Q14683 (SMC1A_HUMAN) 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):
Sb1.8

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. 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. Interacts with RPGR By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12
Subcellular location	Nucleus. Chromosome. Chromosome › centromere › 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
Involvement in disease	Cornelia de Lange syndrome 2 (CDLS2) [MIM:300590]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Miscellaneous	Mutated Cornelia de Lange cell lines display genomic instability and sensitivity to ionizing radiation and interstrand cross-linking agents.
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 Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Mental retardation
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Traceable author statement Ref.6. Source: UniProtKB cell cycle checkpoint Inferred from direct assay Ref.6. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome condensation Inferred from electronic annotation. Source: InterPro mRNA splicing, via spliceosome Traceable author statement. Source: Reactome meiosis Inferred from sequence or structural similarity. Source: UniProtKB mitotic metaphase/anaphase transition Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome mitotic sister chromatid cohesion Traceable author statement Ref.10. Source: UniProtKB mitotic spindle organization Traceable author statement Ref.10. Source: UniProtKB negative regulation of DNA endoreduplication Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL response to radiation Inferred from expression pattern Ref.6. Source: UniProtKB signal transduction in response to DNA damage Inferred from direct assay Ref.6. Source: UniProtKB stem cell maintenance Inferred from electronic annotation. Source: Compara
Cellular_component	cohesin core heterodimer Traceable author statement Ref.9. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell condensed nuclear chromosome Traceable author statement Ref.1. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA kinetochore Inferred from direct assay Ref.10. Source: UniProtKB meiotic cohesin complex Inferred from direct assay PubMed 21242291. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay Ref.9. Source: UniProtKB microtubule motor activity Non-traceable author statement Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCM7	P33993	8	EBI-80690,EBI-355924

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.14
	Modified residue	360	1	Phosphoserine Ref.14 Ref.15 Ref.18
	Modified residue	648	1	N6-acetyllysine Ref.17
	Modified residue	713	1	N6-acetyllysine Ref.17
	Modified residue	957	1	Phosphoserine; by ATM Ref.6 Ref.15 Ref.16 Ref.18
	Modified residue	966	1	Phosphoserine; by ATM and ATR Ref.6 Ref.11 Ref.14 Ref.18
	Modified residue	970	1	Phosphoserine Ref.15
Natural variations
	Natural variant	28	1	T → P. Corresponds to variant rs34530151 [ dbSNP | Ensembl ].		VAR_052438
	Natural variant	58 – 62	5	Missing in CDLS2.		VAR_062785
	Natural variant	133	1	F → V in CDLS2. Ref.22 Ref.25		VAR_062786
	Natural variant	141	1	E → K in CDLS2. Ref.25		VAR_062787
	Natural variant	196	1	R → H in CDLS2. Ref.22 Ref.23 Ref.25 Ref.26		VAR_062788
	Natural variant	268	1	Missing in CDLS2. Ref.25 Ref.26		VAR_062789
	Natural variant	306	1	Missing in CDLS2. Ref.25		VAR_062790
	Natural variant	398	1	R → Q in CDLS2. Ref.25		VAR_062791
	Natural variant	493	1	E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.21 Ref.24		VAR_026529
	Natural variant	496	1	R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.22 Ref.24 Ref.25		VAR_062792
	Natural variant	496	1	R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.22 Ref.24 Ref.25		VAR_062793
	Natural variant	683	1	Missing in CDLS2. Ref.25		VAR_062794
	Natural variant	693	1	R → G in CDLS2. Ref.25		VAR_062795
	Natural variant	711	1	R → Q in CDLS2. Ref.26		VAR_064542
	Natural variant	711	1	R → W in CDLS2. Ref.22 Ref.25		VAR_062796
	Natural variant	781	1	C → F in CDLS2. Ref.25		VAR_062797
	Natural variant	784	1	I → T in CDLS2. Ref.27		VAR_064543
	Natural variant	790	1	R → Q in CDLS2. Ref.22 Ref.25		VAR_062798
	Natural variant	816	1	R → G in CDLS2. Ref.25		VAR_062799
	Natural variant	832	1	Missing in CDLS2. Ref.21		VAR_026530
	Natural variant	1049	1	R → Q in CDLS2. Ref.25		VAR_062800
	Natural variant	1085	1	Y → C in CDLS2. Ref.23		VAR_062801
	Natural variant	1122	1	F → L in CDLS2. Ref.22 Ref.25		VAR_062802
	Natural variant	1123	1	R → W in CDLS2. Ref.25		VAR_062803
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 [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

