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O95251

- KAT7_HUMAN

UniProt

O95251 - KAT7_HUMAN

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Protein

Histone acetyltransferase KAT7

Gene

KAT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 sitei508 – 5081Proton donor/acceptorBy similarity
Binding sitei512 – 5121Acetyl-CoABy similarity
Binding sitei521 – 5211Acetyl-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. sequence-specific DNA binding transcription factor activity Source: InterPro
  3. 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
Complete GO annotation...

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:2.3.1.481 Publication)
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
Complete GO annotation...

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

BgeeiO95251.
CleanExiHS_MYST2.
ExpressionAtlasiO95251. baseline and differential.
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. 31 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
Regioni475 – 4773Acetyl-CoA bindingBy similarity
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.
GeneTreeiENSGT00550000074503.
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

        10         20         30         40         50
MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS
60 70 80 90 100
QSSQDSSPVR NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS
110 120 130 140 150
GSETEQVVDF SDRETKNTAD HDESPPRTPT GNAPSSESDI DISSPNVSHD
160 170 180 190 200
ESIAKDMSLK DSGSDLSHRP KRRRFHESYN FNMKCPTPGC NSLGHLTGKH
210 220 230 240 250
ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ DDNNRHATRH
260 270 280 290 300
QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN
310 320 330 340 350
LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW
360 370 380 390 400
YHSPYPEEYA RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR
410 420 430 440 450
KGSISVFEVD GKKNKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD
460 470 480 490 500
NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ YMRQGYGKML IDFSYLLSKV
510 520 530 540 550
EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS IKEISQETAV
560 570 580 590 600
NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP
610
SCLKWTPPKG T
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 31 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.
GeneTreei ENSGT00550000074503.
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

Bgeei O95251.
CleanExi HS_MYST2.
ExpressionAtlasi O95251. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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