Reviewed, UniProtKB/Swiss-Prot Q14683 (SMC1A_HUMAN)

Names and origin

Protein names

Recommended name:
    Structural maintenance of chromosomes protein 1A
Alternative name(s):
    SMC1alpha protein
    Sb1.8

Gene names

Name:	SMC1A
Synonyms:	DXS423E, KIAA0178, SB1.8, SMC1, SMC1L1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in chromosome cohesion during cell cycle and in DNA repair. 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. Ref.6
Subunit structure	Interacts with POLE. Interacts with SYCP2. Interacts with BRCA1. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/APRIN and PDS5B/SCC-112 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 BRCA1. Interacts with NDC80.
Subcellular location	Nucleus. Kinetochore. 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 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. 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. Integral component of the functional centromere-kinetochore complex at the kinetochore region during mitosis. Ref.10
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 by ATM upon ionizing radiation in a NBS1-dependent manner. Phosphorylated by ATR upon DNA methylation in a MSH2/MSH6-dependent manner. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation. Ref.6 Ref.11 Ref.12 Ref.15 Ref.16
Involvement in disease	Defects in SMC1A are the cause of Cornelia de Lange syndrome type 2 (CDLS2) [MIM:300590]; also known as Cornelia de Lange syndrome X-linked. CDLS is a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. CDLS is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation and various other malformations including gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. Ref.18
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	Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction Ref.6 Inferred from direct assay. Source: UniProtKB DNA repair Ref.6 Traceable author statement. Source: UniProtKB cell cycle checkpoint Ref.6 Inferred from direct assay. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from sequence or structural similarity. Source: UniProtKB mitotic sister chromatid cohesion Ref.10 Traceable author statement. Source: UniProtKB mitotic spindle organization Ref.10 Traceable author statement. Source: UniProtKB nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome response to radiation Ref.6 Inferred from expression pattern. Source: UniProtKB
Cellular component	cohesin core heterodimer Ref.9 Traceable author statement. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell condensed nuclear chromosome Ref.1 Traceable author statement. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Ref.9 Inferred from direct assay. Source: UniProtKB microtubule motor activity Ref.10 Non-traceable author statement. Source: UniProtKB protein heterodimerization activity Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATM	Q13315	1	EBI-80690,EBI-495465
BRCA1	P38398	1	EBI-80690,EBI-349905
CASP4	P49662	1	EBI-80690,EBI-1057327
CDK4	P11802	1	EBI-80690,EBI-295644
MCM6	Q14566	1	EBI-80690,EBI-374900
MCM7	P33993	6	EBI-80690,EBI-355924
POLA1	P09884	1	EBI-80690,EBI-850026
RFC1	P35251	1	EBI-80690,EBI-476616
STYXL1	Q9Y6J8	1	EBI-80690,EBI-1044511

