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Protein

ZZ-type zinc finger-containing protein 3

Gene

ZZZ3

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

Functioni

Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi680 – 70324H-T-H motifPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri817 – 86751ZZ-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
ZZ-type zinc finger-containing protein 3
Gene namesi
Name:ZZZ3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24523. ZZZ3.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134873184.

Polymorphism and mutation databases

BioMutaiZZZ3.
DMDMi74762495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 903903ZZ-type zinc finger-containing protein 3PRO_0000287495Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei394 – 3941N6-acetyllysineBy similarity
Cross-linki647 – 647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei701 – 7011N6-acetyllysineCombined sources
Cross-linki708 – 708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IYH5.
MaxQBiQ8IYH5.
PaxDbiQ8IYH5.
PRIDEiQ8IYH5.

PTM databases

iPTMnetiQ8IYH5.
PhosphoSiteiQ8IYH5.

Expressioni

Gene expression databases

BgeeiQ8IYH5.
CleanExiHS_ZZZ3.
ExpressionAtlasiQ8IYH5. baseline and differential.
GenevisibleiQ8IYH5. HS.

Interactioni

Subunit structurei

Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM124AQ86V423EBI-2795524,EBI-744506
Hoxa1P090223EBI-2795524,EBI-3957603From a different organism.
KAT2AQ928302EBI-2795524,EBI-477622

Protein-protein interaction databases

BioGridi117482. 40 interactions.
DIPiDIP-47289N.
IntActiQ8IYH5. 14 interactions.
MINTiMINT-7032149.
STRINGi9606.ENSP00000359837.

Structurei

Secondary structure

1
903
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi657 – 66913Combined sources
Helixi676 – 68712Combined sources
Beta strandi688 – 6903Combined sources
Helixi692 – 70312Combined sources
Helixi704 – 7063Combined sources
Beta strandi807 – 8093Combined sources
Beta strandi817 – 8204Combined sources
Beta strandi824 – 8263Combined sources
Beta strandi829 – 8335Combined sources
Beta strandi835 – 8417Combined sources
Beta strandi843 – 8453Combined sources
Beta strandi848 – 8503Combined sources
Helixi851 – 8533Combined sources
Beta strandi865 – 8673Combined sources
Beta strandi869 – 8724Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FC7NMR-A807-886[»]
2YUMNMR-A652-713[»]
ProteinModelPortaliQ8IYH5.
SMRiQ8IYH5. Positions 652-715, 807-875.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IYH5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini647 – 70761HTH myb-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH myb-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri817 – 86751ZZ-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IHEM. Eukaryota.
ENOG410ZINA. LUCA.
GeneTreeiENSGT00390000005307.
HOVERGENiHBG062668.
InParanoidiQ8IYH5.
OMAiKLEDHKI.
OrthoDBiEOG7SFHX8.
PhylomeDBiQ8IYH5.
TreeFamiTF106396.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IYH5-1) [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
MAASRSTRVT RSTVGLNGLD ESFCGRTLRN RSIAHPEEIS SNSQVRSRSP
60 70 80 90 100
KKRPEPVPIQ KGNNNGRTTD LKQQSTRESW VSPRKRGLSS SEKDNIERQA
110 120 130 140 150
IENCERRQTE PVSPVLKRIK RCLRSEAPNS SEEDSPIKSD KESVEQRSTV
160 170 180 190 200
VDNDADFQGT KRACRCLILD DCEKREIKKV NVSEEGPLNS AVVEEITGYL
210 220 230 240 250
AVNGVDDSDS AVINCDDCQP DGNTKQNSIG SYVLQEKSVA ENGDTDTQTS
260 270 280 290 300
MFLDSRKEDS YIDHKVPCTD SQVQVKLEDH KIVTACLPVE HVNQLTTEPA
310 320 330 340 350
TGPFSETQSS LRDSEEEVDV VGDSSASKEQ CKENTNNELD TSLESMPASG
360 370 380 390 400
EPEPSPVLDC VSAQMMSLSE PQEHRYTLRT SPRRAAPTRG SPTKNSSPYR
410 420 430 440 450
ENGQFEENNL SPNETNATVS DNVSQSPTNP GEISQNEKGI CCDSQNNGSE
460 470 480 490 500
GVSKPPSEAR LNIGHLPSAK ESASQHITEE EDDDPDVYYF ESDHVALKHN
510 520 530 540 550
KDYQRLLQTI AVLEAQRSQA VQDLESLGRH QREALKNPIG FVEKLQKKAD
560 570 580 590 600
IGLPYPQRVV QLPEIVWDQY THSLGNFERE FKNRKRHTRR VKLVFDKVGL
610 620 630 640 650
PARPKSPLDP KKDGESLSYS MLPLSDGPEG SSSRPQMIRG RLCDDTKPET
660 670 680 690 700
FNQLWTVEEQ KKLEQLLIKY PPEEVESRRW QKIADELGNR TAKQVASRVQ
710 720 730 740 750
KYFIKLTKAG IPVPGRTPNL YIYSKKSSTS RRQHPLNKHL FKPSTFMTSH
760 770 780 790 800
EPPVYMDEDD DRSCFHSHMN TAVEDASDDE SIPIMYRNLP EYKELLQFKK
810 820 830 840 850
LKKQKLQQMQ AESGFVQHVG FKCDNCGIEP IQGVRWHCQD CPPEMSLDFC
860 870 880 890 900
DSCSDCLHET DIHKEDHQLE PIYRSETFLD RDYCVSQGTS YNYLDPNYFP

