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Protein

Structural maintenance of chromosomes protein 1B

Gene

Smc1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. 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 meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: MGI

GO - Biological processi

  • meiotic nuclear division Source: MGI
  • sister chromatid cohesion Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 1B
Short name:
SMC protein 1B
Short name:
SMC-1-beta
Short name:
SMC-1B
Gene namesi
Name:Smc1b
Synonyms:Smc1l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2154049. Smc1b.

Subcellular locationi

  • Nucleus
  • Chromosome
  • Chromosomecentromere

  • Note: Associates with chromatin. In prophase I stage of meiosis, localizes along the AE of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. Remains chromatin associated at the centromeres up to metaphase II. At anaphase II, dissociates from centromeres, allowing chromosomes segregation.

GO - Cellular componenti

  • chromosome, centromeric region Source: MGI
  • condensed nuclear chromosome Source: MGI
  • cytoplasm Source: MGI
  • lateral element Source: MGI
  • meiotic cohesin complex Source: UniProtKB
  • nuclear meiotic cohesin complex Source: MGI
  • nucleoplasm Source: MGI
  • synaptonemal complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12481248Structural maintenance of chromosomes protein 1BPRO_0000118994Add
BLAST

Proteomic databases

EPDiQ920F6.
MaxQBiQ920F6.
PaxDbiQ920F6.
PRIDEiQ920F6.

PTM databases

iPTMnetiQ920F6.
PhosphoSiteiQ920F6.

Expressioni

Tissue specificityi

Testis and ovary specific. Not expressed in somatic cells.

Gene expression databases

BgeeiQ920F6.
CleanExiMM_SMC1B.
ExpressionAtlasiQ920F6. baseline and differential.
GenevisibleiQ920F6. MM.

Interactioni

Subunit structurei

Forms a heterodimer with SMC3. Component of a meiosis-specific cohesin complex, probably composed of the SMC1B and SMC3 heterodimer attached via their hinge domain, RAD21 (or its meiosis-specific related protein REC8), which link them, and STAG3, which interacts with RAD21 or REC8.1 Publication

Protein-protein interaction databases

BioGridi228280. 2 interactions.
IntActiQ920F6. 9 interactions.
MINTiMINT-4134790.
STRINGi10090.ENSMUSP00000023068.

Structurei

3D structure databases

ProteinModelPortaliQ920F6.
SMRiQ920F6. Positions 499-675.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni503 – 665163Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili163 – 502340Sequence analysisAdd
BLAST
Coiled coili666 – 912247Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1123 – 115836Ala/Asp-rich (DA-box)Add
BLAST

