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Q14CW9

- AT7L3_HUMAN

UniProt

Q14CW9 - AT7L3_HUMAN

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Protein

Ataxin-7-like protein 3

Gene

ATXN7L3

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

Functioni

Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex.2 PublicationsUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri84 – 10522SGF11-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  2. transcription coactivator activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone deubiquitination Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Ataxin-7-like protein 3UniRule annotation
Alternative name(s):
SAGA-associated factor 11 homologUniRule annotation
Gene namesi
Name:ATXN7L3UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:25416. ATXN7L3.

Subcellular locationi

Nucleus UniRule annotation

GO - Cellular componenti

  1. DUBm complex Source: UniProtKB-HAMAP
  2. SAGA complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134991793.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Ataxin-7-like protein 3PRO_0000278301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei129 – 1291Phosphoserine1 Publication
Modified residuei131 – 1311Phosphoserine1 Publication
Modified residuei278 – 2781Phosphoserine1 Publication
Modified residuei281 – 2811Phosphoserine4 Publications
Modified residuei326 – 3261Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14CW9.
PaxDbiQ14CW9.
PRIDEiQ14CW9.

PTM databases

PhosphoSiteiQ14CW9.

Expressioni

Gene expression databases

BgeeiQ14CW9.
CleanExiHS_ATXN7L3.
ExpressionAtlasiQ14CW9. baseline.
GenevestigatoriQ14CW9.

Organism-specific databases

HPAiHPA050625.
HPA052419.

Interactioni

Subunit structurei

Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ENY2 and USP22.3 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi121289. 29 interactions.
IntActiQ14CW9. 6 interactions.
MINTiMINT-6774236.
STRINGi9606.ENSP00000397259.

Structurei

Secondary structure

1
347
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi199 – 2046
Turni205 – 2073
Turni214 – 2174
Beta strandi226 – 2283
Helixi231 – 24111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KKTNMR-A197-276[»]
ProteinModelPortaliQ14CW9.
SMRiQ14CW9. Positions 198-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14CW9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 26368SCA7UniRule annotationAdd
BLAST

Domaini

The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.1 PublicationUniRule annotation
The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module.UniRule annotation

Sequence similaritiesi

Belongs to the SGF11 family.UniRule annotation
Contains 1 SCA7 domain.UniRule annotation
Contains 1 SGF11-type zinc finger.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri84 – 10522SGF11-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG271996.
GeneTreeiENSGT00390000012202.
HOGENOMiHOG000006954.
HOVERGENiHBG071455.
InParanoidiQ14CW9.
KOiK11363.
OMAiPFKYSNS.
PhylomeDBiQ14CW9.
TreeFamiTF324580.

Family and domain databases

HAMAPiMF_03047. Sgf11.
InterProiIPR013246. SAGA_su_Sgf11.
IPR013243. SCA7_dom.
[Graphical view]
PfamiPF08313. SCA7. 1 hit.
PF08209. Sgf11. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14CW9) [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
MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL
60 70 80 90 100
DDTDPDSMKD FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP
110 120 130 140 150
HLEKCLGMGR NSSRIANRRI ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK
160 170 180 190 200
KAKKRKSDKN PNSPRRSKSL KHKNGELSNS DPFKYNNSTG ISYETLGPEE
210 220 230 240 250
LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY FLGPSAVLPE
260 270 280 290 300
VESSLDNDSF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT
310 320 330 340
NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN
Length:347
Mass (Da):38,651
Last modified:August 22, 2006 - v1
Checksum:i742D85BFF4ADD0C0
GO
Isoform 2 (identifier: Q14CW9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: K → KLWYLPFQ

Show »
Length:354
Mass (Da):39,599
Checksum:iEDB618080F2200D6
GO

Sequence cautioni

The sequence AAH37418.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB71070.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 1591K → KLWYLPFQ in isoform 2. 1 PublicationVSP_036721

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC037418 mRNA. Translation: AAH37418.1. Different initiation.
BC113595 mRNA. Translation: AAI13596.1.
BC126113 mRNA. Translation: AAI26114.1.
AK056002 mRNA. Translation: BAB71070.1. Different initiation.
AL390158 mRNA. Translation: CAB99093.1.
CCDSiCCDS42345.1. [Q14CW9-1]
CCDS45697.1. [Q14CW9-2]
RefSeqiNP_001092303.1. NM_001098833.1. [Q14CW9-1]
NP_064603.1. NM_020218.1. [Q14CW9-2]
UniGeneiHs.512651.

