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Q9NTJ3 (SMC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 4

Short name=SMC protein 4
Short name=SMC-4
Alternative name(s):
Chromosome-associated polypeptide C
Short name=hCAP-C
XCAP-C homolog
Gene names
Name:SMC4
Synonyms:CAPC, SMC4L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

Forms a heterodimer with SMC2. 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. Ref.7 Ref.8

Subcellular location

Nucleus. Cytoplasm. Chromosome. 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. Ref.7

Tissue specificity

Widely expressed. Higher expression in testis, colon, thymus. Ref.1

Domain

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer By similarity.

Sequence similarities

Belongs to the SMC family. SMC4 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA condensation
Mitosis
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: InterPro

DNA repair

Inferred from electronic annotation. Source: InterPro

kinetochore organization

Inferred from electronic annotation. Source: Ensembl

meiotic chromosome condensation

Inferred from electronic annotation. Source: Ensembl

meiotic chromosome segregation

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic chromosome condensation

Inferred from direct assay Ref.8. Source: UniProtKB

mitotic sister chromatid segregation

Traceable author statement PubMed 11321372. Source: UniProtKB

   Cellular_componentcondensin complex

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 11850403. Source: UniProtKB

   Molecular_functionATP binding

Traceable author statement Ref.8. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMC2O953473EBI-356173,EBI-355822

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NTJ3-1)

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.
Isoform 2 (identifier: Q9NTJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     980-1037: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12881288Structural maintenance of chromosomes protein 4
PRO_0000119006

Regions

Nucleotide binding113 – 1208ATP Potential
Region589 – 766178Flexible hinge
Coiled coil272 – 588317 Potential
Coiled coil767 – 1020254 Potential
Coiled coil1109 – 112921 Potential
Compositional bias18 – 236Poly-Pro
Compositional bias66 – 716Poly-Pro
Compositional bias1191 – 122636Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue221Phosphoserine Ref.12 Ref.15 Ref.17
Modified residue281Phosphoserine Ref.15
Modified residue391Phosphothreonine Ref.15
Modified residue411Phosphoserine Ref.15 Ref.17
Modified residue501Phosphoserine Ref.15
Modified residue1431Phosphoserine Ref.17
Modified residue3811N6-acetyllysine By similarity
Modified residue6791N6-acetyllysine Ref.16
Modified residue10561Phosphoserine Ref.17

Natural variations

Alternative sequence980 – 103758Missing in isoform 2.
VSP_007245
Natural variant1811S → R.
Corresponds to variant rs35214835 [ dbSNP | Ensembl ].
VAR_052439
Natural variant3561N → S.
Corresponds to variant rs33999879 [ dbSNP | Ensembl ].
VAR_052440
Natural variant4151E → D.
Corresponds to variant rs2164675 [ dbSNP | Ensembl ].
VAR_059843

Experimental info

Sequence conflict2721R → Q in AAC72361. Ref.6
Sequence conflict2831E → D in CAB66811. Ref.2
Sequence conflict392 – 3932QL → HV in AAC72361. Ref.6
Sequence conflict5941R → S in AAC72361. Ref.6
Sequence conflict6451V → G in CAD38803. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 23, 2003. Version 2.
Checksum: 9D164D6EB0602464

FASTA1,288147,182
        10         20         30         40         50         60 
MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAETAS EELDNRSLEE 

        70         80         90        100        110        120 
ILNSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI LGPFHKRFSC IIGPNGSGKS 

       130        140        150        160        170        180 
NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD EHKDIQSCTV EVHFQKIIDK EGDDYEVIPN 

       190        200        210        220        230        240 
SNFYVSRTAC RDNTSVYHIS GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP 

       250        260        270        280        290        300 
KGQTEHDEGM LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG 

       310        320        330        340        350        360 
EKNIAIEFLT LENEIFRKKN HVCQYYIYEL QKRIAEMETQ KEKIHEDTKE INEKSNILSN 

       370        380        390        400        410        420 
EMKAKNKDVK DTEKKLNKIT KFIEENKEKF TQLDLEDVQV REKLKHATSK AKKLEKQLQK 

       430        440        450        460        470        480 
DKEKVEEFKS IPAKSNNIIN ETTTRNNALE KEKEKEEKKL KEVMDSLKQE TQGLQKEKES 

       490        500        510        520        530        540 
REKELMGFSK SVNEARSKMD VAQSELDIYL SRHNTAVSQL TKAKEALIAA SETLKERKAA 

       550        560        570        580        590        600 
IRDIEGKLPQ TEQELKEKEK ELQKLTQEET NFKSLVHDLF QKVEEAKSSL AMNRSRGKVL 

       610        620        630        640        650        660 
DAIIQEKKSG RIPGIYGRLG DLGAIDEKYD VAISSCCHAL DYIVVDSIDI AQECVNFLKR 

       670        680        690        700        710        720 
QNIGVATFIG LDKMAVWAKK MTEIQTPENT PRLFDLVKVK DEKIRQAFYF ALRDTLVADN 

       730        740        750        760        770        780 
LDQATRVAYQ KDRRWRVVTL QGQIIEQSGT MTGGGSKVMK GRMGSSLVIE ISEEEVNKME 

       790        800        810        820        830        840 
SQLQNDSKKA MQIQEQKVQL EERVVKLRHS EREMRNTLEK FTASIQRLIE QEEYLNVQVK 

       850        860        870        880        890        900 
ELEANVLATA PDKKKQKLLE ENVSAFKTEY DAVAEKAGKV EAEVKRLHNT IVEINNHKLK 

       910        920        930        940        950        960 
AQQDKLDKIN KQLDECASAI TKAQVAIKTA DRNLQKAQDS VLRTEKEIKD TEKEVDDLTA 

       970        980        990       1000       1010       1020 
ELKSLEDKAA EVVKNTNAAE ESLPEIQKEH RNLLQELKVI QENEHALQKD ALSIKLKLEQ 

      1030       1040       1050       1060       1070       1080 
IDGHIAEHNS KIKYWHKEIS KISLHPIEDN PIEEISVLSP EDLEAIKNPD SITNQIALLE 

      1090       1100       1110       1120       1130       1140 
ARCHEMKPNL GAIAEYKKKE ELYLQRVAEL DKITYERDSF RQAYEDLRKQ RLNEFMAGFY 

      1150       1160       1170       1180       1190       1200 
IITNKLKENY QMLTLGGDAE LELVDSLDPF SEGIMFSVRP PKKSWKKIFN LSGGEKTLSS 

      1210       1220       1230       1240       1250       1260 
LALVFALHHY KPTPLYFMDE IDAALDFKNV SIVAFYIYEQ TKNAQFIIIS LRNNMFEISD 

      1270       1280 
RLIGIYKTYN ITKSVAVNPK EIASKGLC 

« Hide

Isoform 2 [UniParc].

Checksum: DBFFD68DB1C10454
Show »

FASTA1,230140,278

References

« Hide 'large scale' references
[1]"Isolation and characterization of a human cDNA homologous to the Xenopus laevis XCAP-C gene belonging to the structural maintenance of chromosomes (SMC) family."
Nishiwaki T., Daigo Y., Kawasoe T., Nagasawa Y., Ishiguro H., Fujita M., Furukawa Y., Nakamura Y.
J. Hum. Genet. 44:197-202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] OF 87-1288 (ISOFORM 1), INTERACTION WITH SMC2.
Tissue: Teratocarcinoma.
[7]"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 SMC2 AND CNAP1, SUBCELLULAR LOCATION.
[8]"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 SMC2; BRRN1; CNAP1 AND CAPG, FUNCTION OF THE COMPLEX.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-22; SER-28; THR-39; SER-41 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-22; SER-41; SER-143 AND SER-1056, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB019987 mRNA. Translation: BAA73535.1.
AL136877 mRNA. Translation: CAB66811.1.
AL833949 mRNA. Translation: CAD38803.1.
AC024221 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78639.1.
CH471052 Genomic DNA. Translation: EAW78640.1.
AF092564 mRNA. Translation: AAC72361.1.
PIRT46486.
RefSeqNP_001002800.1. NM_001002800.2.
NP_001275682.1. NM_001288753.1.
NP_005487.3. NM_005496.3.
UniGeneHs.58992.

3D structure databases

ProteinModelPortalQ9NTJ3.
SMRQ9NTJ3. Positions 91-338, 597-754, 1096-1267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115362. 31 interactions.
DIPDIP-32946N.
IntActQ9NTJ3. 18 interactions.
MINTMINT-5005675.
STRING9606.ENSP00000341382.

PTM databases

PhosphoSiteQ9NTJ3.

Polymorphism databases

DMDM30173386.

Proteomic databases

PaxDbQ9NTJ3.
PeptideAtlasQ9NTJ3.
PRIDEQ9NTJ3.

Protocols and materials databases

DNASU10051.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344722; ENSP00000341382; ENSG00000113810. [Q9NTJ3-1]
ENST00000357388; ENSP00000349961; ENSG00000113810. [Q9NTJ3-1]
ENST00000360111; ENSP00000353225; ENSG00000113810. [Q9NTJ3-2]
ENST00000462787; ENSP00000420734; ENSG00000113810. [Q9NTJ3-2]
GeneID10051.
KEGGhsa:10051.
UCSCuc003fdh.3. human. [Q9NTJ3-1]
uc010hwd.3. human. [Q9NTJ3-2]

Organism-specific databases

CTD10051.
GeneCardsGC03P160117.
HGNCHGNC:14013. SMC4.
HPACAB055509.
HPA029449.
MIM605575. gene.
neXtProtNX_Q9NTJ3.
PharmGKBPA37834.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000184777.
HOVERGENHBG106696.
InParanoidQ9NTJ3.
KOK06675.
OMAIAIEFLT.
OrthoDBEOG7RJPQJ.
PhylomeDBQ9NTJ3.
TreeFamTF101158.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9NTJ3.
BgeeQ9NTJ3.
CleanExHS_SMC4.
GenevestigatorQ9NTJ3.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

GeneWikiSMC4.
GenomeRNAi10051.
NextBio37969.
PROQ9NTJ3.
SOURCESearch...

Entry information

Entry nameSMC4_HUMAN
AccessionPrimary (citable) accession number: Q9NTJ3
Secondary accession number(s): A6NLT9 expand/collapse secondary AC list , D3DNL8, O95752, Q8NDL4, Q9UNT9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM