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O95251

- KAT7_HUMAN

UniProt

O95251 - KAT7_HUMAN

Protein

Histone acetyltransferase KAT7

Gene

KAT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Specifically represses AR-mediated transcription.4 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei432 – 4321By similarity
    Active sitei474 – 4741NucleophileBy similarity
    Binding sitei477 – 4771Acetyl-CoABy similarity
    Binding sitei512 – 5121Acetyl-CoABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri366 – 38823C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. DNA replication Source: UniProtKB
    3. histone H3 acetylation Source: UniProtKB
    4. histone H4-K12 acetylation Source: UniProtKB
    5. histone H4-K5 acetylation Source: UniProtKB
    6. histone H4-K8 acetylation Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: ProtInc
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    DNA replication, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT7 (EC:2.3.1.48)
    Alternative name(s):
    Histone acetyltransferase binding to ORC1
    Lysine acetyltransferase 7
    MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2
    Short name:
    MYST-2
    Gene namesi
    Name:KAT7
    Synonyms:HBO1, HBOa, MYST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17016. KAT7.

    Subcellular locationi

    Nucleusnucleoplasm 3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. histone acetyltransferase complex Source: UniProtKB
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi371 – 3711C → A: No interaction with MCM2 and ORC1L. 1 Publication

    Organism-specific databases

    PharmGKBiPA134886407.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Histone acetyltransferase KAT7PRO_0000051569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei57 – 571Phosphoserine; by PLK14 Publications
    Modified residuei85 – 851Phosphothreonine; by CDK13 Publications
    Modified residuei88 – 881Phosphothreonine; by CDK15 Publications
    Modified residuei102 – 1021Phosphoserine3 Publications
    Modified residuei124 – 1241Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine2 Publications
    Modified residuei164 – 1641Phosphoserine1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei277 – 2771N6-acetyllysineBy similarity
    Modified residuei432 – 4321N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei506 – 5061Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior Phosphorylation at Thr-85 and Thr-88 by CDK1.6 Publications
    Autoacetylation at Lys-432 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95251.
    PaxDbiO95251.
    PRIDEiO95251.

    PTM databases

    PhosphoSiteiO95251.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in testis.2 Publications

    Gene expression databases

    ArrayExpressiO95251.
    BgeeiO95251.
    CleanExiHS_MYST2.
    GenevestigatoriO95251.

    Organism-specific databases

    HPAiHPA044470.

    Interactioni

    Subunit structurei

    Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with MCM2 and ORC1L. Interacts with the androgen receptor (AR) in the presence of dihydrotestosterone.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102755EBI-473199,EBI-608057
    BARD1Q997282EBI-473199,EBI-473181
    KIAA1377Q9P2H02EBI-473199,EBI-473176
    VIMP086704EBI-473199,EBI-353844

    Protein-protein interaction databases

    BioGridi116315. 55 interactions.
    DIPiDIP-29697N.
    IntActiO95251. 30 interactions.
    MINTiMINT-141769.
    STRINGi9606.ENSP00000259021.

    Structurei

    3D structure databases

    ProteinModelPortaliO95251.
    SMRiO95251. Positions 183-211, 340-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini332 – 607276MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni482 – 4887Acetyl-CoA bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 5748Ser-richAdd
    BLAST

    Domaini

    The C2HC-type zinc finger is required for interaction with MCM2 and ORC1L.1 Publication
    The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction.By similarity

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri366 – 38823C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    HOGENOMiHOG000182457.
    HOVERGENiHBG053268.
    InParanoidiO95251.
    KOiK11307.
    OMAiVYSTRRV.
    OrthoDBiEOG7WHH8N.
    PhylomeDBiO95251.
    TreeFamiTF317619.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    IPR015880. Znf_C2H2-like.
    IPR002515. Znf_C2HC.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF01530. zf-C2HC. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95251-1) [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

    MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS    50
    QSSQDSSPVR NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS 100
    GSETEQVVDF SDRETKNTAD HDESPPRTPT GNAPSSESDI DISSPNVSHD 150
    ESIAKDMSLK DSGSDLSHRP KRRRFHESYN FNMKCPTPGC NSLGHLTGKH 200
    ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ DDNNRHATRH 250
    QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN 300
    LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW 350
    YHSPYPEEYA RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR 400
    KGSISVFEVD GKKNKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD 450
    NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ YMRQGYGKML IDFSYLLSKV 500
    EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS IKEISQETAV 550
    NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP 600
    SCLKWTPPKG T 611
    Length:611
    Mass (Da):70,642
    Last modified:May 1, 1999 - v1
    Checksum:i8368E7C4F07D8D7C
    GO
    Isoform 2 (identifier: O95251-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-193: Missing.
         222-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:501
    Mass (Da):58,136
    Checksum:i005414956B922380
    GO
    Isoform 3 (identifier: O95251-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         55-113: Missing.
         114-193: Missing.
         222-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:442
    Mass (Da):51,440
    Checksum:iEF5AA3D8E63B35D0
    GO
    Isoform 4 (identifier: O95251-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         222-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:581
    Mass (Da):66,947
    Checksum:i30A3E4C3E47EFBED
    GO
    Isoform 5 (identifier: O95251-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         55-113: Missing.
         114-193: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:472
    Mass (Da):55,135
    Checksum:i906F630E44BAFD2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 447Missing in BAG57945. (PubMed:14702039)Curated
    Sequence conflicti41 – 411R → Q in BAG57346. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei55 – 11359Missing in isoform 3 and isoform 5. 1 PublicationVSP_042552Add
    BLAST
    Alternative sequencei114 – 19380Missing in isoform 2, isoform 3 and isoform 5. 1 PublicationVSP_042553Add
    BLAST
    Alternative sequencei222 – 25130Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_042554Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074606 mRNA. Translation: AAC99368.1.
    AF140360 mRNA. Translation: AAD42348.1.
    AF217502 mRNA. Translation: AAL56649.1.
    AK023890 mRNA. Translation: BAG51236.1.
    AK293976 mRNA. Translation: BAG57346.1.
    AK294014 mRNA. Translation: BAG57375.1.
    AK294052 mRNA. Translation: BAG57401.1.
    AK294836 mRNA. Translation: BAG57945.1.
    AC015795 Genomic DNA. No translation available.
    AC027801 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94658.1.
    CH471109 Genomic DNA. Translation: EAW94659.1.
    BC032640 mRNA. Translation: AAH32640.1.
    CCDSiCCDS11554.1. [O95251-1]
    CCDS56035.1. [O95251-4]
    CCDS56036.1. [O95251-2]
    CCDS56037.1. [O95251-5]
    CCDS56038.1. [O95251-3]
    RefSeqiNP_001186084.1. NM_001199155.1. [O95251-4]
    NP_001186085.1. NM_001199156.1. [O95251-5]
    NP_001186086.1. NM_001199157.1. [O95251-2]
    NP_001186087.1. NM_001199158.1. [O95251-3]
    NP_008998.1. NM_007067.4. [O95251-1]
    UniGeneiHs.21907.

    Genome annotation databases

    EnsembliENST00000259021; ENSP00000259021; ENSG00000136504. [O95251-1]
    ENST00000424009; ENSP00000398961; ENSG00000136504. [O95251-4]
    ENST00000454930; ENSP00000413415; ENSG00000136504. [O95251-5]
    ENST00000509773; ENSP00000424577; ENSG00000136504. [O95251-2]
    ENST00000510819; ENSP00000423385; ENSG00000136504. [O95251-3]
    GeneIDi11143.
    KEGGihsa:11143.
    UCSCiuc002ipl.2. human.
    uc002ipm.3. human. [O95251-1]
    uc010wmb.2. human. [O95251-2]
    uc010wmc.2. human. [O95251-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074606 mRNA. Translation: AAC99368.1 .
    AF140360 mRNA. Translation: AAD42348.1 .
    AF217502 mRNA. Translation: AAL56649.1 .
    AK023890 mRNA. Translation: BAG51236.1 .
    AK293976 mRNA. Translation: BAG57346.1 .
    AK294014 mRNA. Translation: BAG57375.1 .
    AK294052 mRNA. Translation: BAG57401.1 .
    AK294836 mRNA. Translation: BAG57945.1 .
    AC015795 Genomic DNA. No translation available.
    AC027801 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94658.1 .
    CH471109 Genomic DNA. Translation: EAW94659.1 .
    BC032640 mRNA. Translation: AAH32640.1 .
    CCDSi CCDS11554.1. [O95251-1 ]
    CCDS56035.1. [O95251-4 ]
    CCDS56036.1. [O95251-2 ]
    CCDS56037.1. [O95251-5 ]
    CCDS56038.1. [O95251-3 ]
    RefSeqi NP_001186084.1. NM_001199155.1. [O95251-4 ]
    NP_001186085.1. NM_001199156.1. [O95251-5 ]
    NP_001186086.1. NM_001199157.1. [O95251-2 ]
    NP_001186087.1. NM_001199158.1. [O95251-3 ]
    NP_008998.1. NM_007067.4. [O95251-1 ]
    UniGenei Hs.21907.