Genome annotation databases

EnsembliENST00000389384; ENSP00000374035; ENSG00000087152. [Q14CW9-1]
ENST00000454077; ENSP00000397259; ENSG00000087152. [Q14CW9-2]
GeneIDi56970.
KEGGihsa:56970.
UCSCiuc002ifz.3. human. [Q14CW9-2]
uc002iga.3. human. [Q14CW9-1]

Polymorphism databases

DMDMi121948758.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC037418 mRNA. Translation: AAH37418.1 . Different initiation.
BC113595 mRNA. Translation: AAI13596.1 .
BC126113 mRNA. Translation: AAI26114.1 .
AK056002 mRNA. Translation: BAB71070.1 . Different initiation.
AL390158 mRNA. Translation: CAB99093.1 .
CCDSi CCDS42345.1. [Q14CW9-1 ]
CCDS45697.1. [Q14CW9-2 ]
RefSeqi NP_001092303.1. NM_001098833.1. [Q14CW9-1 ]
NP_064603.1. NM_020218.1. [Q14CW9-2 ]
UniGenei Hs.512651.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KKT NMR - A 197-276 [» ]
ProteinModelPortali Q14CW9.
SMRi Q14CW9. Positions 198-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121289. 29 interactions.
IntActi Q14CW9. 6 interactions.
MINTi MINT-6774236.
STRINGi 9606.ENSP00000397259.

PTM databases

PhosphoSitei Q14CW9.

Polymorphism databases

DMDMi 121948758.

Proteomic databases

MaxQBi Q14CW9.
PaxDbi Q14CW9.
PRIDEi Q14CW9.

Protocols and materials databases

DNASUi 56970.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389384 ; ENSP00000374035 ; ENSG00000087152 . [Q14CW9-1 ]
ENST00000454077 ; ENSP00000397259 ; ENSG00000087152 . [Q14CW9-2 ]
GeneIDi 56970.
KEGGi hsa:56970.
UCSCi uc002ifz.3. human. [Q14CW9-2 ]
uc002iga.3. human. [Q14CW9-1 ]

Organism-specific databases

CTDi 56970.
GeneCardsi GC17M042269.
HGNCi HGNC:25416. ATXN7L3.
HPAi HPA050625.
HPA052419.
neXtProti NX_Q14CW9.
PharmGKBi PA134991793.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271996.
GeneTreei ENSGT00390000012202.
HOGENOMi HOG000006954.
HOVERGENi HBG071455.
InParanoidi Q14CW9.
KOi K11363.
OMAi PFKYSNS.
PhylomeDBi Q14CW9.
TreeFami TF324580.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTracei Q14CW9.
GenomeRNAii 56970.
NextBioi 62612.
PROi Q14CW9.

Gene expression databases

Bgeei Q14CW9.
CleanExi HS_ATXN7L3.
ExpressionAtlasi Q14CW9. baseline.
Genevestigatori Q14CW9.

Family and domain databases

HAMAPi MF_03047. Sgf11.
InterProi IPR013246. SAGA_su_Sgf11.
IPR013243. SCA7_dom.
[Graphical view ]
Pfami PF08313. SCA7. 1 hit.
PF08209. Sgf11. 1 hit.
[Graphical view ]
PROSITEi PS51505. SCA7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-347 (ISOFORM 2).
    Tissue: Lymph.
  2. "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 123-347 (ISOFORM 1).
    Tissue: Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-347.
    Tissue: Amygdala.
  4. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
    Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
    Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH ENY2 AND USP22, DOMAIN.
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-278 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-281 AND SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements."
    Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M., Devys D., Tora L.
    Mol. Cell. Biol. 31:3734-3744(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
  10. "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-129; SER-131 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties."
    Bonnet J., Wang Y.H., Spedale G., Atkinson R.A., Romier C., Hamiche A., Pijnappel W.W., Timmers H.T., Tora L., Devys D., Kieffer B.
    EMBO Rep. 11:612-618(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 197-276 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiAT7L3_HUMAN
AccessioniPrimary (citable) accession number: Q14CW9
Secondary accession number(s): Q8IY68, Q96N40, Q9NPU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: August 22, 2006
Last modified: October 29, 2014
This is version 77 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3