ANR
Length:903
Mass (Da):102,023
Last modified:March 1, 2003 - v1
Checksum:i16ED137C0A8202EA
GO
Isoform 2 (identifier: Q8IYH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     598-598: Missing.

Show »
Length:902
Mass (Da):101,924
Checksum:iB7E306C19A1011D8
GO
Isoform 3 (identifier: Q8IYH5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-494: Missing.
     495-502: VALKHNKD → MIDLWLYS

Note: No experimental confirmation available.
Show »
Length:409
Mass (Da):47,716
Checksum:iE0ADB97A8D186009
GO
Isoform 4 (identifier: Q8IYH5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     661-683: KKLEQLLIKYPPEEVESRRWQKI → VINISKSCRLKKTSKQLTSESVL
     684-903: Missing.

Note: No experimental confirmation available.
Show »
Length:683
Mass (Da):76,126
Checksum:i50C9B12134DB1D66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti596 – 5961D → G in AAH35079 (PubMed:15489334).Curated
Sequence conflicti655 – 6551W → G in CAB45694 (PubMed:17974005).Curated
Sequence conflicti698 – 6981R → Q in AAH35079 (PubMed:15489334).Curated
Sequence conflicti721 – 7211Y → C in AAH35079 (PubMed:15489334).Curated
Sequence conflicti807 – 8071Q → R in CAE45800 (PubMed:17974005).Curated
Sequence conflicti877 – 8771T → A in CAE45870 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti456 – 4561P → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035718

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 494494Missing in isoform 3. 1 PublicationVSP_025509Add
BLAST
Alternative sequencei495 – 5028VALKHNKD → MIDLWLYS in isoform 3. 1 PublicationVSP_025510
Alternative sequencei598 – 5981Missing in isoform 2. 2 PublicationsVSP_025511
Alternative sequencei661 – 68323KKLEQ…RWQKI → VINISKSCRLKKTSKQLTSE SVL in isoform 4. 1 PublicationVSP_025512Add
BLAST
Alternative sequencei684 – 903220Missing in isoform 4. 1 PublicationVSP_025513Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL080063 mRNA. Translation: CAB45694.1.
BX641001 mRNA. Translation: CAE46004.1.
BX640658 mRNA. Translation: CAE45800.1.
BX640766 mRNA. Translation: CAE45870.1.
AC093575 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX06376.1.
BC035397 mRNA. Translation: AAH35397.1.
BC035079 mRNA. Translation: AAH35079.1.
BC035818 mRNA. Translation: AAH35818.1.
AK074119 mRNA. Translation: BAB84945.1.
CCDSiCCDS677.1. [Q8IYH5-1]
CCDS76172.1. [Q8IYH5-3]
PIRiT12463.
RefSeqiNP_001295166.1. NM_001308237.1. [Q8IYH5-3]
NP_056349.1. NM_015534.5. [Q8IYH5-1]
XP_005270782.1. XM_005270725.2. [Q8IYH5-1]
XP_005270783.1. XM_005270726.2. [Q8IYH5-1]
XP_005270784.1. XM_005270727.2. [Q8IYH5-2]
XP_005270786.1. XM_005270729.3. [Q8IYH5-3]
UniGeneiHs.480506.

Genome annotation databases

EnsembliENST00000370798; ENSP00000359834; ENSG00000036549. [Q8IYH5-3]
ENST00000370801; ENSP00000359837; ENSG00000036549. [Q8IYH5-1]
GeneIDi26009.
KEGGihsa:26009.
UCSCiuc001dhq.4. human. [Q8IYH5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL080063 mRNA. Translation: CAB45694.1.
BX641001 mRNA. Translation: CAE46004.1.
BX640658 mRNA. Translation: CAE45800.1.
BX640766 mRNA. Translation: CAE45870.1.
AC093575 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX06376.1.
BC035397 mRNA. Translation: AAH35397.1.
BC035079 mRNA. Translation: AAH35079.1.
BC035818 mRNA. Translation: AAH35818.1.
AK074119 mRNA. Translation: BAB84945.1.
CCDSiCCDS677.1. [Q8IYH5-1]
CCDS76172.1. [Q8IYH5-3]
PIRiT12463.
RefSeqiNP_001295166.1. NM_001308237.1. [Q8IYH5-3]
NP_056349.1. NM_015534.5. [Q8IYH5-1]
XP_005270782.1. XM_005270725.2. [Q8IYH5-1]
XP_005270783.1. XM_005270726.2. [Q8IYH5-1]
XP_005270784.1. XM_005270727.2. [Q8IYH5-2]
XP_005270786.1. XM_005270729.3. [Q8IYH5-3]
UniGeneiHs.480506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FC7NMR-A807-886[»]
2YUMNMR-A652-713[»]
ProteinModelPortaliQ8IYH5.
SMRiQ8IYH5. Positions 652-715, 807-875.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117482. 40 interactions.
DIPiDIP-47289N.
IntActiQ8IYH5. 14 interactions.
MINTiMINT-7032149.
STRINGi9606.ENSP00000359837.

PTM databases

iPTMnetiQ8IYH5.
PhosphoSiteiQ8IYH5.

Polymorphism and mutation databases

BioMutaiZZZ3.
DMDMi74762495.

Proteomic databases

EPDiQ8IYH5.
MaxQBiQ8IYH5.
PaxDbiQ8IYH5.
PRIDEiQ8IYH5.

Protocols and materials databases

DNASUi26009.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370798; ENSP00000359834; ENSG00000036549. [Q8IYH5-3]
ENST00000370801; ENSP00000359837; ENSG00000036549. [Q8IYH5-1]
GeneIDi26009.
KEGGihsa:26009.
UCSCiuc001dhq.4. human. [Q8IYH5-1]

Organism-specific databases

CTDi26009.
GeneCardsiZZZ3.
HGNCiHGNC:24523. ZZZ3.
neXtProtiNX_Q8IYH5.
PharmGKBiPA134873184.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHEM. Eukaryota.
ENOG410ZINA. LUCA.
GeneTreeiENSGT00390000005307.
HOVERGENiHBG062668.
InParanoidiQ8IYH5.
OMAiKLEDHKI.
OrthoDBiEOG7SFHX8.
PhylomeDBiQ8IYH5.
TreeFamiTF106396.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiZZZ3. human.
EvolutionaryTraceiQ8IYH5.
GeneWikiiZZZ3.
GenomeRNAii26009.
NextBioi47745.
PROiQ8IYH5.

Gene expression databases

BgeeiQ8IYH5.
CleanExiHS_ZZZ3.
ExpressionAtlasiQ8IYH5. baseline and differential.
GenevisibleiQ8IYH5. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-903 (ISOFORM 2).
    Tissue: Adipose tissue, Colon endothelium and Rectum tumor.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-903 (ISOFORM 2).
    Tissue: Brain, Lymph and Placenta.
  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] OF 161-903 (ISOFORM 4).
    Tissue: Spleen.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-131 AND SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
    Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
    Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
  9. "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-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647 AND LYS-708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Solution structure of the ZZ domain of ZZZ3 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 807-875 IN COMPLEX WITH ZINC IONS.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-456.

Entry informationi

Entry nameiZZZ3_HUMAN
AccessioniPrimary (citable) accession number: Q8IYH5
Secondary accession number(s): B7WPC6
, Q6N004, Q6N070, Q8IYP0, Q8IYR1, Q8TEK4, Q9Y4U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 137 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.