    3D structure databases

    ProteinModelPortali O95251.
    SMRi O95251. Positions 183-211, 340-607.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116315. 55 interactions.
    DIPi DIP-29697N.
    IntActi O95251. 30 interactions.
    MINTi MINT-141769.
    STRINGi 9606.ENSP00000259021.

    PTM databases

    PhosphoSitei O95251.

    Proteomic databases

    MaxQBi O95251.
    PaxDbi O95251.
    PRIDEi O95251.

    Protocols and materials databases

    DNASUi 11143.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259021 ; ENSP00000259021 ; ENSG00000136504 . [O95251-1 ]
    ENST00000424009 ; ENSP00000398961 ; ENSG00000136504 . [O95251-4 ]
    ENST00000454930 ; ENSP00000413415 ; ENSG00000136504 . [O95251-5 ]
    ENST00000509773 ; ENSP00000424577 ; ENSG00000136504 . [O95251-2 ]
    ENST00000510819 ; ENSP00000423385 ; ENSG00000136504 . [O95251-3 ]
    GeneIDi 11143.
    KEGGi hsa:11143.
    UCSCi uc002ipl.2. human.
    uc002ipm.3. human. [O95251-1 ]
    uc010wmb.2. human. [O95251-2 ]
    uc010wmc.2. human. [O95251-3 ]

    Organism-specific databases

    CTDi 11143.
    GeneCardsi GC17P047867.
    HGNCi HGNC:17016. KAT7.
    HPAi HPA044470.
    MIMi 609880. gene.
    neXtProti NX_O95251.
    PharmGKBi PA134886407.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000182457.
    HOVERGENi HBG053268.
    InParanoidi O95251.
    KOi K11307.
    OMAi VYSTRRV.
    OrthoDBi EOG7WHH8N.
    PhylomeDBi O95251.
    TreeFami TF317619.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    GeneWikii MYST2.
    GenomeRNAii 11143.
    NextBioi 42360.
    PROi O95251.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95251.
    Bgeei O95251.
    CleanExi HS_MYST2.
    Genevestigatori O95251.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    IPR015880. Znf_C2H2-like.
    IPR002515. Znf_C2HC.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF01530. zf-C2HC. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein."
      Iizuka M., Stillman B.
      J. Biol. Chem. 274:23027-23034(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ORC1L, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Epithelium.
    2. "Androgen receptor interacts with a novel MYST protein, HBO1."
      Sharma M., Zarnegar M., Li X., Lim B., Sun Z.
      J. Biol. Chem. 275:35200-35208(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR, FUNCTION.
      Tissue: Prostate.
    3. "Cloning and identifying histone acetyltransferase HBOa."
      Jian J., Guangtao L., Guangwei D., Yan Z., Jianhe C., Jiangang Y., Boqin Q.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."
      Borrow J., Housman D.E.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
      Tissue: Brain, Cerebellum and Thyroid.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Lymph.
    9. "Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1."
      Burke T.W., Cook J.G., Asano M., Nevins J.R.
      J. Biol. Chem. 276:15397-15408(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM2 AND ORC1L, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-371.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX, INTERACTION WITH MCM2, SUBCELLULAR LOCATION.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57; THR-85; THR-88 AND SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Role for Plk1 phosphorylation of Hbo1 in regulation of replication licensing."
      Wu Z.Q., Liu X.
      Proc. Natl. Acad. Sci. U.S.A. 105:1919-1924(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-57 BY PLK1, PHOSPHORYLATION AT THR-85 AND THR-88 BY CDK1.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-85; THR-88 AND SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-88; SER-102; SER-124; SER-162 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKAT7_HUMAN
    AccessioniPrimary (citable) accession number: O95251
    Secondary accession number(s): B3KN74
    , B4DF85, B4DFB4, B4DFE0, B4DGY4, E7ER15, G5E9K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3