Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural maintenance of chromosomes protein 2

Gene

smc2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 2
Short name:
SMC protein 2
Short name:
SMC-2
Alternative name(s):
Chromosome assembly protein XCAP-E
Chromosome-associated protein E
Gene namesi
Name:smc2
Synonyms:cape, smc2l1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5826203. smc2.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity

  • Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001189981 – 1203Structural maintenance of chromosomes protein 2Add BLAST1203

Proteomic databases

PRIDEiP50533.

Interactioni

Subunit structurei

Forms a heterodimer with XCAP-C/SMC4. Component of the condensin complex, which contains the XCAP-E/SMC2 and XCAP-C/SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: XCAP-H/BRRN1, XCAP-D2/CNAP1 and XCAP-G/CAPG.1 Publication

Protein-protein interaction databases

BioGridi99139. 4 interactors.
DIPiDIP-48586N.
IntActiP50533. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliP50533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni514 – 669Flexible hingeAdd BLAST156

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili172 – 513Sequence analysisAdd BLAST342
Coiled coili670 – 1032Sequence analysisAdd BLAST363

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1095 – 1121Ala/Asp-rich (DA-box)Add BLAST27

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with XCAP-C, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG106605.
KOiK06674.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
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. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

P50533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHVKSIIIDG FKSYAQRTEI NGFDPLFNAI TGLNGSGKSN ILDSICFLLG
60 70 80 90 100
ISNLTQVRAS NLQDLVYKNG QAGITKATVS ITFDNYDKKQ SPLGFEAHDE
110 120 130 140 150
ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI
160 170 180 190 200
TKVLNMKPPE ILAMIEEAAG TRMYECKKIA AQKTIEKKEA KLKEIQTILE
210 220 230 240 250
EEITPTIHKL KEERSSYLEY QKIMREIEHL SRLYVAYQFV CAEETKVRSA
260 270 280 290 300
EELKEMQDSI LKLQDTMAEN ERKVKELGKE IAELEKMRDQ EVGGALRSLE
310 320 330 340 350
EALSEAQRAD TKVQSALDLK KQNMKAEREK KRKELVKSME EDAKVLTAKE
360 370 380 390 400
KEVKKITDGL SSLQEASQKD VEAFTSAQQH FNAVSAGLSS NEDGEEATLA
410 420 430 440 450
GQMMACKNET SKAETEAKQA QMKLKHAQQE LKTKQAEVKK MDGGYKKDNE
460 470 480 490 500
AFEAVKKSKE KLEVEMKKLN YEDGREEQLL EKRRGLSRDV NRLREAYESL
510 520 530 540 550
MARFPNLQFE YKDPEKNWDS DRVKGLVASL ISIKDVSTAT ALEVVAGGRL
560 570 580 590 600
YNVVVDTEVT GKKLLEKGEL KRRFTIIPLN KISARCLGKD TVNVAKNLVG
610 620 630 640 650
ADNVNLALSL VGYESELQKA MEYVFGTTLV CDTMDNAKKV TFDKRIMTKT
660 670 680 690 700
VTLGGDTFDP QGTLSGGARS QNASVLVRLQ ELKDVQDELK AKETELQEVE
710 720 730 740 750
KELMTLKNTV ERYRQLKQQW EMKSEEAELL QTKLQQSSYH KQQEELDSLK
760 770 780 790 800
QTIEESEETL KNTKEVQKKA EEKFKVLEHK MKNAEAERER ELKEAQQKLD
810 820 830 840 850
TAKKKADASN KKMKEKQQEV DALVLELEEL KREQTTYKQQ IETVDEAMKA
860 870 880 890 900
YQEQADSMAS EVSKNKEAVK KAQDELAKQK EIIMGHDKEI KTKSSEAGKL
910 920 930 940 950
RENNNDLQLK IKELEHNISK HKKDSADAAA KVAKMLNDYE WIASEKHLFG
960 970 980 990 1000
QANTAYDFKT NNPKEAGQRL HKLQEKKEKL GRNVNMRAMN MLTQAEERYN
1010 1020 1030 1040 1050
DLMKRKRIVE NDKSKILTTI EELDQKKNEA LNIAWQKVNK DFGSIFSTLL
1060 1070 1080 1090 1100
PGANAMLAPP EGQSVLDGLE FKVALGNTWK ENLTELSGGQ RSLVALSLIL
1110 1120 1130 1140 1150
AMLLFKPAPI YILDEVDAAL DLSHTQNIGQ MLRTHFRHSQ FIVVSLKDGM
1160 1170 1180 1190 1200
FNNANVLFKT KFVDGVSTVA RFAQNQNGGS SAGQQRSDKS KTKERRNRME

VDK
Length:1,203
Mass (Da):136,342
Last modified:October 1, 1996 - v1
Checksum:i04323DD0027DF309
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13674 mRNA. Translation: AAA64680.1.
PIRiB55094.
RefSeqiNP_001081372.1. NM_001087903.1.
UniGeneiXl.928.

Genome annotation databases

GeneIDi397800.
KEGGixla:397800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13674 mRNA. Translation: AAA64680.1.
PIRiB55094.
RefSeqiNP_001081372.1. NM_001087903.1.
UniGeneiXl.928.

3D structure databases

ProteinModelPortaliP50533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi99139. 4 interactors.
DIPiDIP-48586N.
IntActiP50533. 1 interactor.

Proteomic databases

PRIDEiP50533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397800.
KEGGixla:397800.

Organism-specific databases

CTDi10592.
XenbaseiXB-GENE-5826203. smc2.

Phylogenomic databases

HOVERGENiHBG106605.
KOiK06674.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
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. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC2_XENLA
AccessioniPrimary (citable) accession number: P50533
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.