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Protein

Structural maintenance of chromosomes protein 1A

Gene

Smc1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 39ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Smc1a
Synonyms:Sb1.8, Smc1, Smc1l1, Smcb
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1344345 Smc1a

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001189901 – 1233Structural maintenance of chromosomes protein 1AAdd BLAST1233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei358PhosphoserineBy similarity1
Modified residuei360PhosphoserineBy similarity1
Modified residuei648N6-acetyllysineBy similarity1
Modified residuei713N6-acetyllysineBy similarity1
Modified residuei957PhosphoserineBy similarity1
Modified residuei962PhosphoserineBy similarity1
Modified residuei966PhosphoserineBy similarity1
Modified residuei970PhosphoserineBy similarity1
Modified residuei1037N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9CU62

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9CU62

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9CU62

PeptideAtlas

More...
PeptideAtlasi
Q9CU62

PRoteomics IDEntifications database

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PRIDEi
Q9CU62

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9CU62

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9CU62

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000041133 Expressed in 286 organ(s), highest expression level in rostral migratory stream

CleanEx database of gene expression profiles

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CleanExi
MM_SMC1A

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9CU62 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9CU62 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms a heterodimer with SMC3 in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC 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 (PubMed:10375619). Interacts with STAG3 (PubMed:11483963). Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Found in a complex containing POLE and SMC3. Interacts with BRCA1, SYCP2, NDC80, RPGR and BRAT1. Found in a cohesin complex with SMC3, STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By similarity).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
204874, 42 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9CU62

Database of interacting proteins

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DIPi
DIP-57021N

Protein interaction database and analysis system

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IntActi
Q9CU62, 39 interactors

Molecular INTeraction database

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MINTi
Q9CU62

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000044645

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9CU62

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9CU62

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9CU62

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini515 – 629SMC hingeAdd BLAST115

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili104 – 124Sequence analysisAdd BLAST21
Coiled coili163 – 503Sequence analysisAdd BLAST341
Coiled coili667 – 935Sequence analysisAdd BLAST269
Coiled coili988 – 1068Sequence analysisAdd BLAST81

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1128 – 1163Ala/Asp-rich (DA-box)Add BLAST36

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The flexible SMC 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).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SMC family. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0018 Eukaryota
COG1196 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155614

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000195481

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG039593

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9CU62

KEGG Orthology (KO)

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KOi
K06636

Identification of Orthologs from Complete Genome Data

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OMAi
YMEAIVV

Database of Orthologous Groups

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OrthoDBi
EOG091G00R5

TreeFam database of animal gene trees

More...
TreeFami
TF101156

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR029683 SMC1A_metazoan
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf

The PANTHER Classification System

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PANTHERi
PTHR18937:SF170 PTHR18937:SF170, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF005719 SMC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00968 SMC_hinge, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF75553 SSF75553, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9CU62-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG
60 70 80 90 100
EKTSNLRVKT LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG
110 120 130 140 150
GSSEYKINNK VVQLHEYSEE LEKLGILIKA RNFLVFQGAV ESIAMKNPKE
160 170 180 190 200
RTALFEEISR SGELAQEYDK RKKEMVKAEE DTQFNYHRKK NIAAERKEAK
210 220 230 240 250
QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK ELASKNKEIE
260 270 280 290 300
KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
310 320 330 340 350
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF
360 370 380 390 400
EERMEEESQS QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ
410 420 430 440 450
KADQDRLDLE ERKKVETEAK IKQKLREIEE NQKRIEKLEE YITTSKQSLE
460 470 480 490 500
EQKKLEGELT EEVEMAKRRI DEINKELNQV MEQLGDARID RQESSRQQRK
510 520 530 540 550
AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK NMDAIIVDSE
560 570 580 590 600
KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
610 620 630 640 650
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG
660 670 680 690 700
VISGGASDLK AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ
710 720 730 740 750
VQSQAHGLQM RLKYSQSDLE QTKTRHLALN LQEKSKLESE LANFGPRIND
760 770 780 790 800
IKRIIQSRER EMKDLKEKMN QVEDEVFEEF CREIGVRNIR EFEEEKVKRQ
810 820 830 840 850
NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ TVKKDENEIE
860 870 880 890 900
KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
910 920 930 940 950
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI
960 970 980 990 1000
SQEEGSSQGE ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK
1010 1020 1030 1040 1050
QEMNTLQQKL NEQQSVLQRI AAPNMKAMEK LESVRDKFQE TSDEFEAARK
1060 1070 1080 1090 1100
RAKKAKQAFE QIKKERFDRF NACFESVATN IDEIYKALSR NSSAQAFLGP
1110 1120 1130 1140 1150
ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL LFAIHSYKPA
1160 1170 1180 1190 1200
PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
1210 1220 1230
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
Length:1,233
Mass (Da):143,235
Last modified:July 27, 2011 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE62CEB174854D9A6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
S4R179S4R179_MOUSE
Structural maintenance of chromosom...
Smc1a
54Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti321N → H in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti679E → G in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti922K → E in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti944K → E in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti977A → G in BAE43202 (PubMed:16141072).Curated1
Sequence conflicti1013Q → R in AAD27753 (PubMed:10375619).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF047600 mRNA Translation: AAD27753.1
AL672180 Genomic DNA No translation available.
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS30473.1

NCBI Reference Sequences

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RefSeqi
NP_062684.2, NM_019710.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.482095

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133

Database of genes from NCBI RefSeq genomes

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GeneIDi
24061

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:24061

UCSC genome browser

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UCSCi
uc009upx.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047600 mRNA Translation: AAD27753.1
AL672180 Genomic DNA No translation available.
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
CCDSiCCDS30473.1
RefSeqiNP_062684.2, NM_019710.2
UniGeneiMm.482095

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70A461-685[»]
ProteinModelPortaliQ9CU62
SMRiQ9CU62
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204874, 42 interactors
CORUMiQ9CU62
DIPiDIP-57021N
IntActiQ9CU62, 39 interactors
MINTiQ9CU62
STRINGi10090.ENSMUSP00000044645

PTM databases

iPTMnetiQ9CU62
PhosphoSitePlusiQ9CU62

Proteomic databases

EPDiQ9CU62
MaxQBiQ9CU62
PaxDbiQ9CU62
PeptideAtlasiQ9CU62
PRIDEiQ9CU62

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133
GeneIDi24061
KEGGimmu:24061
UCSCiuc009upx.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8243
MGIiMGI:1344345 Smc1a

Phylogenomic databases

eggNOGiKOG0018 Eukaryota
COG1196 LUCA
GeneTreeiENSGT00940000155614
HOGENOMiHOG000195481
HOVERGENiHBG039593
InParanoidiQ9CU62
KOiK06636
OMAiYMEAIVV
OrthoDBiEOG091G00R5
TreeFamiTF101156

Enzyme and pathway databases

ReactomeiR-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

Miscellaneous databases

EvolutionaryTraceiQ9CU62

Protein Ontology

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PROi
PR:Q9CU62

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000041133 Expressed in 286 organ(s), highest expression level in rostral migratory stream
CleanExiMM_SMC1A
ExpressionAtlasiQ9CU62 baseline and differential
GenevisibleiQ9CU62 MM

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR029683 SMC1A_metazoan
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf
PANTHERiPTHR18937:SF170 PTHR18937:SF170, 1 hit
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF75553 SSF75553, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSMC1A_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9CU62
Secondary accession number(s): A2AFQ5
, Q3V480, Q9CUX9, Q9D959, Q9WTU1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 164 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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