Skip Header

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

O95347

- SMC2_HUMAN

UniProt

O95347 - SMC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Structural maintenance of chromosomes protein 2

Gene

SMC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. kinetochore organization Source: Ensembl
  2. meiotic chromosome condensation Source: Ensembl
  3. meiotic chromosome segregation Source: Ensembl
  4. mitotic cell cycle Source: Reactome
  5. mitotic chromosome condensation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
REACT_172744. Condensation of Prophase Chromosomes.

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-associated protein E
Short name:
hCAP-E
XCAP-E homolog
Gene namesi
Name:SMC2
Synonyms:CAPE, SMC2L1
ORF Names:PRO0324
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:14011. SMC2.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication. Chromosome 1 Publication
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.

GO - Cellular componenti

  1. condensed chromosome Source: UniProtKB
  2. condensin complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. nuclear chromosome Source: UniProtKB
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37833.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11971197Structural maintenance of chromosomes protein 2PRO_0000118995Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-acetyllysine1 Publication
Modified residuei222 – 2221N6-acetyllysine1 Publication
Modified residuei677 – 6771N6-acetyllysine1 Publication
Modified residuei1158 – 11581N6-acetyllysine1 Publication
Modified residuei1160 – 11601N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO95347.
PaxDbiO95347.
PRIDEiO95347.

PTM databases

PhosphoSiteiO95347.

Expressioni

Gene expression databases

BgeeiO95347.
CleanExiHS_SMC2.
ExpressionAtlasiO95347. baseline and differential.
GenevestigatoriO95347.

Interactioni

Subunit structurei

Forms a heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG. Interacts with BRD4 (isoform B), leading to insulate chromatin from DNA damage response pathway.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPHQ150032EBI-355822,EBI-1046410
NCAPH2Q6IBW42EBI-355822,EBI-2548296
SMC4Q9NTJ33EBI-355822,EBI-356173

Protein-protein interaction databases

BioGridi115841. 42 interactions.
DIPiDIP-35422N.
IntActiO95347. 15 interactions.
MINTiMINT-1161754.
STRINGi9606.ENSP00000286398.

Structurei

3D structure databases

ProteinModelPortaliO95347.
SMRiO95347. Positions 506-660.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 671164Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili173 – 507335Sequence AnalysisAdd
BLAST
Coiled coili672 – 926255Sequence AnalysisAdd
BLAST
Coiled coili963 – 103169Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1085 – 112036Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074857.
HOGENOMiHOG000228249.
HOVERGENiHBG106605.
InParanoidiO95347.
KOiK06674.
OMAiCQNGKIP.
OrthoDBiEOG7SR4KV.
PhylomeDBiO95347.
TreeFamiTF101157.

Family and domain databases

Gene3Di3.40.50.300. 3 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. 2 hits.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95347-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG
60 70 80 90 100
ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE
110 120 130 140 150
ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI
160 170 180 190 200
TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA AQKTIEKKEA KLKEIKTILE
210 220 230 240 250
EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL LAEDTKVRSA
260 270 280 290 300
EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE
310 320 330 340 350
DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK
360 370 380 390 400
EVKKITDGLH ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG
410 420 430 440 450
QMMACKNDIS KAQTEAKQAQ MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA
460 470 480 490 500
LEAVKRLKEK LEAEMKKLNY EENKEESLLE KRRQLSRDIG RLKETYEALL
510 520 530 540 550
ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA LELVAGERLY
560 570 580 590 600
NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
610 620 630 640 650
DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV
660 670 680 690 700
TLGGDVFDPH GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE
710 720 730 740 750
ELAGLKNTAE KYRQLKQQWE MKTEEADLLQ TKLQQSSYHK QQEELDALKK
760 770 780 790 800
TIEESEETLK NTKEIQRKAE EKYEVLENKM KNAEAERERE LKDAQKKLDC
810 820 830 840 850
AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL EAVNEAIKSY
860 870 880 890 900
ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK
910 920 930 940 950
EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ
960 970 980 990 1000
PNSAYDFKTN NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND
1010 1020 1030 1040 1050
LMKKKRIVEN DKSKILTTIE DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP
1060 1070 1080 1090 1100
GANAMLAPPE GQTVLDGLEF KVALGNTWKE NLTELSGGQR SLVALSLILS
1110 1120 1130 1140 1150
MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF IVVSLKEGMF
1160 1170 1180 1190
NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
Length:1,197
Mass (Da):135,656
Last modified:November 25, 2008 - v2
Checksum:i15EBB56B31FC1364
GO
Isoform 2 (identifier: O95347-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1091-1099: SLVALSLIL → QKQQNHTTG
     1100-1197: Missing.

Note: No experimental confirmation available.

