Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q562F6 (SGOL2_HUMAN)

Last modified February 9, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

Subunit structure

Directly interacts with PPP2CA. Ref.5

Subcellular location

Nucleus. Centromere. Kinetochore By similarity. Note: During meiosis I, accumulates at centromeres during diplotene, and co-localizes 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.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.8 Ref.9 Ref.10

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: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Meiosis
   Cellular componentCentromere
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitotic cohesin complex

Inferred from direct assay. Source: MGI

   Molecular functionprotein binding Ref.5 Ref.7

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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 residue2661Phosphoserine Ref.6
Modified residue4211Phosphoserine Ref.9
Modified residue4971Phosphothreonine Ref.9
Modified residue5071Phosphoserine Ref.8
Modified residue8451Phosphothreonine Ref.6
Modified residue11441Phosphoserine Ref.10
Modified residue11501Phosphoserine Ref.10
Modified residue11511Phosphoserine Ref.10

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: dbSNP rs1036533. Ref.4
VAR_024784
Natural variant3431E → A: dbSNP rs13417812.
VAR_057178
Natural variant4961I → V: dbSNP rs17448235. Ref.1
VAR_024785
Natural variant6601N → S: dbSNP rs17532665. Ref.1
VAR_057179
Natural variant10991I → T: dbSNP rs11896759.
VAR_057180
Natural variant11431H → R: dbSNP rs16833776.
VAR_057181

Experimental info

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.

Checksum: A76F72D7168C9FC7
Show »

FASTA1,261144,181
Isoform 3.

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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 698-1265 (ISOFORM 1).
[3]"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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ASP-9.
Tissue: Lymph, Testis and Uterus.
[5]"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: 16541025] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA.
[6]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND THR-845, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17485487] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, MASS SPECTROMETRY.
[9]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND THR-497, MASS SPECTROMETRY.
[10]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1144; SER-1150 AND SER-1151, MASS SPECTROMETRY.
+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.
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.
IPIIPI00218013.
IPI00395828.
IPI00657858.
RefSeqNP_001153518.1.
NP_689737.4.
UniGeneHs.655182

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ562F6. 10 interactions.
STRINGQ562F6.

PTM databases

PhosphoSiteQ562F6.

Proteomic databases

PRIDEQ562F6.

Genome annotation databases

EnsemblENST00000357799; ENSP00000350447; ENSG00000163535; Homo sapiens. [Genome view]
GeneID151246.
UCSCuc002uvv.2. human.
uc002uvw.1. human.

Organism-specific databases

CTD151246.
GeneCardsGC02P201099.
HGNCHGNC:30812. SGOL2.
MIM612425. gene.
PharmGKBPA134901462.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16739.
HOVERGENQ562F6.
InParanoidQ562F6.
OMAITAIEMS.
OrthoDBEOG97Q0RG.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressQ562F6.
BgeeQ562F6.
CleanExHS_SGOL2.
GenevestigatorQ562F6.
GermOnlineENSG00000163535. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio86645.
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: February 9, 2010
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents