Q9CU62 (SMC1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Structural maintenance of chromosomes protein 1A
Short name=SMC protein 1A
Short name=SMC-1-alpha
Short name=SMC-1A

Alternative name(s):
Chromosome segregation protein SmcB
Sb1.8

Gene names

Name:	Smc1a
Synonyms:	Sb1.8, Smc1, Smc1l1, Smcb

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	1233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint By similarity. Central component of cohesin complex. The cohesin complex is 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. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
Subunit structure	Interacts with POLE and BRCA1. Interacts with SYCP2. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/APRIN and PDS5B/SCC-112. Interacts with NDC80 By similarity. Forms a heterodimer with SMC3 in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. In germ cell cohesin complexes, SMC1A is mutually exclusive with SMC1B. Interacts with RPGR By similarity. Ref.1 Ref.5
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Note: Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function By similarity. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex 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.
Tissue specificity	Ubiquitous.
Domain	The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure By similarity.
Post-translational modification	Phosphorylated upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation By similarity.
Sequence similarities	Belongs to the SMC family. SMC1 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA repair Meiosis Mitosis
Cellular component	Centromere Chromosome Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle checkpoint Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome condensation Inferred from electronic annotation. Source: InterPro meiosis Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of DNA endoreduplication Inferred from electronic annotation. Source: Compara response to radiation Inferred from sequence or structural similarity. Source: UniProtKB signal transduction in response to DNA damage Inferred from sequence or structural similarity. Source: UniProtKB sister chromatid cohesion Inferred from electronic annotation. Source: Compara stem cell maintenance Inferred from mutant phenotype PubMed 20720539. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara kinetochore Inferred from sequence or structural similarity. Source: UniProtKB meiotic cohesin complex Inferred from direct assay PubMed 21527826. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB mediator complex binding Inferred from direct assay PubMed 20720539. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1233

1233

Structural maintenance of chromosomes protein 1A

PRO_0000118990

Regions

Nucleotide binding

32 – 39

8

ATP Potential

Region

504 – 666

163

Flexible hinge

Coiled coil

104 – 124

21

Potential

Coiled coil

163 – 503

341

Potential

Coiled coil

667 – 935

269

Potential

Coiled coil

988 – 1068

81

Potential

Compositional bias

1128 – 1163

36

Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue

358

1

Phosphoserine By similarity

Modified residue

360

1

Phosphoserine By similarity

Modified residue

648

1

N6-acetyllysine By similarity

Modified residue

713

1

N6-acetyllysine By similarity

Modified residue

957

1

Phosphoserine By similarity

Modified residue

966

1

Phosphoserine By similarity

Modified residue

970

1

Phosphoserine By similarity

Experimental info

Sequence conflict

321

1

N → H in AAD27753. Ref.1

Sequence conflict

679

1

E → G in AAD27753. Ref.1

Sequence conflict

922

1

K → E in AAD27753. Ref.1

Sequence conflict

944

1

K → E in AAD27753. Ref.1

Sequence conflict

977

1

A → G in BAE43202. Ref.4

Sequence conflict

1013

1

Q → R in AAD27753. Ref.1

Secondary structure

1

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1233

Helix Strand Turn

Details...

Helix

501 – 510

10

Helix

512 – 514

3

Beta strand

515 – 518

4

Helix

519 – 522

4

Beta strand

523 – 527

5

Helix

528 – 530

3

Helix

531 – 538

8

Helix

539 – 542

4

Beta strand

545 – 548

4

Helix

550 – 562

13

Beta strand

568 – 572

5

Turn

573 – 575

3

Helix

583 – 587

5

Beta strand

592 – 594

3

Helix

595 – 597

3

Beta strand

598 – 602

5

Helix

603 – 605

3

Helix

606 – 612

7

Turn

613 – 615

3

Beta strand

617 – 621

5

Helix

622 – 630

9

Beta strand

631 – 634

4

Beta strand

638 – 640

3

Beta strand

652 – 654

3

Helix

656 – 662

7

Helix

665 – 670

6

Turn

671 – 673

3

Sequences

	Sequence		Length	Mass (Da)
	Q9CU62 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: E62CEB174854D9A6	FASTA	1,233	143,235
	10 20 30 40 50 60 MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 70 80 90 100 110 120 LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 130 140 150 160 170 180 LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE 190 200 210 220 230 240 DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK 250 260 270 280 290 300 ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 310 320 330 340 350 360 AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS 370 380 390 400 410 420 QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK 430 440 450 460 470 480 IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV 490 500 510 520 530 540 MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK 550 560 570 580 590 600 NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 610 620 630 640 650 660 EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK 670 680 690 700 710 720 AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE 730 740 750 760 770 780 QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF 790 800 810 820 830 840 CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ 850 860 870 880 890 900 TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 910 920 930 940 950 960 ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE 970 980 990 1000 1010 1020 ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI 1030 1040 1050 1060 1070 1080 AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN 1090 1100 1110 1120 1130 1140 IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL 1150 1160 1170 1180 1190 1200 LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 1210 1220 1230 IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the components of the putative mammalian sister chromatid cohesion complex." Darwiche N., Freeman L.A., Strunnikov A. Gene 233:39-47(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3 AND RAD21. Tissue: Embryo.
[2]	"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.
[3]	"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].
[4]	"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 1-301 AND 977-1233. Strain: C57BL/6J and NOD. Tissue: Hippocampus, Pancreas and Thymus.
[5]	"Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I." Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S., Barbero J.L. Nat. Cell Biol. 3:761-766(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STAG3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF047600 mRNA. Translation: AAD27753.1.
AL672180 Genomic DNA. Translation: CAM23830.1.
BC131667 mRNA. Translation: AAI31668.1.
AK007334 mRNA. Translation: BAE43202.1.
AK013648 mRNA. Translation: BAB28937.1.
AK017948 mRNA. Translation: BAB31016.3.
AK088183 mRNA. Translation: BAC40193.1.

IPI

IPI00123870.

RefSeq

NP_062684.2. NM_019710.2.

UniGene

Mm.482095.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WD5	X-ray	2.70	A	461-685	[»]

ProteinModelPortal

Q9CU62.

SMR

Q9CU62. Positions 2-161, 499-675, 1059-1223.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-57021N.

IntAct

Q9CU62. 2 interactions.

STRING

10090.ENSMUSP00000044645.

PTM databases

PhosphoSite

Q9CU62.

Proteomic databases

PaxDb

Q9CU62.

PRIDE

Q9CU62.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.

GeneID

24061.

KEGG

mmu:24061.

Organism-specific databases

CTD

8243.

MGI

MGI:1344345. Smc1a.

Phylogenomic databases

eggNOG

COG1196.

GeneTree

ENSGT00580000081569.

HOGENOM

HOG000195481.

HOVERGEN

HBG039593.

InParanoid

A2AFQ5.

KO

K06636.

OrthoDB

EOG4HX507.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

ArrayExpress

Q9CU62.

Bgee

Q9CU62.

CleanEx

MM_SMC1A.

Genevestigator

Q9CU62.

GermOnline

ENSMUSG00000041133. Mus musculus.

Family and domain databases

InterPro

IPR003395. RecF/RecN/SMC.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]

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.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9CU62.

NextBio

304025.

SOURCE

Search...

Entry information

Entry name

SMC1A_MOUSE

Accession

Primary (citable) accession number: Q9CU62
Secondary accession number(s): A2AFQ5 , Q3V480, Q9CUX9, Q9D959, Q9WTU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program