Q9Y2Z0 (SUGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Suppressor of G2 allele of SKP1 homolog

Alternative name(s):
Protein 40-6-3
Sgt1

Gene names

Name:

SUGT1

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	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in ubiquitination and subsequent proteasomal degradation of target proteins.
Subunit structure	Probably associates with SCF (SKP1-CUL1-F-box protein) complex through interaction with SKP1. Interacts with S100A6. Interacts with HSP90. Ref.1 Ref.11 Ref.16 Ref.17
Subcellular location	Cytoplasm. Nucleus. Note: Translocates to the nucleus upon heat shock, requiring S100A6. Ref.16
Domain	The CS domain mediates interaction with HSP90.
Post-translational modification	Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex. Ref.16
Sequence similarities	Belongs to the SUGT1 family. Contains 1 CS domain. Contains 1 SGS domain. Contains 3 TPR repeats.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	innate immune response Traceable author statement. Source: Reactome mitosis Traceable author statement Ref.1. Source: ProtInc nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome kinetochore Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y2Z0-1)

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: Q9Y2Z0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-142: IETGFHRVGQAGLQLLTSSDPPALDSQSAGITG → S

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10

Chain

2 – 365

364

Suppressor of G2 allele of SKP1 homolog

PRO_0000106332

Regions

Repeat

11 – 44

34

TPR 1

Repeat

45 – 78

34

TPR 2

Repeat

79 – 112

34

TPR 3

Domain

169 – 258

90

CS

Domain

276 – 365

90

SGS

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.14

Modified residue

265

1

Phosphothreonine Ref.14

Modified residue

281

1

Phosphoserine Ref.16

Modified residue

331

1

Phosphoserine Ref.14 Ref.16

Natural variations

Alternative sequence

110 – 142

33

IETGF…AGITG → S in isoform 2.

VSP_013420

Experimental info

Sequence conflict

120

1

A → V in AAQ01749. Ref.4

Secondary structure

1

.

.

.

.

.

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.

.

.

.

.

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.

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365

Helix Strand Turn

Details...

