.
TreeFami TF106483.

Enzyme and pathway databases

Reactomei REACT_198384. HATs acetylate histones.

Miscellaneous databases

NextBioi 656228.
PROi Q5TKR9.

Gene expression databases

Genevestigatori Q5TKR9.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Cloning and characterization of a cDNA encoding histone acetyltransferase MOZ (monocytic leukemia zinc finger protein) from rat."
    Ohta K., Osada S., Nishikawa J., Nishihara T.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1998.
    Strain: Wistar.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAT6A_RAT
AccessioniPrimary (citable) accession number: Q5TKR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 95 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3