Reviewed, UniProtKB/Swiss-Prot Q8CG48 (SMC2_MOUSE)

Names and origin

Protein names

Recommended name:
    Structural maintenance of chromosomes protein 2
Alternative name(s):
    Chromosome-associated protein E
    XCAP-E homolog
    FGF-inducible protein 16

Gene names

Name:	Smc2
Synonyms:	Cape, Fin16, Smc2l1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases By similarity.
Subunit structure	Forms an heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase By similarity.
Domain	The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer By similarity.
Sequence similarities	Belongs to the SMC family. SMC2 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromosome Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Wasf2	Q8BH43	2	EBI-643436,EBI-643162

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1191	1191	Structural maintenance of chromosomes protein 2		PRO_0000118996
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	508 – 671	164	Flexible hinge
	Coiled coil	173 – 507	335	Potential
	Coiled coil	672 – 936	265	Potential
	Coiled coil	963 – 1031	69	Potential
	Compositional bias	1085 – 1120	36	Ala/Asp-rich (DA-box)
Experimental info
	Sequence conflict	62	1	F → L in BAB28654. Ref.2
	Sequence conflict	62	1	F → L in BAB31946. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8CG48-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 582C937D019FD893	FASTA	1,191	134,273
	10 20 30 40 50 60 MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 70 80 90 100 110 120 NFQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE ITVTRQVVIG GRNKYLINGV 130 140 150 160 170 180 NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA 190 200 210 220 230 240 AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL 250 260 270 280 290 300 RAEDTKERSA GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE 310 320 330 340 350 360 DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK EVKKITDGLH 370 380 390 400 410 420 GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMIACKNDIS KAQTEAKQAQ 430 440 450 460 470 480 MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA FEAVKKAKEK LETEMKKLNY EENKEEKLLE 490 500 510 520 530 540 KHRQLSRDIN NLKGKHEALL AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA 550 560 570 580 590 600 LEVVAGERLY NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 610 620 630 640 650 660 DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV TLGGDVFDPH 670 680 690 700 710 720 GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE ELAGLKNVAE KYRQLKQQWE 730 740 750 760 770 780 MKTEEGDLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK STKEIQKKAE EKYEALENKM 790 800 810 820 830 840 KNAEAEREKE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL 850 860 870 880 890 900 DAVNEAIKAY EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN 910 920 930 940 950 960 LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ PNSAYDFKTN 970 980 990 1000 1010 1020 NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND LMKKKRIVEN DKSKILATIE 1030 1040 1050 1060 1070 1080 DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE 1090 1100 1110 1120 1130 1140 NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF 1150 1160 1170 1180 1190 IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQSQAGKIP KEAKSRGKEP N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The evolution of SMC proteins: phylogenetic analysis and structural implications." Cobbe N., Heck M.M.S. Mol. Biol. Evol. 21:332-347(2004) [PubMed: 14660695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284. Strain: C57BL/6J. Tissue: Embryo.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 562-570, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Induction of expression of growth-related genes by FGF-4 in mouse fibroblasts." Guthridge M.A., Seldin M., Basilico C. Oncogene 12:1267-1278(1996) [PubMed: 8649829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ534939 mRNA. Translation: CAD59182.1. AK013109 mRNA. Translation: BAB28654.1. AK019977 mRNA. Translation: BAB31946.1. U42385 mRNA. Translation: AAB08867.1. Different initiation.
IPI	IPI00889938.
UniGene	Mm.2999
3D structure databases
HSSP	HSSP built from PDB template 1IC2 based on UniProtKB P04268.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CG48. 1 interaction.
PTM databases
PhosphoSite	Q8CG48.
Genome annotation databases
Ensembl	ENSMUSG00000028312. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:106067. Smc2.
Phylogenomic databases
HOVERGEN	Q8CG48.
Gene expression databases
ArrayExpress	Q8CG48.
Bgee	Q8CG48.
CleanEx	MM_SMC2.
GermOnline	ENSMUSG00000028312. Mus musculus.
Family and domain databases
InterPro	IPR003395. RecF/RecN/SMC_N. IPR010935. SMC_hinge. [Graphical view]
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

SMC2_MOUSE

Accession

Primary (citable) accession number: Q8CG48
Secondary accession number(s): Q61076, Q9CS17, Q9CSD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)