Beta strand

174 – 178

5

Beta strand

180 – 187

8

Helix

194 – 196

3

Beta strand

197 – 200

4

Beta strand

202 – 204

3

Beta strand

206 – 211

6

Beta strand

215 – 222

8

Beta strand

224 – 226

3

Helix

230 – 232

3

Beta strand

233 – 237

5

Beta strand

239 – 247

9

Beta strand

255 – 258

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4A5A413E70561D9A	FASTA	365	41,024
	10 20 30 40 50 60 MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ RAYCHILLGN 70 80 90 100 110 120 YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE TFTEGQKLDI ETGFHRVGQA 130 140 150 160 170 180 GLQLLTSSDP PALDSQSAGI TGADANFSVW IKRCQEAQNG SESEVWTHQS KIKYDWYQTE 190 200 210 220 230 240 SQVVITLMIK NVQKNDVNVE FSEKELSALV KLPSGEDYNL KLELLHPIIP EQSTFKVLST 250 260 270 280 290 300 KIEIKLKKPE AVRWEKLEGQ GDVPTPKQFV ADVKNLYPSS SPYTRNWDKL VGEIKEEEKN 310 320 330 340 350 360 EKLEGDAALN RLFQQIYSDG SDEVKRAMNK SFMESGGTVL STNWSDVGKR KVEINPPDDM EWKKY
	Isoform 2 [UniParc]. Checksum: 14DE069A1623DB53	FASTA	333	37,805
	10 20 30 40 50 60 MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ RAYCHILLGN 70 80 90 100 110 120 YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE TFTEGQKLDS ADANFSVWIK 130 140 150 160 170 180 RCQEAQNGSE SEVWTHQSKI KYDWYQTESQ VVITLMIKNV QKNDVNVEFS EKELSALVKL 190 200 210 220 230 240 PSGEDYNLKL ELLHPIIPEQ STFKVLSTKI EIKLKKPEAV RWEKLEGQGD VPTPKQFVAD 250 260 270 280 290 300 VKNLYPSSSP YTRNWDKLVG EIKEEEKNEK LEGDAALNRL FQQIYSDGSD EVKRAMNKSF 310 320 330 MESGGTVLST NWSDVGKRKV EINPPDDMEW KKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex." Kitagawa K., Skowyra D., Elledge S.J., Harper J.W., Hieter P. Mol. Cell 4:21-33(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT.
[2]	Schmidt T. Thesis (2001), University of Goettingen, Germany Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Identification of a novel splice variant: human SGT1B (SUGT1B)." Niikura Y., Kitagawa K. DNA Seq. 14:436-441(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	Zou X., Mao Y., Xie Y. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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 2). Tissue: Cervix.
[9]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Tissue: Platelet.
[10]	Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 195-204; 222-236 AND 312-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[11]	"Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins." Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K., Kuznicki J. J. Biol. Chem. 278:26923-26928(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH S100A6.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265 AND SER-331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Nuclear translocation of Sgt1 depends on its phosphorylation state." Prus W., Zabka M., Bieganowski P., Filipek A. Int. J. Biochem. Cell Biol. 43:1747-1753(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-281 AND SER-331, SUBCELLULAR LOCATION, INTERACTION WITH S100A6.
[17]	"Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain." Lee Y.-T., Jacob J., Michowski W., Nowotny M., Kuznicki J., Chazin W.J. J. Biol. Chem. 279:16511-16517(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 167-276, INTERACTION WITH HSP90.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132856 mRNA. Translation: AAD30062.1.
AJ344097 mRNA. Translation: CAC51433.1.
AY321358 mRNA. Translation: AAQ76039.1.
AY271314 mRNA. Translation: AAQ01749.1.
BT009798 mRNA. Translation: AAP88800.1.
AL139089 Genomic DNA. Translation: CAI17072.1.
AL139089 Genomic DNA. Translation: CAM23909.1.
CH471124 Genomic DNA. Translation: EAW52045.1.
BC000911 mRNA. Translation: AAH00911.1.

IPI

IPI00791573.
IPI00828150.

RefSeq

NP_001124384.1. NM_001130912.1.
NP_006695.1. NM_006704.3.

UniGene

Hs.281902.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RL1	NMR	-	A	167-276	[»]

ProteinModelPortal

Q9Y2Z0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2Z0. 6 interactions.

MINT

MINT-5005759.

STRING

9606.ENSP00000367208.

PTM databases

PhosphoSite

Q9Y2Z0.

Polymorphism databases

DMDM

62512186.

Proteomic databases

PaxDb

Q9Y2Z0.

PRIDE

Q9Y2Z0.

Protocols and materials databases

DNASU

10910.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310528; ENSP00000308067; ENSG00000165416.
ENST00000343788; ENSP00000367208; ENSG00000165416.

GeneID

10910.

KEGG

hsa:10910.

UCSC

uc001vhb.2. human.
uc001vhc.2. human.

Organism-specific databases

CTD

10910.

GeneCards

GC13P053226.

H-InvDB

HIX0026254.
HIX0201992.

HGNC

HGNC:16987. SUGT1.

HPA

CAB015942.

MIM

604098. gene.

neXtProt

NX_Q9Y2Z0.

PharmGKB

PA134880121.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

HOGENOM

HOG000248210.

HOVERGEN

HBG055080.

InParanoid

Q9Y2Z0.

KO

K12795.

OMA

QRTHQSK.

OrthoDB

EOG4PNXHJ.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9Y2Z0.

Bgee

Q9Y2Z0.

CleanEx

HS_SUGT1.

Genevestigator

Q9Y2Z0.

GermOnline

ENSG00000165416. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR007052. CS-like_domain.
IPR017447. CS_domain.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
[Graphical view]

SUPFAM

SSF49764. HSP20_chap. 1 hit.

PROSITE

PS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y2Z0.

GenomeRNAi

10910.

NextBio

41435.

SOURCE

Search...

Entry information

Entry name

SUGT1_HUMAN

Accession

Primary (citable) accession number: Q9Y2Z0
Secondary accession number(s): A2A303 , Q5JAK5, Q5TAM6, Q6VXY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 3 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.