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[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-966, MUTAGENESIS OF SER-966.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC3; RAD21; PDS5A AND PDS5B.
[13]	Erratum Rankin S., Ayad N.G., Kirschner M.W. Mol. Cell 18:609-609(2005)
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-360 AND SER-966, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-957 AND SER-970, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-648 AND LYS-713, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-957 AND SER-966, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS CDLS2 ALA-493 AND GLN-832 DEL.
[22]	"Mutations in cohesin complex members SMC3 and SMC1A cause a mild variant of Cornelia de Lange syndrome with predominant mental retardation." Deardorff M.A., Kaur M., Yaeger D., Rampuria A., Korolev S., Pie J., Gil-Rodriguez C., Arnedo M., Loeys B., Kline A.D., Wilson M., Lillquist K., Siu V., Ramos F.J., Musio A., Jackson L.S., Dorsett D., Krantz I.D. Am. J. Hum. Genet. 80:485-494(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDLS2 58-VAL--ARG-62 DEL; VAL-133; HIS-196; CYS-496; HIS-496; TRP-711; GLN-790 AND LEU-1122.
[23]	"Incidence and clinical features of X-linked Cornelia de Lange syndrome due to SMC1L1 mutations." Borck G., Zarhrate M., Bonnefont J.-P., Munnich A., Cormier-Daire V., Colleaux L. Hum. Mutat. 28:205-206(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDLS2 HIS-196 AND CYS-1085.
[24]	"Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding to DNA." Revenkova E., Focarelli M.L., Susani L., Paulis M., Bassi M.T., Mannini L., Frattini A., Delia D., Krantz I., Vezzoni P., Jessberger R., Musio A. Hum. Mol. Genet. 18:418-427(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS CDLS2 ALA-493; CYS-496 AND HIS-496, GENOMIC INSTABILITY OF CDLS CELL LINES TO IONIZING RADIATION.
[25]	"SMC1A expression and mechanism of pathogenicity in probands with X-Linked Cornelia de Lange syndrome." Liu J., Feldman R., Zhang Z., Deardorff M.A., Haverfield E.V., Kaur M., Li J.R., Clark D., Kline A.D., Waggoner D.J., Das S., Jackson L.G., Krantz I.D. Hum. Mutat. 30:1535-1542(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDLS2 58-VAL--ARG-62 DEL; VAL-133; LYS-141; HIS-196; LYS-268 DEL; SER-306 DEL; GLN-398; CYS-496; HIS-496; GLU-683 DEL; GLY-693; TRP-711; PHE-781; GLN-790; GLY-816; GLN-1049; LEU-1122 AND TRP-1123.
[26]	"Mutations and variants in the cohesion factor genes NIPBL, SMC1A, and SMC3 in a cohort of 30 unrelated patients with Cornelia de Lange syndrome." Pie J., Gil-Rodriguez M.C., Ciero M., Lopez-Vinas E., Ribate M.P., Arnedo M., Deardorff M.A., Puisac B., Legarreta J., de Karam J.C., Rubio E., Bueno I., Baldellou A., Calvo M.T., Casals N., Olivares J.L., Losada A., Hegardt F.G. , Krantz I.D., Gomez-Puertas P., Ramos F.J. Am. J. Med. Genet. A 152:924-929(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDLS2 HIS-196; LYS-268 DEL AND GLN-711.
[27]	"Hypertrophic cardiomyopathy in a girl with Cornelia de Lange syndrome due to mutation in SMC1A." Limongelli G., Russo S., Digilio M.C., Masciadri M., Pacileo G., Fratta F., Martone F., Maddaloni V., D'Alessandro R., Calabro P., Russo M.G., Calabro R., Larizza L. Am. J. Med. Genet. A 152:2127-2129(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDLS2 THR-784.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_006306.2.
UniGene	Hs.211602.
3D structure databases
ProteinModelPortal	Q14683.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-30911N.
IntAct	Q14683. 32 interactions.
MINT	MINT-233274.
STRING	9606.ENSP00000323421.
PTM databases
PhosphoSite	Q14683.
Polymorphism databases
DMDM	29336622.
Proteomic databases
PaxDb	Q14683.
PeptideAtlas	Q14683.
PRIDE	Q14683.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322213; ENSP00000323421; ENSG00000072501. ENST00000594240; ENSP00000471583; ENSG00000269384.
GeneID	8243.
KEGG	hsa:8243.
UCSC	uc004dsg.3. human.
Organism-specific databases
CTD	8243.
GeneCards	GC0XM053417.
HGNC	HGNC:11111. SMC1A.
HPA	CAB025404. HPA005499.
MIM	300040. gene. 300590. phenotype.
neXtProt	NX_Q14683.
Orphanet	199. Cornelia de Lange syndrome.
PharmGKB	PA35961.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1196.
HOGENOM	HOG000195481.
HOVERGEN	HBG039593.
InParanoid	Q14683.
KO	K06636.
OMA	NALVCET.
OrthoDB	EOG4HX507.
PhylomeDB	Q14683.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_1675. mRNA Processing. REACT_21300. Mitotic M-M/G1 phases. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q14683.
Bgee	Q14683.
CleanEx	HS_SMC1A.
Genevestigator	Q14683.
GermOnline	ENSG00000072501. Homo sapiens.
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
ChiTaRS	SMC1A. human.
GenomeRNAi	8243.
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:	May 1, 2013
This is version 139 of the entry and version 2 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.