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Q14CW9 (AT7L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-7-like protein 3
Alternative name(s):
SAGA-associated factor 11 homolog
Gene names
Name:ATXN7L3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.9

Subunit structure

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. Ref.4 Ref.9

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03047.

Domain

The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. Ref.4

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 By similarity. Ref.4

Sequence similarities

Belongs to the SGF11 family.

Contains 1 SCA7 domain.

Contains 1 SGF11-type zinc finger.

Sequence caution

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

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14CW9-1)

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.
Isoform 2 (identifier: Q14CW9-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Ataxin-7-like protein 3 HAMAP-Rule MF_03047
PRO_0000278301

Regions

Domain196 – 26368SCA7
Zinc finger84 – 10522SGF11-type HAMAP-Rule MF_03047

Amino acid modifications

Modified residue1291Phosphoserine Ref.10
Modified residue1311Phosphoserine Ref.10
Modified residue2781Phosphoserine Ref.7
Modified residue2811Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10
Modified residue3261Phosphoserine Ref.8

Natural variations

Alternative sequence1591K → KLWYLPFQ in isoform 2.
VSP_036721

Secondary structure

.......... 347
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 742D85BFF4ADD0C0

FASTA34738,651
        10         20         30         40         50         60 
MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL DDTDPDSMKD 

        70         80         90        100        110        120 
FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI 

       130        140        150        160        170        180 
ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSDKN PNSPRRSKSL KHKNGELSNS 

       190        200        210        220        230        240 
DPFKYNNSTG ISYETLGPEE LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY 

       250        260        270        280        290        300 
FLGPSAVLPE VESSLDNDSF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT 

       310        320        330        340 
NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN 

« Hide

Isoform 2 [UniParc].

Checksum: EDB618080F2200D6
Show »

FASTA35439,599

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS42345.1. [Q14CW9-1]
CCDS45697.1. [Q14CW9-2]
RefSeqNP_001092303.1. NM_001098833.1. [Q14CW9-1]
NP_064603.1. NM_020218.1. [Q14CW9-2]
UniGeneHs.512651.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KKTNMR-A197-276[»]
ProteinModelPortalQ14CW9.
SMRQ14CW9. Positions 198-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121289. 16 interactions.
IntActQ14CW9. 6 interactions.
MINTMINT-6774236.
STRING9606.ENSP00000397259.

PTM databases

PhosphoSiteQ14CW9.

Polymorphism databases

DMDM121948758.

Proteomic databases

MaxQBQ14CW9.
PaxDbQ14CW9.
PRIDEQ14CW9.

Protocols and materials databases

DNASU56970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389384; ENSP00000374035; ENSG00000087152. [Q14CW9-1]
ENST00000454077; ENSP00000397259; ENSG00000087152. [Q14CW9-2]
GeneID56970.
KEGGhsa:56970.
UCSCuc002ifz.3. human. [Q14CW9-2]
uc002iga.3. human. [Q14CW9-1]

Organism-specific databases

CTD56970.
GeneCardsGC17M042269.
HGNCHGNC:25416. ATXN7L3.
HPAHPA050625.
HPA052419.
neXtProtNX_Q14CW9.
PharmGKBPA134991793.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271996.
HOGENOMHOG000006954.
HOVERGENHBG071455.
InParanoidQ14CW9.
KOK11363.
OMAPFKYSNS.
PhylomeDBQ14CW9.
TreeFamTF324580.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ14CW9.
BgeeQ14CW9.
CleanExHS_ATXN7L3.
GenevestigatorQ14CW9.

Family and domain databases

HAMAPMF_03047. Sgf11.
InterProIPR013246. SAGA_su_Sgf11.
IPR013243. SCA7_dom.
[Graphical view]
PfamPF08313. SCA7. 1 hit.
PF08209. Sgf11. 1 hit.
[Graphical view]
PROSITEPS51505. SCA7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14CW9.
GenomeRNAi56970.
NextBio62612.
PROQ14CW9.

Entry information

Entry nameAT7L3_HUMAN
AccessionPrimary (citable) accession number: Q14CW9
Secondary accession number(s): Q8IY68, Q96N40, Q9NPU5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: August 22, 2006
Last modified: July 9, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM