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Q562F6 (SGOL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Shugoshin-like 2
Alternative name(s):
Shugoshin-2
Short name=Sgo2
Tripin
Gene names
Name:SGOL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation By similarity. Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Ref.6 Ref.7

Subunit structure

Directly interacts with PPP2CA. Part of an astrin (SPAG5) -kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2. Ref.6 Ref.7 Ref.9

Subcellular location

Nucleus. Chromosomecentromere. Chromosomecentromerekinetochore By similarity. Note: During meiosis I, accumulates at centromeres during diplotene, and colocalizes differentially with the cohesin subunits RAD21 and REC8 at metaphase I centromeres. SGO2 and RAD21 change their relative distributions during telophase I when sister-kinetochore association is lost. During meiosis II, it shows a striking tension-dependent redistribution within centromeres throughout chromosome congression during prometaphase II, as it does during mitosis By similarity. In Hela cells, localizes at centromeres throughout prophase until metaphase and disappears at anaphase. Centromeric localization requires the presence of BUB1 and AUKRB. Ref.6 Ref.7

Miscellaneous

Shugoshin is Japanese for guardian spirit (as it is known to be a protector of centromeric cohesin).

Sequence similarities

Belongs to the shugoshin family.

Sequence caution

The sequence AAH35764.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAB71617.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC04524.1 differs from that shown. Reason: Frameshift at position 649.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q562F6-1)

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: Q562F6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1261-1265: DKMRR → E
Note: No experimental confirmation available.
Isoform 3 (identifier: Q562F6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     235-247: ESHSHSDQSSKTS → GEIVLKIHFEYLY
     248-1265: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12651265Shugoshin-like 2
PRO_0000055439

Regions

Coiled coil69 – 11648 Potential
Coiled coil452 – 47625 Potential
Coiled coil603 – 62624 Potential

Amino acid modifications

Modified residue11441Phosphoserine Ref.8

Natural variations

Alternative sequence235 – 24713ESHSH…SSKTS → GEIVLKIHFEYLY in isoform 3.
VSP_016798
Alternative sequence248 – 12651018Missing in isoform 3.
VSP_016799
Alternative sequence1261 – 12655DKMRR → E in isoform 2.
VSP_016800
Natural variant91G → D. Ref.5
Corresponds to variant rs1036533 [ dbSNP | Ensembl ].
VAR_024784
Natural variant3431E → A.
Corresponds to variant rs13417812 [ dbSNP | Ensembl ].
VAR_057178
Natural variant4961I → V. Ref.1
Corresponds to variant rs17448235 [ dbSNP | Ensembl ].
VAR_024785
Natural variant6601N → S. Ref.1
Corresponds to variant rs17532665 [ dbSNP | Ensembl ].
VAR_057179
Natural variant10991I → T.
Corresponds to variant rs11896759 [ dbSNP | Ensembl ].
VAR_057180
Natural variant11431H → R.
Corresponds to variant rs16833776 [ dbSNP | Ensembl ].
VAR_057181

Experimental info

Sequence conflict1221I → T in BX647433. Ref.3
Sequence conflict1451I → V in BX647433. Ref.3
Sequence conflict1931S → R in AAM21971. Ref.1
Sequence conflict2051E → G in AAM21971. Ref.1
Sequence conflict2151N → H in AAM21971. Ref.1
Sequence conflict450 – 4512FI → LF in AAM21971. Ref.1
Sequence conflict12431T → A in BAB71617. Ref.2

Sequences

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

Last modified January 10, 2006. Version 2.
Checksum: 6A678CB3E6DF72D7

FASTA1,265144,739
        10         20         30         40         50         60 
MECPVMETGS LFTSGIKRHL KDKRISKTTK LNVSLASKIK TKILNNSSIF KISLKHNNRA 

        70         80         90        100        110        120 
LAQALSREKE NSRRITTEKM LLQKEVEKLN FENTFLRLKL NNLNKKLIDI EALMNNNLIT 

       130        140        150        160        170        180 
AIEMSSLSEF HQSSFLLSAS KKKRISKQCK LMRLPFARVP LTSNDDEDED KEKMQCDNNI 

       190        200        210        220        230        240 
KSKTLPDIPS SGSTTQPLST QDNSEVLFLK ENNQNVYGLD DSEHISSIVD VPPRESHSHS 

       250        260        270        280        290        300 
DQSSKTSLMS EMRNAQSIGR RWEKPSPSNV TERKKRGSSW ESNNLSADTP CATVLDKQHI 

       310        320        330        340        350        360 
SSPELNCNNE INGHTNETNT EMQRNKQDLP GLSSESAREP NAECMNQIED NDDFQLQKTV 

       370        380        390        400        410        420 
YDADMDLTAS EVSKIVTVST GIKKKSNKKT NEHGMKTFRK VKDSSSEKKR ERSKRQFKNS 

       430        440        450        460        470        480 
SDVDIGEKIE NRTERSDVLD GKRGAEDPGF IFNNEQLAQM NEQLAQVNEL KKMTLQTGFE 

       490        500        510        520        530        540 
QGDRENVLCN KKEKRITNEQ EETYSLSQSS GKFHQESKFD KGQNSLTCNK SKASRQTFVI 

       550        560        570        580        590        600 
HKLEKDNLLP NQKDKVTIYE NLDVTNEFHT ANLSTKDNGN LCDYGTHNIL DLKKYVTDIQ 

       610        620        630        640        650        660 
PSEQNESNIN KLRKKVNRKT EIISGMNHMY EDNDKDVVHG LKKGNFFFKT QEDKEPISEN 

       670        680        690        700        710        720 
IEVSKELQIP ALSTRDNENQ CDYRTQNVLG LQKQITNMYP VQQNESKVNK KLRQKVNRKT 

       730        740        750        760        770        780 
EIISEVNHLD NDKSIEYTVK SHSLFLTQKD KEIIPGNLED PSEFETPALS TKDSGNLYDS 

       790        800        810        820        830        840 
EIQNVLGVKH GHDMQPACQN DSKIGKKPRL NVCQKSEIIP ETNQIYENDN KGVHDLEKDN 

       850        860        870        880        890        900 
FFSLTPKDKE TISENLQVTN EFQTVDLLIK DNGNLCDYDT QNILELKKYV TDRKSAEQNE 

       910        920        930        940        950        960 
SKINKLRNKV NWKTEIISEM NQIYEDNDKD AHVQESYTKD LDFKVNKSKQ KLECQDIINK 

       970        980        990       1000       1010       1020 
HYMEVNSNEK ESCDQILDSY KVVKKRKKES SCKAKNILTK AKNKLASQLT ESSQTSISLE 

      1030       1040       1050       1060       1070       1080 
SDLKHITSEA DSDPGNPVEL CKTQKQSTTT LNKKDLPFVE EIKEGECQVK KVNKMTSKSK 

      1090       1100       1110       1120       1130       1140 
KRKTSIDPSP ESHEVMERIL DSVQGKSTVS EQADKENNLE NEKMVKNKPD FYTKAFRSLS 

      1150       1160       1170       1180       1190       1200 
EIHSPNIQDS SFDSVREGLV PLSVSSGKNV IIKENFALEC SPAFQVSDDE HEKMNKMKFK 

      1210       1220       1230       1240       1250       1260 
VNRRTQKSGI GDRPLQDLSN TSFVSNNTAE SENKSEDLSS ERTSRRRRCT PFYFKEPSLR 


DKMRR 

« Hide

Isoform 2 [UniParc].

Checksum: A76F72D7168C9FC7
Show »

FASTA1,261144,181
Isoform 3 [UniParc].

Checksum: 32F5E22581F1A7D9
Show »

FASTA24728,230

References

« Hide 'large scale' references
[1]"Cloning and characterization of TRIPIN: an inhibitor of TRIP function on TRAF2 mediated activation of NF-kB."
Oliveira V., Fiorentino L., Chan H., Matsuzawa S., Chu Z., Saraiva M.J., Reed J.C.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-496 AND SER-660.
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 698-1265 (ISOFORM 1).
[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].
Tissue: Colon endothelium.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 3), VARIANT ASP-9.
Tissue: Lymph, Testis and Uterus.
[6]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA.
[7]"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA.
[8]"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-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment."
Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.
J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; PLK1 AND DYNLL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY094614 mRNA. Translation: AAM21971.1.
AK057940 mRNA. Translation: BAB71617.1. Different initiation.
AK095291 mRNA. Translation: BAC04524.1. Frameshift.
BX647433 mRNA. No translation available.
AC012459 Genomic DNA. Translation: AAY24310.1.
AC080164 Genomic DNA. Translation: AAY24264.1.
BC035764 mRNA. Translation: AAH35764.1. Sequence problems.
BC048349 mRNA. Translation: AAH48349.1.
BC092412 mRNA. Translation: AAH92412.1.
RefSeqNP_001153518.1. NM_001160046.1.
NP_689737.4. NM_152524.5.
XP_005246402.1. XM_005246345.1.
UniGeneHs.655182.

3D structure databases

ProteinModelPortalQ562F6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127357. 6 interactions.
DIPDIP-36615N.
IntActQ562F6. 15 interactions.
MINTMINT-4995654.
STRING9606.ENSP00000350447.

PTM databases

PhosphoSiteQ562F6.

Polymorphism databases

DMDM85542144.

Proteomic databases

PaxDbQ562F6.
PRIDEQ562F6.

Protocols and materials databases

DNASU151246.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357799; ENSP00000350447; ENSG00000163535. [Q562F6-1]
ENST00000409203; ENSP00000386249; ENSG00000163535. [Q562F6-3]
GeneID151246.
KEGGhsa:151246.
UCSCuc002uvv.4. human. [Q562F6-3]
uc002uvw.2. human. [Q562F6-1]
uc010zhd.1. human. [Q562F6-2]

Organism-specific databases

CTD151246.
GeneCardsGC02P201375.
HGNCHGNC:30812. SGOL2.
HPAHPA035163.
HPA040817.
MIM612425. gene.
neXtProtNX_Q562F6.
PharmGKBPA134901462.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25773.
HOVERGENHBG093950.
InParanoidQ562F6.
KOK11581.
OMAKVNRKTE.
OrthoDBEOG790G02.
PhylomeDBQ562F6.
TreeFamTF350100.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ562F6.
BgeeQ562F6.
CleanExHS_SGOL2.
GenevestigatorQ562F6.

Family and domain databases

InterProIPR026706. SGOL2.
[Graphical view]
PANTHERPTHR21577:SF0. PTHR21577:SF0. 1 hit.
ProtoNetSearch...

Other

GeneWikiSGOL2.
GenomeRNAi151246.
NextBio86645.
PROQ562F6.
SOURCESearch...

Entry information

Entry nameSGOL2_HUMAN
AccessionPrimary (citable) accession number: Q562F6
Secondary accession number(s): Q53RR9 expand/collapse secondary AC list , Q53T20, Q86XY4, Q8IWK2, Q8IZK1, Q8N1Q5, Q96LQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 98 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM