Q8N3U4 (STAG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cohesin subunit SA-2

Alternative name(s):
SCC3 homolog 2
Stromal antigen 2

Gene names

Name:	STAG2
Synonyms:	SA2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Subunit structure	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.
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex.
Post-translational modification	Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation By similarity. Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the SCC3 family. Contains 1 SCD (stromalin conservative) domain.
Sequence caution	The sequence CAA99732.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Meiosis Mitosis
Cellular component	Centromere Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic metaphase/anaphase transition Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of DNA endoreduplication Inferred from mutant phenotype. Source: BHF-UCL sister chromatid cohesion Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	chromatin Inferred from direct assay. Source: UniProtKB chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDS5A	Q29RF7	3	EBI-1057252,EBI-1175454
PDS5B	Q9NTI5	3	EBI-1057252,EBI-1175604
SMC3	Q9UQE7	6	EBI-1057252,EBI-80718

Alternative products

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

Isoform 1 (identifier: Q8N3U4-1)

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: Q8N3U4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1156: N → NTQVTWMLAQRQQEEARQQQERAAMSYVKLRTNLQHAI

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1231	1231	Cohesin subunit SA-2		PRO_0000120185
Regions
	Domain	293 – 378	86	SCD
	Compositional bias	1096 – 1101	6	Poly-Ser
Amino acid modifications
	Modified residue	607	1	N6-acetyllysine Ref.13
	Modified residue	1058	1	Phosphoserine Ref.11 Ref.12
	Modified residue	1061	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	1065	1	Phosphoserine Ref.11
	Modified residue	1112	1	Phosphothreonine Ref.12
	Modified residue	1160	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	1156	1	N → NTQVTWMLAQRQQEEARQQQ ERAAMSYVKLRTNLQHAI in isoform 2.		VSP_041119
	Natural variant	699	1	N → K. Corresponds to variant rs6655782 [ dbSNP | Ensembl ].		VAR_060114
Experimental info
	Sequence conflict	46	1	G → D in CAD38591. Ref.1
	Sequence conflict	302	1	A → R in CAA99732. Ref.5
	Sequence conflict	327	1	S → G in CAD38591. Ref.1
	Sequence conflict	607 – 608	2	KH → ND in CAA99732. Ref.5
	Sequence conflict	706	1	W → R in CAA99732. Ref.5
	Sequence conflict	710	1	A → V in CAD38591. Ref.1
	Sequence conflict	835	1	I → T in CAD38591. Ref.1
	Sequence conflict	971	1	A → T in CAH18271. Ref.1
	Sequence conflict	992	1	H → Y in CAD38591. Ref.1
	Sequence conflict	1105	1	S → T in CAA99732. Ref.5
	Sequence conflict	1144	1	M → K in CAA99732. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 3. Checksum: 692358EFFFF61BB9	FASTA	1,231	141,326
	10 20 30 40 50 60 MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG 70 80 90 100 110 120 GKPPSGPNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF 130 140 150 160 170 180 FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG 190 200 210 220 230 240 VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN 250 260 270 280 290 300 MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRDA 310 320 330 340 350 360 IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL 370 380 390 400 410 420 NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS SEEVLTAEDC ENVYHLVYSA 430 440 450 460 470 480 HRPVAVAAGE FLYKKLFSRR DPEEDGMMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL 490 500 510 520 530 540 VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG 550 560 570 580 590 600 RGTGKRVLTA KEKKTQLDDR TKITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY 610 620 630 640 650 660 TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE 670 680 690 700 710 720 LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI 730 740 750 760 770 780 ENGDMPEQIV IHALQCTHYV ILWQLAKITE SSSTKEDLLR LKKQMRVFCQ ICQHYLTNVN 790 800 810 820 830 840 TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD 850 860 870 880 890 900 NNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII 910 920 930 940 950 960 KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE LARRFALTFG 970 980 990 1000 1010 1020 LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV 1030 1040 1050 1060 1070 1080 YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGISSRGSTV RSKKSKPSTG 1090 1100 1110 1120 1130 1140 KRKVVEGMQL SLTEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS 1150 1160 1170 1180 1190 1200 VYPMQTEHHQ TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP 1210 1220 1230 SKNRRERTEL KPDFFDPASI MDESVLGVSM F
	Isoform 2 [UniParc]. Checksum: 38F24736F06D9054	FASTA	1,268	145,751
	10 20 30 40 50 60 MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG 70 80 90 100 110 120 GKPPSGPNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF 130 140 150 160 170 180 FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG 190 200 210 220 230 240 VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN 250 260 270 280 290 300 MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRDA 310 320 330 340 350 360 IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL 370 380 390 400 410 420 NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS SEEVLTAEDC ENVYHLVYSA 430 440 450 460 470 480 HRPVAVAAGE FLYKKLFSRR DPEEDGMMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL 490 500 510 520 530 540 VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG 550 560 570 580 590 600 RGTGKRVLTA KEKKTQLDDR TKITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY 610 620 630 640 650 660 TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE 670 680 690 700 710 720 LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI 730 740 750 760 770 780 ENGDMPEQIV IHALQCTHYV ILWQLAKITE SSSTKEDLLR LKKQMRVFCQ ICQHYLTNVN 790 800 810 820 830 840 TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD 850 860 870 880 890 900 NNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII 910 920 930 940 950 960 KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE LARRFALTFG 970 980 990 1000 1010 1020 LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV 1030 1040 1050 1060 1070 1080 YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGISSRGSTV RSKKSKPSTG 1090 1100 1110 1120 1130 1140 KRKVVEGMQL SLTEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS 1150 1160 1170 1180 1190 1200 VYPMQTEHHQ TPLDYNTQVT WMLAQRQQEE ARQQQERAAM SYVKLRTNLQ HAIRRGTSLM 1210 1220 1230 1240 1250 1260 EDDEEPIVED VMMSSEGRIE DLNEGMDFDT MDIDLPPSKN RRERTELKPD FFDPASIMDE SVLGVSMF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Retina and Spinal cord.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM 1). Tissue: Eye.
[5]	"SA-1, a nuclear protein encoded by one member of a novel gene family: molecular cloning and detection in hemopoietic organs." Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I., Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G., Aracil M., Marquez G., Barbero J.L., Zipori D. Gene 195:151-159(1997) [PubMed: 9305759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-1231 (ISOFORM 1). Tissue: Thymus.
[6]	Erratum Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I., Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G., Aracil M., Marquez G., Barbero J.L., Zipori D. Gene 206:283-286(1998)
[7]	"Characterization of vertebrate cohesin complexes and their regulation in prophase." Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M. J. Cell Biol. 151:749-762(2000) [PubMed: 11076961] [Abstract] Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND SMC3.
[8]	"STAG2 and Rad21 mammalian mitotic cohesins are implicated in meiosis." Prieto I., Pezzi N., Buesa J.M., Kremer L., Barthelemy I., Carreiro C., Roncal F., Martinez A., Gomez L., Fernandez R., Martinez-A C., Barbero J.L. EMBO Rep. 3:543-550(2002) [PubMed: 12034751] [Abstract] Cited for: FUNCTION IN EARLY STEPS OF MEIOSIS.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-1058; SER-1061 AND SER-1065, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058; SER-1061 AND THR-1112, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, MASS SPECTROMETRY.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL831939 mRNA. Translation: CAD38591.1. CR749433 mRNA. Translation: CAH18271.1. AL355476 Genomic DNA. Translation: CAI40990.1. AL355476 Genomic DNA. Translation: CAI40991.1. CH471107 Genomic DNA. Translation: EAX11853.1. CH471107 Genomic DNA. Translation: EAX11854.1. CH471107 Genomic DNA. Translation: EAX11855.1. CH471107 Genomic DNA. Translation: EAX11856.1. CH471107 Genomic DNA. Translation: EAX11857.1. BC001765 mRNA. Translation: AAH01765.2. Z75331 mRNA. Translation: CAA99732.1. Different initiation.
IPI	IPI00470883. IPI00552978.
RefSeq	NP_001036214.1. NM_001042749.1. NP_001036215.1. NM_001042750.1. NP_001036216.1. NM_001042751.1. NP_006594.3. NM_006603.4.
UniGene	Hs.496710. Hs.624663.
3D structure databases
ProteinModelPortal	Q8N3U4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35418N.
IntAct	Q8N3U4. 11 interactions.
MINT	MINT-6178117.
STRING	Q8N3U4.
PTM databases
PhosphoSite	Q8N3U4.
Polymorphism databases
DMDM	73621291.
Proteomic databases
PRIDE	Q8N3U4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371144; ENSP00000360186; ENSG00000101972. ENST00000371157; ENSP00000360199; ENSG00000101972. ENST00000371160; ENSP00000360202; ENSG00000101972.
GeneID	10735.
KEGG	hsa:10735.
UCSC	uc004etz.2. human.
Organism-specific databases
CTD	10735.
GeneCards	GC0XP123094.
H-InvDB	HIX0017034.
HGNC	HGNC:11355. STAG2.
HPA	HPA002857.
MIM	300826. gene.
neXtProt	NX_Q8N3U4.
PharmGKB	PA36177.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11650.
GeneTree	ENSGT00390000014094.
HOVERGEN	HBG057636.
PhylomeDB	Q8N3U4.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q8N3U4.
Bgee	Q8N3U4.
CleanEx	HS_STAG2.
Genevestigator	Q8N3U4.
GermOnline	ENSG00000101972. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR020839. SCD. IPR013721. STAG. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 5 hits.
KO	K06671.
Pfam	PF08514. STAG. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS51425. SCD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	40752.
SOURCE	Search...

Entry information

Entry name

STAG2_HUMAN

Accession

Primary (citable) accession number: Q8N3U4
Secondary accession number(s): B1AMT5 , D3DTF5, O00540, Q5JTI6, Q68DE9, Q9H1N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	August 16, 2005
Last modified:	January 25, 2012
This is version 97 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.