Domaini

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 or REC8 protein, forming a ring structure (By similarity).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0018. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ920F6.
KOiK06636.
OMAiISMKKPK.
OrthoDBiEOG7K3TK5.
PhylomeDBiQ920F6.
TreeFamiTF101156.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Q920F6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGHLELLLVE NFKSWRGRQV IGPFKRFTCI IGPNGSGKSN VMDALSFVMG
60 70 80 90 100
EKTTNLRVKN IQELIHGAHT GKPVSSSASV TIIYIEDSGE EKTFTRIIRG
110 120 130 140 150
GCSEYHFGDK PVSRSVYVAQ LENIGIIVKA QNCLVFQGTV ESISMKKPKE
160 170 180 190 200
RTQFFEEIST SGEFIGEYEA KKKKLQKAEE DAQFHFNVKK NVAAERKHAK
210 220 230 240 250
IEKEEAEHYQ NLLEELKINK IQLMLFQLYY NEEKINVLNT ELEQMDGNLS
260 270 280 290 300
VVKDTLSHHE NIFKAKKKDY GMLTRQLQQT AKELKSVEAI LNQKRPQYIK
310 320 330 340 350
AKENTSHHLK KLDLSKKLIT DNEKQCSKQE DGIRALVAEL ADLDRAWKSF
360 370 380 390 400
EKQMEEKILQ KGRDIELENS QLDRYKLLKE QVRRKVGIMT QQLEKLQWEQ
410 420 430 440 450
KAEKERLAFE KRRHGDTQGN LKQIKEQIEE HKKRIEKLEE YTKTCMDCLE
460 470 480 490 500
DKKQQEEALK KEIENTKSRM SEVNEELSLI RNELQNAGID NHEGKRQQKR
510 520 530 540 550
AEVLEHLKRL YPDSVFGRLL DLCHPIHKKY QLAVTKLFGR YMVAIVVASE
560 570 580 590 600
KIAKDCIRFL KAERAEPETF LALDYLDIKP INERLREIKG CKMMIDVIKT
610 620 630 640 650
QFPQLKKVIQ FVCGNGLVCE TVEEARHIAF GGPERRKAVA LDGTLFLKSG
660 670 680 690 700
VISGGSSDLK HKALCWDEKE LHNLRDKRSQ LVQELKELMK TLRKETDLKQ
710 720 730 740 750
IQTLVQGTNT RLKYSQNELE MIKKKHLATF YREQSQLQSE LLNIDSQCTM
760 770 780 790 800
LSEGINKQQQ KIEEFQDKID EVEDDIFQDF CEEIGVENIR EFENKHVKQQ
810 820 830 840 850
QENDQKRLEF EKQKTRLNIQ LEYSRNQLKK KLNNIDTLKT TIQKGKEDID
860 870 880 890 900
NLKKTEEECL KIVEELMVKQ EQIKEVLATQ SSNIEKIHIQ IEEERKKVLA
910 920 930 940 950
VDREVGKLQK EVVIIQGSLE QKLLEKHNLL LDCKVQDIDI SLVLGSLEDI
960 970 980 990 1000
IEMELTETES TQATADIYEK EASIQIDYSP LREDLKALQS DKEVEAHLTL
1010 1020 1030 1040 1050
LLQQVASQEN TLLKTTAPNL RAQENLKTVR DKFQESADVF EASRKEARIC
1060 1070 1080 1090 1100
RQEFEQVKRR RYDAFSQCFE HISVSIDQIY KKLCRNNSAQ AFLSPENPEE
1110 1120 1130 1140 1150
PYLDGISYNC VAPGKRFMPM DNLSGGEKCV AALALLFAVH SFRPAPFFVL
1160 1170 1180 1190 1200
DEVDAALDNT NIGKVSSYIK EQSQEQFQMI IISLKEEFYS KADALIGVYP
1210 1220 1230 1240
EHNECMFSHV LTLDLSKYPD TEDQEGSRSH RKPRVPRVSM SPKSPQSR
Length:1,248
Mass (Da):144,513
Last modified:December 1, 2001 - v1
Checksum:i6C31DB46217BC94D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303827 mRNA. Translation: AAL09333.1.
CCDSiCCDS27718.1.
RefSeqiNP_536718.1. NM_080470.1.
UniGeneiMm.182737.

Genome annotation databases

EnsembliENSMUST00000023068; ENSMUSP00000023068; ENSMUSG00000022432.
GeneIDi140557.
KEGGimmu:140557.
UCSCiuc007xcx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303827 mRNA. Translation: AAL09333.1.
CCDSiCCDS27718.1.
RefSeqiNP_536718.1. NM_080470.1.
UniGeneiMm.182737.

3D structure databases

ProteinModelPortaliQ920F6.
SMRiQ920F6. Positions 499-675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228280. 2 interactions.
IntActiQ920F6. 9 interactions.
MINTiMINT-4134790.
STRINGi10090.ENSMUSP00000023068.

PTM databases

iPTMnetiQ920F6.
PhosphoSiteiQ920F6.

Proteomic databases

EPDiQ920F6.
MaxQBiQ920F6.
PaxDbiQ920F6.
PRIDEiQ920F6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023068; ENSMUSP00000023068; ENSMUSG00000022432.
GeneIDi140557.
KEGGimmu:140557.
UCSCiuc007xcx.1. mouse.

Organism-specific databases

CTDi27127.
MGIiMGI:2154049. Smc1b.

Phylogenomic databases

eggNOGiKOG0018. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ920F6.
KOiK06636.
OMAiISMKKPK.
OrthoDBiEOG7K3TK5.
PhylomeDBiQ920F6.
TreeFamiTF101156.

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.

Miscellaneous databases

NextBioi369861.
PROiQ920F6.
SOURCEiSearch...

Gene expression databases

BgeeiQ920F6.
CleanExiMM_SMC1B.
ExpressionAtlasiQ920F6. baseline and differential.
GenevisibleiQ920F6. MM.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CHARACTERIZATION, INTERACTION WITH SMC3.
    Tissue: Testis.
  2. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 847-854, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Cohesin SMC1 beta is required for meiotic chromosome dynamics, sister chromatid cohesion and DNA recombination."
    Revenkova E., Eijpe M., Heyting C., Hodges C.A., Hunt P.A., Liebe B., Scherthan H., Jessberger R.
    Nat. Cell Biol. 6:555-562(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiSMC1B_MOUSE
AccessioniPrimary (citable) accession number: Q920F6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: March 16, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.