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Q5TKR9

- KAT6A_RAT

UniProt

Q5TKR9 - KAT6A_RAT

Protein

Histone acetyltransferase KAT6A

Gene

Kat6a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    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].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei602 – 6021By similarity
    Active sitei644 – 6441NucleophileBy 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

    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:2.3.1.48)
    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. nucleolus Source: UniProtKB-SubCell
    3. nucleosome Source: InterPro
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB

    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.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

    MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ     50
    LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN 100
    KLLKRAFEGL AESGGSTLKS IERFLKSQKD VSAACGGTAA SGFHQQLRLA 150
    IKRAVGHGRL LKDGPLYRLN TKAANAEGKE GCESLSCLPP VSLLPHEKDK 200
    PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS CLKFSPELTV 250
    RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
    PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK 350
    GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK 400
    FNKKTKGLID GLTKFFTPSP DGRKARGEAV DYSELRIRKK GNRKSSTSHW 450
    PTDNQDGWES KQESEERLFG SQEIMTERDM ELFRDIQEQA LQKVGVTGPP 500
    DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF CLKYMKSRTI 550
    LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD 600
    HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ 650
    YQRKGYGRFL IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC 700
    LYHQNDKQIS IKKLSKLTGV CPQDITSTLH HLRMLDFRSD QFVIIRREKL 750
    IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS NSVVSEEEDE EADDGEKEEP 800
    QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE LASSSRLSKQ 850
    ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY 900
    GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL 950
    KKSPETLKCR LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS 1000
    PPVLTKPTLK RKKPILHRRR RVRKRKHHNS SVVTETISET TEVLDEPFED 1050
    SDSERPMPRL EPTFEIEEEE EEEDENELFP RGYFHCLSSQ DILRCQASSK 1100
    RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE PDTSTPMKKK 1150
    KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR 1200
    KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL 1250
    DSSNSPDADP KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE 1300
    ANQNEDHDAD DEDDGHLDSL KTKEPEGQPA REDGTEEPGT QESFLDASIQ 1350
    DSRENAKDKD ETEADSEEEQ PSHEASVGSE TMPGSEEDHE EDSNTKEELI 1400
    ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE ETLAACQTLQ 1450
    SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES 1500
    GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE 1550
    STTENYENPS SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ 1600
    QMASMGNSCS MLQQNSVQPA TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP 1650
    PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP QQQPQPPPPP QQQPPLSQCS 1700
    MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ PSATFSLAKL 1750
    QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA 1800
    QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS 1850
    IRSKSAPLPS ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT 1900
    PAYNVNSMNM NTLNAMNSYR MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG 1950
    MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY MNAAGVPKQS LNGPYMRR 1998
    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

    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 1, 2014
    This is version 94 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