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_0000118989
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	504 – 659	156	Flexible hinge
	Coiled coil	104 – 124	21	Potential
	Coiled coil	163 – 503	341	Potential
	Coiled coil	660 – 935	276	Potential
	Coiled coil	991 – 1068	78	Potential
	Compositional bias	1128 – 1163	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	358	1	Phosphoserine Ref.15
	Modified residue	360	1	Phosphoserine Ref.12 Ref.15 Ref.16
	Modified residue	951	1	Phosphoserine Ref.15
	Modified residue	957	1	Phosphoserine; by ATM Ref.6 Ref.12 Ref.15 Ref.16
	Modified residue	962	1	Phosphoserine Ref.12
	Modified residue	966	1	Phosphoserine; by ATM and ATR Ref.6 Ref.11 Ref.15
	Modified residue	970	1	Phosphoserine Ref.16
Natural variations
	Natural variant	28	1	T → P: dbSNP rs34530151.		VAR_052438
	Natural variant	493	1	E → A in CDLS2. Ref.18		VAR_026529
	Natural variant	832	1	Missing in CDLS2. Ref.18		VAR_026530
Experimental info
	Mutagenesis	957	1	S → A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966. Ref.6
	Mutagenesis	966	1	S → A: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957. Ref.6 Ref.11
	Sequence conflict	163 – 164	2	EL → DV in AAB34405. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q14683-1 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: E0A44CA7476C88A6	FASTA	1,233	143,233
	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 DSVSGSQRIS 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]	"The human SB1.8 gene (DXS423E) encodes a putative chromosome segregation protein conserved in lower eukaryotes and prokaryotes." Rocques P.J., Clark J., Ball S., Crew J., Gill S., Christodoulou Z., Borts R.H., Louis E.J., Davies K.E., Cooper C.S. Hum. Mol. Genet. 4:243-249(1995) [PubMed: 7757074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed: 8724849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"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].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint." Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J. Genes Dev. 16:571-582(2002) [PubMed: 11877377] [Abstract] Cited for: PROTEIN SEQUENCE OF 945-984, FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT SER-957 AND SER-966, MUTAGENESIS OF SER-957 AND SER-966.
[7]	"HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins." Chen Y., Sharp Z.D., Lee W.-H. J. Biol. Chem. 272:24081-24087(1997) [PubMed: 9295362] [Abstract] Cited for: INTERACTION WITH NDC80.
[8]	"Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins." Zheng L., Chen Y., Lee W.-H. Mol. Cell. Biol. 19:5417-5428(1999) [PubMed: 10409732] [Abstract] Cited for: INTERACTION WITH NDC80.
[9]	"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 SMC3; STAG1 OR STAG2.
[10]	"Localization of human SMC1 protein at kinetochores." Gregson H.C., Van Hooser A.A., Ball A.R. Jr., Brinkley B.R., Yokomori K. Chromosome Res. 10:267-277(2002) [PubMed: 12199140] [Abstract] Cited for: SUBCELLULAR LOCATION DURING CELL CYCLE.
[11]	"MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation." Wang Y., Qin J. Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003) [PubMed: 14657349] [Abstract] Cited for: PHOSPHORYLATION AT SER-966, MUTAGENESIS OF SER-966.
[12]	"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-360; SER-957 AND SER-962, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates." Rankin S., Ayad N.G., Kirschner M.W. Mol. Cell 18:185-200(2005) [PubMed: 15837422] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC3; RAD21; PDS5A AND PDS5B.
[14]	Erratum Rankin S., Ayad N.G., Kirschner M.W. Mol. Cell 18:609-609(2005)
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-360; SER-951; SER-957 AND SER-966, MASS SPECTROMETRY.
[16]	"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-360; SER-957 AND SER-970, MASS SPECTROMETRY.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"X-linked Cornelia de Lange syndrome owing to SMC1L1 mutations." Musio A., Selicorni A., Focarelli M.L., Gervasini C., Milani D., Russo S., Vezzoni P., Larizza L. Nat. Genet. 38:528-530(2006) [PubMed: 16604071] [Abstract] Cited for: VARIANTS CDLS2 ALA-493 AND GLN-832 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	S78271 mRNA. Translation: AAB34405.1. D80000 mRNA. Translation: BAA11495.2. AL161779, Z97054 Genomic DNA. Translation: CAI42089.1. Z97054, AL161779 Genomic DNA. Translation: CAI42646.1. BC112127 mRNA. Translation: AAI12128.1.
IPI	IPI00291939.
PIR	I54383.
RefSeq	NP_006297.2.
UniGene	Hs.211602
3D structure databases
HSSP	HSSP built from PDB template 1GMJ based on UniProtKB P01096.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14683. 22 interactions.
PTM databases
PhosphoSite	Q14683.
Proteomic databases
PeptideAtlas	Q14683.
PRIDE	Q14683.
Genome annotation databases
Ensembl	ENSG00000072501. Homo sapiens. [Contig view]
GeneID	8243.
KEGG	hsa:8243.
NMPDR	fig|9606.3.peg.32835.
UCSC	uc004dsg.1. human.
Organism-specific databases
GeneCards	GC0XM053417.
H-InvDB	HIX0056242.
HGNC	HGNC:11111. SMC1A.
HPA	HPA005499.
MIM	300040. gene. 300590. phenotype.
Orphanet	199. Cornelia de Lange syndrome.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q14683.
HOVERGEN	Q14683.
OMA	Q14683. QPSPFFV.
Enzyme and pathway databases
Reactome	REACT_125. Processing of Capped Intron-Containing Pre-mRNA. REACT_152. Cell Cycle, Mitotic. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q14683.
Bgee	Q14683.
CleanEx	HS_SMC1A.
GermOnline	ENSG00000072501. Homo sapiens.
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]
ProDom	PD000006. ABC_transporter. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	31006.
SOURCE	Search...

Entry information

Entry name

SMC1A_HUMAN

Accession

Primary (citable) accession number: Q14683
Secondary accession number(s): O14995, Q16351, Q2M228

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2002
Last modified:	July 7, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)