Q24141 (SGO1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Shugoshin

Alternative name(s):
Meiotic protein S332

Gene names

Name:	mei-S332
ORF Names:	CG5303

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a central role in chromosome cohesion during meiosis and mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by protecting or Rad21 from cleavage by Sse/separase. Required during meiosis in both males and females. Ref.1 Ref.5 Ref.6 Ref.7
Subunit structure	Homodimer. Interacts with Incenp. Ref.5 Ref.11
Subcellular location	Nucleus. Chromosome › centromere. Note: Localizes to the centromere of meiotic and mitotic chromosomes. During meiosis, it assembles onto centromeres during prometaphase I, remains attached until anaphase II, during which it is displaced from centromeres without being degraded. Localization onto centromeres is independent of kinetochore formation and cohesin complex. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11
Developmental stage	Expressed both maternally and zygotically. Present throughout embryogenesis and larval stages.
Post-translational modification	Phosphorylation by polo-like kinase (PLK) on Thr-331 antagonizes cohesive function. Phosphorylation on Thr-331 at the metaphase anaphase transition leads to its dissociation from centromeres. In contrast, phosphorylation by ial on either Ser-124, Ser-125 or Ser-126 is required for association with centromeres.
Sequence similarities	Belongs to the shugoshin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Meiosis Mitosis
Cellular component	Centromere Chromosome Nucleus
Domain	Coiled coil
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW female meiosis Inferred from mutant phenotype. Source: FlyBase male meiosis Inferred from mutant phenotype. Source: FlyBase meiotic chromosome segregation Inferred from electronic annotation. Source: InterPro meiotic metaphase I Traceable author statement. Source: FlyBase mitosis Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW sister chromatid cohesion Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	chromosome, centromeric region Inferred from direct assay Ref.1. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 401	401	Shugoshin		PRO_0000055443
Regions
	Coiled coil	3 – 49	47	Potential
Amino acid modifications
	Modified residue	124	1	Phosphoserine; by ial Probable
	Modified residue	125	1	Phosphoserine; by ial Probable
	Modified residue	126	1	Phosphoserine; by ial Probable
	Modified residue	331	1	Phosphothreonine; by PLK1 Probable
Experimental info
	Mutagenesis	13	1	N → I in mei-S332-9; induces missegregation of chromatids during meiosis. Ref.5
	Mutagenesis	28	1	G → D in mei-S332-3; induces missegregation of chromatids during meiosis. Ref.1 Ref.5
	Mutagenesis	34	1	V → E in mei-S332-8; induces missegregation of chromatids during meiosis. Ref.1 Ref.5
	Mutagenesis	112	1	L → M in mei-S332-4; induces missegregation of chromatids during meiosis; when associated with H-. Ref.1
	Mutagenesis	124 – 126	3	SSS → AAA: Does not stably associate with centromeres during mitosis. Ref.11
	Mutagenesis	234	1	S → A: Does not affect phosphorylation. Ref.10
	Mutagenesis	277	1	S → F in mei-S332-5; induces missegregation of chromatids during meiosis. Ref.5
	Mutagenesis	331	1	T → A: Affects phosphorylation and localization to centromeres. Ref.10
	Mutagenesis	375	1	C → Y in mei-S332-2; induces missegregation of chromatids during meiosis. Ref.1
	Mutagenesis	377	1	P → H in mei-S332-4; induces missegregation of chromatids during meiosis; when associated with M-112. Ref.1
	Mutagenesis	382	1	E → K in mei-S332-10; induces missegregation of chromatids during meiosis. Ref.5
	Mutagenesis	384	1	S → R in mei-S332-6; induces missegregation of chromatids during meiosis. Ref.1 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q24141 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 76D3EA53577B315F	FASTA	401	44,402
