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Protein Page:
STAG2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
STAG2 Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Interacts directly with RAD21 in cohesin complex. Cohesin complexes are composed of a heterodimer between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge domain, and RAD21 which link them at their heads, and one STAG protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG2 is mutually exclusive with STAG1 and STAG3. Belongs to the SCC3 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor
Cellular Component: nucleoplasm; chromatin; nucleus; chromosome, pericentric region
Molecular Function: protein binding
Biological Process: meiosis; M phase of mitotic cell cycle; cell division; sister chromatid cohesion; negative regulation of DNA endoreduplication; mitotic cell cycle; mitotic metaphase/anaphase transition; mitotic prometaphase
Reference #:  Q8N3U4 (UniProtKB)
Alt. Names/Synonyms: bA517O1.1; Cohesin subunit SA-2; DKFZp686P168; DKFZp781H1753; FLJ25871; SA-2; SA2; SCC3 homolog 2; STAG2; Stromal antigen 2
Gene Symbols: STAG2
Molecular weight: 141,326 Da
Basal Isoelectric point: 5.27  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

STAG2
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 1 S17 DFNLLQESETHFSSD
0 1 T132-p SGCKGVVtAEMFRHM
0 1 S173-p PQWKKFKssFCEFIG
0 1 S174-p QWKKFKssFCEFIGV
0 4 K270-u RLELLLQkRKELQEN
0 1 K363-u YNKELNSkLELFTSR
0 42 Y433-p VAAGEFLyKKLFSRR
0 1 T602-p FDLEIYTtGRLEkHL
0 1 K607-a YTtGRLEkHLDALLR
0 1 K607-u YTtGRLEkHLDALLR
0 1 K664-u LIDELADkFNRLLED
0 18 Y685-p EPDEDDAyQVLSTLk
0 1 K692-u yQVLSTLkRITAFHN
0 1 T737-p VIHALQCtHYVILWQ
0 1 T749-p LWQLAKItEssSTkE
0 1 S751-p QLAKItEssSTkEDL
0 1 S752-p LAKItEssSTkEDLL
0 1 K755-u ItEssSTkEDLLRLK
0 1 Y775-p FCQICQHyLTNVNTT
0 3 S843-p EQDDDNNsADGQQED
0 2 Y892-p IFKQYMKyyNDyGDI
0 2 Y893-p FKQYMKyyNDyGDII
0 2 Y896-p YMKyyNDyGDIIKET
0 2 K965-u TFGLDQLkTREAIAM
0 1 Y1019 RQDKRTVYVYLEKFM
0 1 S1047 PLMSYRNSLLAGGDD
0 3 T1056-p LAGGDDDtMsVIsGI
0 7 S1058-p GGDDDtMsVIsGIss
0 19 S1061-p DDtMsVIsGIssrGS
0 7 S1064-p MsVIsGIssrGSTVR
0 2 S1065-p sVIsGIssrGSTVRS
0 1 R1066-m1 VIsGIssrGSTVRSK
0 1 S1072 srGSTVRSKKSKPST
0 1 S1091-p VVEGMQLsLTEESSS
0 1 S1099 LTEESSSSDSMWLSR
0 1 T1109-p MWLSREQtLHtPVMM
0 10 T1112-p SREQtLHtPVMMQtP
0 6 T1118-p HtPVMMQtPQLTStI
0 1 T1124-p QtPQLTStIMREPKR
0 1 S1137-p KRLRPEDsFMsVyPM
0 1 S1140-p RPEDsFMsVyPMQtE
0 1 Y1142-p EDsFMsVyPMQtEHH
0 2 T1146-p MsVyPMQtEHHQtPL
0 2 T1151-p MQtEHHQtPLDYNRR
0 2 T1160-p LDYNRRGtSLMEDDE
0 1 S1161 DYNRRGtSLMEDDEE
0 2 S1177-p IVEDVMMssEGRIED
0 2 S1178-p VEDVMMssEGRIEDL
0 1 T1193-p NEGMDFDtMDIDLPP
0 1 S1219-p PDFFDPAsIMDEsVL
2 6 S1224-p PAsIMDEsVLGVsMF
0 3 S1229-p DEsVLGVsMF_____
  STAG2 iso2  
S17 DFNLLQESETHFSSD
T132 SGCKGVVTAEMFRHM
S173 PQWKKFKSSFCEFIG
S174 QWKKFKSSFCEFIGV
K270 RLELLLQKRKELQEN
K363 YNKELNSKLELFTSR
Y433 VAAGEFLYKKLFSRR
T602 FDLEIYTTGRLEKHL
K607 YTTGRLEKHLDALLR
K607 YTTGRLEKHLDALLR
K664 LIDELADKFNRLLED
Y685 EPDEDDAYQVLSTLK
K692 YQVLSTLKRITAFHN
T737 VIHALQCTHYVILWQ
T749 LWQLAKITESSSTKE
S751 QLAKITESSSTKEDL
S752 LAKITESSSTKEDLL
K755 ITESSSTKEDLLRLK
Y775 FCQICQHYLTNVNTT
S843 EQDDDNNSADGQQED
Y892 IFKQYMKYYNDYGDI
Y893 FKQYMKYYNDYGDII
Y896 YMKYYNDYGDIIKET
K965 TFGLDQLKTREAIAM
Y1019 RQDKRTVYVYLEKFM
S1047 PLMSYRNSLLAGGDD
T1056 LAGGDDDTMSVISGI
S1058 GGDDDTMSVISGISS
S1061 DDTMSVISGISSRGS
S1064 MSVISGISSRGSTVR
S1065 SVISGISSRGSTVRS
R1066 VISGISSRGSTVRSK
S1072 SRGSTVRSKKSKPST
S1091 VVEGMQLSLTEESSS
S1099 LTEESSSSDSMWLSR
T1109 MWLSREQTLHTPVMM
T1112 SREQTLHTPVMMQTP
T1118 HTPVMMQTPQLTSTI
T1124 QTPQLTSTIMREPKR
S1137 KRLRPEDSFMSVYPM
S1140 RPEDSFMSVYPMQTE
Y1142 EDSFMSVYPMQTEHH
T1146 MSVYPMQTEHHQTPL
T1151 MQTEHHQTPLDYNTQ
T1197 QHAIRRGTSLMEDDE
S1198 HAIRRGTSLMEDDEE
S1214 IVEDVMMSSEGRIED
S1215 VEDVMMSSEGRIEDL
T1230 NEGMDFDTMDIDLPP
S1256 PDFFDPASIMDESVL
S1261 PASIMDESVLGVSMF
S1266 DESVLGVSMF_____
  mouse

 
S17-p DFNLLQEsETHFSSD
T132 SGCKGVVTAEMFRHM
S173 PQWKKFKSSFCEFIG
S174 QWKKFKSSFCEFIGV
K270-u RLELLLQkRKELQEN
K363 YNKELNSKLELFTSR
Y433-p VAAGEFLyKKLFSRR
T602 FDLEIYTTGRLEKHL
K607 YTTGRLEKHLDALLR
K607 YTTGRLEKHLDALLR
K664 LIDELADKFNRLLED
Y685 EPDEDDAYQVLSTLK
K692 YQVLSTLKRITAFHN
A737 VIHALQCAHYVILWQ
T749 LWQLAKITESTSTKE
S751 QLAKITESTSTKEDL
T752 LAKITESTSTKEDLL
K755 ITESTSTKEDLLRLK
Y775 FCQICQHYLTNVNTT
S843 EQDDDSNSADGQQED
Y892 IFKQYMKYYNDYGDI
Y893 FKQYMKYYNDYGDII
Y896 YMKYYNDYGDIIKET
K965-u TFGLDQLkTREAIAM
Y1019 RQDKRTVYVYLEKFM
S1047-p PLMSYRNsLLAGGDD
T1056-p LAGGDDDtMsVIsGM
S1058-p GGDDDtMsVIsGMss
S1061-p DDtMsVIsGMssRGS
S1064-p MsVIsGMssRGSTVR
S1065-p sVIsGMssRGSTVRs
R1066 VIsGMssRGSTVRsK
S1072-p sRGSTVRsKKSKPST
A1091 VVEGMQLALPEESSS
S1099-p LPEESSSsDSMWLSR
T1109-p MWLSREQtLHtPVMM
T1112-p SREQtLHtPVMMQTP
T1118 HtPVMMQTPQLTSTI
T1124 QTPQLTSTIMREPKR
S1137 KRLRPEDSFMSVYPM
S1140 RPEDSFMSVYPMQAE
Y1142 EDSFMSVYPMQAEHH
A1146 MSVYPMQAEHHQTPL
T1151 MQAEHHQTPLDYNRR
T1160-p LDYNRRGtsLMEDDE
S1161-p DYNRRGtsLMEDDEE
S1177-p IVEDVMMssEGRIED
S1178-p VEDVMMssEGRIEDL
T1193 NEGMDFDTMDIDLPP
S1219 PDFFDPASIMDESVL
S1224 PASIMDESVLGVSMF
S1229 DESVLGVSMF_____
  rat

 
S17 DFNLLQESETHFSSD
T132 SGCKGVVTAEMFRHM
S173 PQWKKFKSSFCEFIG
S174 QWKKFKSSFCEFIGV
K270 RLELLLQKRKELQEN
K363 YNKELNSKLELFTSR
Y433 VAAGEFLYKKLFSRR
T602 FDLEIYTTGRLEKHL
K607 YTTGRLEKHLDALLR
K607 YTTGRLEKHLDALLR
K664 LIDELADKFNRLLED
Y685 EPDEDDAYQVLSTLK
K692 YQVLSTLKRITAFHN
A737 VIHALQCAHYVILWQ
T749 LWQLAKITESTSTKE
S751 QLAKITESTSTKEDL
T752 LAKITESTSTKEDLL
K755 ITESTSTKEDLLRLK
Y775 FCQICQHYLTNVNTT
S843 EQDDDSNSADGQQED
Y892 IFKQYMKYYNDYGDI
Y893 FKQYMKYYNDYGDII
Y896 YMKYYNDYGDIIKET
K965 TFGLDQLKTREAIAM
Y1019-p RQDKRTVyVYLEKFM
S1047 PLMSYRNSLLAGGDD
T1056 LAGGDDDTMSVISGM
S1058 GGDDDTMSVISGMSS
S1061 DDTMSVISGMSSRGS
S1064 MSVISGMSSRGSTVR
S1065 SVISGMSSRGSTVRS
R1066 VISGMSSRGSTVRSK
S1072 SRGSTVRSKKSKPST
A1091 VLEGMQLALPEESSS
S1099 LPEESSSSDSMWLSR
T1109 MWLSREQTLHTPVMM
T1112 SREQTLHTPVMMQTP
T1118 HTPVMMQTPQLTSTI
T1124 QTPQLTSTIMREPKR
S1137 KRLRPEDSFMSVYPM
S1140 RPEDSFMSVYPMQTE
Y1142 EDSFMSVYPMQTEHH
T1146 MSVYPMQTEHHQTPL
T1151 MQTEHHQTPLDYNQR
T1160 LDYNQRGTSIMEDDE
S1161 DYNQRGTSIMEDDEE
S1177 IVEDVMMSSEGRIED
S1178 VEDVMMSSEGRIEDL
T1193 NEGMDFDTMDIDLPP
S1219 PDFFDPASIMDESVL
S1224 PASIMDESVLGVSMF
S1229 DESVLGVSMF_____
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