Show »
Length:1,099
Mass (Da):124,926
Checksum:i68BB895EA6EBA265
GO

Sequence cautioni

The sequence AAC72360.1 differs from that shown. Reason: Frameshift at positions 890 and 908. Curated
The sequence AAF29579.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941G → V in AAC72360. (PubMed:9789013)Curated
Sequence conflicti916 – 9161N → H in AAC72360. (PubMed:9789013)Curated
Sequence conflicti998 – 9981Y → C in AAC72360. (PubMed:9789013)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1009 – 10091E → K.
Corresponds to variant rs4562395 [ dbSNP | Ensembl ].
VAR_047489

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1091 – 10999SLVALSLIL → QKQQNHTTG in isoform 2. 1 PublicationVSP_007243
Alternative sequencei1100 – 119798Missing in isoform 2. 1 PublicationVSP_007244Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092563 mRNA. Translation: AAC72360.1. Frameshift.
AL833191 mRNA. Translation: CAI46187.1.
AL161791, AL354938 Genomic DNA. Translation: CAI16866.1.
AL354938, AL161791 Genomic DNA. Translation: CAI16923.1.
CH471105 Genomic DNA. Translation: EAW58973.1.
BC130385 mRNA. Translation: AAI30386.1.
AF113673 mRNA. Translation: AAF29579.1. Different initiation.
BN000163 mRNA. Translation: CAD89875.1.
CCDSiCCDS35086.1. [O95347-1]
RefSeqiNP_001036015.1. NM_001042550.1. [O95347-1]
NP_001036016.1. NM_001042551.1. [O95347-1]
NP_001252531.1. NM_001265602.1. [O95347-1]
NP_006435.2. NM_006444.2. [O95347-1]
XP_006716996.1. XM_006716933.1. [O95347-1]
UniGeneiHs.119023.

Genome annotation databases

EnsembliENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1]
ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1]
ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1]
ENST00000493955; ENSP00000431534; ENSG00000136824.
GeneIDi10592.
KEGGihsa:10592.
UCSCiuc004bbv.3. human. [O95347-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092563 mRNA. Translation: AAC72360.1 . Frameshift.
AL833191 mRNA. Translation: CAI46187.1 .
AL161791 , AL354938 Genomic DNA. Translation: CAI16866.1 .
AL354938 , AL161791 Genomic DNA. Translation: CAI16923.1 .
CH471105 Genomic DNA. Translation: EAW58973.1 .
BC130385 mRNA. Translation: AAI30386.1 .
AF113673 mRNA. Translation: AAF29579.1 . Different initiation.
BN000163 mRNA. Translation: CAD89875.1 .
CCDSi CCDS35086.1. [O95347-1 ]
RefSeqi NP_001036015.1. NM_001042550.1. [O95347-1 ]
NP_001036016.1. NM_001042551.1. [O95347-1 ]
NP_001252531.1. NM_001265602.1. [O95347-1 ]
NP_006435.2. NM_006444.2. [O95347-1 ]
XP_006716996.1. XM_006716933.1. [O95347-1 ]
UniGenei Hs.119023.

3D structure databases

ProteinModelPortali O95347.
SMRi O95347. Positions 506-660.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115841. 42 interactions.
DIPi DIP-35422N.
IntActi O95347. 15 interactions.
MINTi MINT-1161754.
STRINGi 9606.ENSP00000286398.

PTM databases

PhosphoSitei O95347.

Proteomic databases

MaxQBi O95347.
PaxDbi O95347.
PRIDEi O95347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286398 ; ENSP00000286398 ; ENSG00000136824 . [O95347-1 ]
ENST00000374787 ; ENSP00000363919 ; ENSG00000136824 . [O95347-1 ]
ENST00000374793 ; ENSP00000363925 ; ENSG00000136824 . [O95347-1 ]
ENST00000493955 ; ENSP00000431534 ; ENSG00000136824 .
GeneIDi 10592.
KEGGi hsa:10592.
UCSCi uc004bbv.3. human. [O95347-1 ]

Organism-specific databases

CTDi 10592.
GeneCardsi GC09P106856.
H-InvDB HIX0008250.
HGNCi HGNC:14011. SMC2.
MIMi 605576. gene.
neXtProti NX_O95347.
PharmGKBi PA37833.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1196.
GeneTreei ENSGT00550000074857.
HOGENOMi HOG000228249.
HOVERGENi HBG106605.
InParanoidi O95347.
KOi K06674.
OMAi CQNGKIP.
OrthoDBi EOG7SR4KV.
PhylomeDBi O95347.
TreeFami TF101157.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_172744. Condensation of Prophase Chromosomes.

Miscellaneous databases

ChiTaRSi SMC2. human.
GeneWikii SMC2.
GenomeRNAii 10592.
NextBioi 40225.
PROi O95347.
SOURCEi Search...

Gene expression databases

Bgeei O95347.
CleanExi HS_SMC2.
ExpressionAtlasi O95347. baseline and differential.
Genevestigatori O95347.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view ]
PANTHERi PTHR18937:SF9. PTHR18937:SF9. 1 hit.
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 2 hits.
[Graphical view ]
PIRSFi PIRSF005719. SMC. 1 hit.
SMARTi SM00968. SMC_hinge. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics."
    Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S., Yokomori K.
    Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SMC4.
    Tissue: Teratocarcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph node.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 1).
    Tissue: Brain.
  6. "Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2).
    Tissue: Fetal liver.
  7. "The evolution of SMC proteins: phylogenetic analysis and structural implications."
    Cobbe N., Heck M.M.S.
    Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation."
    Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.
    Mol. Cell. Biol. 20:6996-7006(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 AND CNAP1, SUBCELLULAR LOCATION.
  9. "Chromosome condensation by a human condensin complex in Xenopus egg extracts."
    Kimura K., Cuvier O., Hirano T.
    J. Biol. Chem. 276:5417-5420(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRRN1; CNAP1 AND CAPG, FUNCTION OF THE COMPLEX.
  10. "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-114; LYS-222; LYS-677; LYS-1158 AND LYS-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: INTERACTION WITH BRD4.

Entry informationi

Entry nameiSMC2_HUMAN
AccessioniPrimary (citable) accession number: O95347
Secondary accession number(s): Q6IEE0, Q9P1P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3