	10 20 30 40 50 60 MGSKVEQQYK LLNAELMDQV QKQRLEIGEY RKRVISLERE IMDIREEHVL QNHRQRMENI 70 80 90 100 110 120 SIVRSLMLSL NVDSDSLAVR QEPAPAAQIN RPSGPRRSSR EICKDMRRTC ALARTTRPIS 130 140 150 160 170 180 PRRSSSVTST VSSTSRRSSA EVQSEVVTTR IPEDRRANKP TPPPRRPAEL VFDEDDSDDD 190 200 210 220 230 240 FDEAVSPVEE TQTEQNEENN RLFSIIEENG SEGESTDSSS SCEAIYCDTT FESSPPNAQV 250 260 270 280 290 300 TVTPSGRALR EVDTNIPVAV SLSRGKETGK GSWLAISVAV EDSPQEPSIQ CPRLAVTRPS 310 320 330 340 350 360 QSSGIFPDVN GLTPRRSLFN GIGKMAGSTS TPKSFLVEEM PSIRTRSRTA ANKKSENTDM 370 380 390 400 SSSFCNNSAR PSRSCRPTSL VEPSLKNKLR NGSKGKAKAK K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mei-S332, a Drosophila protein required for sister-chromatid cohesion, can localize to meiotic centromere regions." Kerrebrock A.W., Moore D.P., Wu J.S., Orr-Weaver T.L. Cell 83:247-256(1995) [PubMed: 7585942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-28; VAL-34; LEU-112; CYS-375; PRO-377 AND SER-384. Tissue: Testis.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Maintenance of sister-chromatid cohesion at the centromere by the Drosophila MEI-S332 protein." Tang T.-T., Bickel S.E., Young L.M., Orr-Weaver T.L. Genes Dev. 12:3843-3856(1998) [PubMed: 9869638] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ASN-13; GLY-28; VAL-34; SER-277; GLU-382 AND SER-384.
[6]	"The cohesion protein MEI-S332 localizes to condensed meiotic and mitotic centromeres until sister chromatids separate." Moore D.P., Page A.W., Tang T.-T., Kerrebrock A.W., Orr-Weaver T.L. J. Cell Biol. 140:1003-1012(1998) [PubMed: 9490715] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"The mitotic centromeric protein MEI-S332 and its role in sister-chromatid cohesion." LeBlanc H.N., Tang T.-T., Wu J.S., Orr-Weaver T.L. Chromosoma 108:401-411(1999) [PubMed: 10654079] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Sister-chromatid cohesion via MEI-S332 and kinetochore assembly are separable functions of the Drosophila centromere." Lopez J.M., Karpen G.H., Orr-Weaver T.L. Curr. Biol. 10:997-1000(2000) [PubMed: 10985388] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Control of centromere localization of the MEI-S332 cohesion protection protein." Lee J.Y., Dej K.J., Lopez J.M., Orr-Weaver T.L. Curr. Biol. 14:1277-1283(2004) [PubMed: 15268859] [Abstract] Cited for: LACK OF DEGRADATION.
[10]	"POLO kinase regulates the Drosophila centromere cohesion protein MEI-S332." Clarke A.S., Tang T.-T., Ooi D.L.-Y., Orr-Weaver T.L. Dev. Cell 8:53-64(2005) [PubMed: 15621529] [Abstract] Cited for: PHOSPHORYLATION, PHOSPHORYLATION AT THR-331, MUTAGENESIS OF SER-234 AND THR-331.
[11]	"INCENP and Aurora B promote meiotic sister chromatid cohesion through localization of the Shugoshin MEI-S332 in Drosophila." Resnick T.D., Satinover D.L., MacIsaac F., Stukenberg P.T., Earnshaw W.C., Orr-Weaver T.L., Carmena M. Dev. Cell 11:57-68(2006) [PubMed: 16824953] [Abstract] Cited for: INTERACTION WITH INCENP, PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 124-SER--SER-126.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36583 mRNA. Translation: AAA87038.1. AE013599 Genomic DNA. Translation: AAF46802.1. AY058633 mRNA. Translation: AAL13862.1.
PIR	A57226.
RefSeq	NP_476634.1. NM_057286.4.
UniGene	Dm.12274.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17412N.
IntAct	Q24141. 6 interactions.
MINT	MINT-745645.
STRING	Q24141.
Proteomic databases
PRIDE	Q24141.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071761; FBpp0071675; FBgn0002715.
GeneID	37523.
KEGG	dme:Dmel_CG5303.
NMPDR	fig|7227.3.peg.6788.
Organism-specific databases
CTD	37523.
FlyBase	FBgn0002715. mei-S332.
Phylogenomic databases
GeneTree	EMGT00050000022284.
InParanoid	Q24141.
OMA	LNAELMD.
OrthoDB	EOG4HDR91.
PhylomeDB	Q24141.
Gene expression databases
ArrayExpress	Q24141.
Bgee	Q24141.
GermOnline	CG5303. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011515. Shugoshin_C. IPR011516. Shugoshin_N. [Graphical view]
Pfam	PF07557. Shugoshin_C. 1 hit. PF07558. Shugoshin_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	804088.

Entry information

Entry name

SGO1_DROME

Accession

Primary (citable) accession number: Q24141

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project