Q8CG48 (SMC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Structural maintenance of chromosomes protein 2
Short name=SMC protein 2
Short name=SMC-2

Alternative name(s):
Chromosome-associated protein E
FGF-inducible protein 16
XCAP-E homolog

Gene names

Name:	Smc2
Synonyms:	Cape, Fin16, Smc2l1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1191 AA.
Sequence status	Complete.
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 a 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. Chromosome 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.
Sequence caution	The sequence AAB08867.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Inferred from electronic annotation. Source: InterPro cell division Inferred from electronic annotation. Source: UniProtKB-KW kinetochore organization Inferred from mutant phenotype PubMed 21795393. Source: MGI meiotic chromosome condensation Inferred from mutant phenotype PubMed 21795393. Source: MGI meiotic chromosome segregation Inferred from mutant phenotype PubMed 21795393. Source: MGI mitotic chromosome condensation Inferred from electronic annotation. Source: Compara sister chromatid cohesion Inferred from electronic annotation. Source: InterPro
Cellular_component	condensed chromosome Inferred from direct assay PubMed 21795393. Source: MGI condensin complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear chromosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Wasf2	Q8BH43	4	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)

Amino acid modifications

Modified residue

114

1

N6-acetyllysine By similarity

Modified residue

222

1

N6-acetyllysine By similarity

Modified residue

677

1

N6-acetyllysine By similarity

Modified residue

1158

1

N6-acetyllysine By similarity

Modified residue

1160

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

62

1

L → F in CAD59182. Ref.1

Secondary structure

1

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1191

Helix Strand Turn

Details...

Helix

519 – 521

3

Beta strand

522 – 525

4

Helix

526 – 528

3

Beta strand

531 – 533

3

Helix

535 – 537

3

Helix

538 – 545

8

Helix

546 – 550

5

Beta strand

552 – 555

4

Helix

557 – 566

10

Beta strand

573 – 577

5

Turn

578 – 580

3

Helix

588 – 598

11

Beta strand

602 – 605

4

Helix

606 – 609

4

Helix

614 – 616

3

Helix

617 – 624

8

Beta strand

628 – 632

5

Helix

633 – 641

9

Turn

643 – 645

3

Beta strand

649 – 651

3

Sequences

	Sequence		Length	Mass (Da)
	Q8CG48 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 56CC351A7855D0BB	FASTA	1,191	134,239
	10 20 30 40 50 60 MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 70 80 90 100 110 120 NLQDLVYKNG 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284. Strain: C57BL/6J. Tissue: Embryo.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Strain: C57BL/6. Tissue: Brain.
[6]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 562-570, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ534939 mRNA. Translation: CAD59182.1.
AK013109 mRNA. Translation: BAB28654.1.
AK019977 mRNA. Translation: BAB31946.1.
AL732619 Genomic DNA. Translation: CAM14006.1.
CH466565 Genomic DNA. Translation: EDL02299.1.
BC094380 mRNA. Translation: AAH94380.1.
U42385 mRNA. Translation: AAB08867.1. Different initiation.

IPI

IPI00987134.

RefSeq

NP_032043.3. NM_008017.3.

UniGene

Mm.2999.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L51	X-ray	1.51	A	506-666	[»]

ProteinModelPortal

Q8CG48.

SMR

Q8CG48. Positions 2-170, 462-688, 1033-1168.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8CG48. 1 interaction.

MINT

MINT-1748639.

PTM databases

PhosphoSite

Q8CG48.

Proteomic databases

PaxDb

Q8CG48.

PRIDE

Q8CG48.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312.
ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312.

GeneID

14211.

KEGG

mmu:14211.

UCSC

uc008swk.1. mouse.

Organism-specific databases

CTD

10592.

MGI

MGI:106067. Smc2.

Phylogenomic databases

eggNOG

COG1196.

GeneTree

ENSGT00550000074857.

HOVERGEN

HBG106605.

InParanoid

Q52KE9.

KO

K06674.

OMA

CQNGKIP.

OrthoDB

EOG49S65K.

Gene expression databases

ArrayExpress

Q8CG48.

Bgee

Q8CG48.

CleanEx

MM_SMC2.

Genevestigator

Q8CG48.

GermOnline

ENSMUSG00000028312. Mus musculus.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]

PANTHER

PTHR18937:SF9. PTHR18937:SF9. 1 hit.

Pfam

PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]

PIRSF

PIRSF005719. SMC. 1 hit.

SMART

SM00968. SMC_hinge. 1 hit.
[Graphical view]

SUPFAM

SSF75553. SMC_hinge. 1 hit.
SSF52540. SSF52540. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8CG48.

NextBio

285461.

SOURCE

Search...

Entry information

Entry name

SMC2_MOUSE

Accession

Primary (citable) accession number: Q8CG48
Secondary accession number(s): Q52KE9 , Q61076, Q9CS17, Q9CSD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program