Q14CW9 (AT7L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ataxin-7-like protein 3

Alternative name(s):
SAGA-associated factor 11 homolog

Gene names

Name:

ATXN7L3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Subunit structure	Component of some SAGA transcription coactivator-HAT complex, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ATXN7L3, ENY2 and USP22 form a subcomplex required for histone deubiquitination. Interacts directly with ENY2 and USP22. Ref.4
Subcellular location	Nucleus Probable.
Domain	The SGF11-type zinc finger mediates the interaction with USP22 and ENY2.
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone deubiquitination Inferred from direct assay Ref.4. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.4. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SAGA complex Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	ligand-dependent nuclear receptor transcription coactivator activity Inferred from direct assay Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 347

347

Ataxin-7-like protein 3

PRO_0000278301

Regions

Domain

196 – 263

68

SCA7

Zinc finger

84 – 105

22

SGF11-type

Amino acid modifications

Modified residue

129

1

Phosphoserine Ref.9

Modified residue

131

1

Phosphoserine Ref.9

Modified residue

278

1

Phosphoserine Ref.7

Modified residue

281

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

326

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

159

1

K → KLWYLPFQ in isoform 2.

VSP_036721

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

347

Helix Strand Turn

Details...

Helix

199 – 204

6

Turn

205 – 207

3

Turn

214 – 217

4

Beta strand

226 – 228

3

Helix

231 – 241

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 742D85BFF4ADD0C0	FASTA	347	38,651
	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
	Isoform 2 [UniParc]. Checksum: EDB618080F2200D6	FASTA	354	39,599
	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 KAKKRKSDKL WYLPFQNPNS PRRSKSLKHK 190 200 210 220 230 240 NGELSNSDPF KYNNSTGISY ETLGPEELRS LLTTQCGVIS EHTKKMCTRS LRCPQHTDEQ 250 260 270 280 290 300 RRTVRIYFLG PSAVLPEVES SLDNDSFDMT DSQALISRLQ WDGSSDLSPS DSGSSKTSEN 310 320 330 340 350 QGWGLGTNSS ESRKTKKKKS HLSLVGTASG LGSNKKKKPK PPAPPTPSIY DDIN

References

	« Hide 'large scale' referencesShow '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. , 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.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00401194.
IPI00783398.

RefSeq

NP_001092303.1. NM_001098833.1.
NP_064603.1. NM_020218.1.

UniGene

Hs.512651.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KKT	NMR	-	A	197-276	[»]

ProteinModelPortal

Q14CW9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14CW9. 6 interactions.

MINT

MINT-6774236.

STRING

9606.ENSP00000397259.

PTM databases

PhosphoSite

Q14CW9.

Polymorphism databases

DMDM

121948758.

Proteomic databases

PaxDb

Q14CW9.

PRIDE

Q14CW9.

Protocols and materials databases

DNASU

56970.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389384; ENSP00000374035; ENSG00000087152.
ENST00000454077; ENSP00000397259; ENSG00000087152.

GeneID

56970.

KEGG

hsa:56970.

UCSC

uc002ifz.3. human.
uc002iga.3. human.

Organism-specific databases

CTD

56970.

GeneCards

GC17M042269.

HGNC

HGNC:25416. ATXN7L3.

HPA

HPA050625.

neXtProt

NX_Q14CW9.

PharmGKB

PA134991793.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG271996.

HOGENOM

HOG000006954.

HOVERGEN

HBG071455.

InParanoid

Q14CW9.

KO

K11363.

OMA

PFKYSNS.

Gene expression databases

ArrayExpress

Q14CW9.

Bgee

Q14CW9.

CleanEx

HS_ATXN7L3.

Genevestigator

Q14CW9.

Family and domain databases

InterPro

IPR013246. SAGA_su_Sgf11.
IPR013243. SCA7_dom.
[Graphical view]

Pfam

PF08313. SCA7. 1 hit.
PF08209. Sgf11. 1 hit.
[Graphical view]

PROSITE

PS51505. SCA7. 1 hit. Uncertain.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q14CW9.

GenomeRNAi

56970.

NextBio

62612.

Entry information

Entry name

AT7L3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.