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Q9NTJ3

- SMC4_HUMAN

UniProt

Q9NTJ3 - SMC4_HUMAN

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Protein

Structural maintenance of chromosomes protein 4

Gene
SMC4, CAPC, SMC4L1
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 bindingi113 – 1208ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. 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
  6. mitotic sister chromatid segregation 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 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 namesi
Name:SMC4
Synonyms:CAPC, SMC4L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:14013. SMC4.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. condensin complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12881288Structural maintenance of chromosomes protein 4PRO_0000119006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine3 Publications
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei39 – 391Phosphothreonine1 Publication
Modified residuei41 – 411Phosphoserine2 Publications
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei381 – 3811N6-acetyllysine By similarity
Modified residuei679 – 6791N6-acetyllysine1 Publication
Modified residuei1056 – 10561Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NTJ3.
PaxDbiQ9NTJ3.
PeptideAtlasiQ9NTJ3.
PRIDEiQ9NTJ3.

PTM databases

PhosphoSiteiQ9NTJ3.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9NTJ3.
BgeeiQ9NTJ3.
CleanExiHS_SMC4.
GenevestigatoriQ9NTJ3.

Organism-specific databases

HPAiCAB055509.
HPA029449.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMC2O953473EBI-356173,EBI-355822

Protein-protein interaction databases

BioGridi115362. 36 interactions.
DIPiDIP-32946N.
IntActiQ9NTJ3. 18 interactions.
MINTiMINT-5005675.
STRINGi9606.ENSP00000341382.

Structurei

3D structure databases

ProteinModelPortaliQ9NTJ3.
SMRiQ9NTJ3. Positions 91-338, 597-754, 1096-1267.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni589 – 766178Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili272 – 588317 Reviewed predictionAdd
BLAST
Coiled coili767 – 1020254 Reviewed predictionAdd
BLAST
Coiled coili1109 – 112921 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 236Poly-Pro
Compositional biasi66 – 716Poly-Pro
Compositional biasi1191 – 122636Ala/Asp-rich (DA-box)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the SMC family. SMC4 subfamily.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
HOGENOMiHOG000184777.
HOVERGENiHBG106696.
InParanoidiQ9NTJ3.
KOiK06675.
OMAiPSEEIDN.
OrthoDBiEOG7RJPQJ.
PhylomeDBiQ9NTJ3.
TreeFamiTF101158.

Family and domain databases

Gene3Di3.40.50.300. 4 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. 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: Q9NTJ3-1) [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

MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAETAS     50
EELDNRSLEE ILNSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI 100
LGPFHKRFSC IIGPNGSGKS NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD 150
EHKDIQSCTV EVHFQKIIDK EGDDYEVIPN SNFYVSRTAC RDNTSVYHIS 200
GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP KGQTEHDEGM 250
LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG 300
EKNIAIEFLT LENEIFRKKN HVCQYYIYEL QKRIAEMETQ KEKIHEDTKE 350
INEKSNILSN EMKAKNKDVK DTEKKLNKIT KFIEENKEKF TQLDLEDVQV 400
REKLKHATSK AKKLEKQLQK DKEKVEEFKS IPAKSNNIIN ETTTRNNALE 450
KEKEKEEKKL KEVMDSLKQE TQGLQKEKES REKELMGFSK SVNEARSKMD 500
VAQSELDIYL SRHNTAVSQL TKAKEALIAA SETLKERKAA IRDIEGKLPQ 550
TEQELKEKEK ELQKLTQEET NFKSLVHDLF QKVEEAKSSL AMNRSRGKVL 600
DAIIQEKKSG RIPGIYGRLG DLGAIDEKYD VAISSCCHAL DYIVVDSIDI 650
AQECVNFLKR QNIGVATFIG LDKMAVWAKK MTEIQTPENT PRLFDLVKVK 700
DEKIRQAFYF ALRDTLVADN LDQATRVAYQ KDRRWRVVTL QGQIIEQSGT 750
MTGGGSKVMK GRMGSSLVIE ISEEEVNKME SQLQNDSKKA MQIQEQKVQL 800
EERVVKLRHS EREMRNTLEK FTASIQRLIE QEEYLNVQVK ELEANVLATA 850
PDKKKQKLLE ENVSAFKTEY DAVAEKAGKV EAEVKRLHNT IVEINNHKLK 900
AQQDKLDKIN KQLDECASAI TKAQVAIKTA DRNLQKAQDS VLRTEKEIKD 950
TEKEVDDLTA ELKSLEDKAA EVVKNTNAAE ESLPEIQKEH RNLLQELKVI 1000
QENEHALQKD ALSIKLKLEQ IDGHIAEHNS KIKYWHKEIS KISLHPIEDN 1050
PIEEISVLSP EDLEAIKNPD SITNQIALLE ARCHEMKPNL GAIAEYKKKE 1100
ELYLQRVAEL DKITYERDSF RQAYEDLRKQ RLNEFMAGFY IITNKLKENY 1150
QMLTLGGDAE LELVDSLDPF SEGIMFSVRP PKKSWKKIFN LSGGEKTLSS 1200
LALVFALHHY KPTPLYFMDE IDAALDFKNV SIVAFYIYEQ TKNAQFIIIS 1250
LRNNMFEISD RLIGIYKTYN ITKSVAVNPK EIASKGLC 1288
Length:1,288
Mass (Da):147,182
Last modified:April 23, 2003 - v2
Checksum:i9D164D6EB0602464
GO
Isoform 2 (identifier: Q9NTJ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     980-1037: Missing.

Note: No experimental confirmation available.

Show »
Length:1,230
Mass (Da):140,278
Checksum:iDBFFD68DB1C10454
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811S → R.
Corresponds to variant rs35214835 [ dbSNP | Ensembl ].
VAR_052439
Natural varianti356 – 3561N → S.
Corresponds to variant rs33999879 [ dbSNP | Ensembl ].
VAR_052440
Natural varianti415 – 4151E → D.
Corresponds to variant rs2164675 [ dbSNP | Ensembl ].
VAR_059843

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei980 – 103758Missing in isoform 2. VSP_007245Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2721R → Q in AAC72361. 1 Publication
Sequence conflicti283 – 2831E → D in CAB66811. 1 Publication
Sequence conflicti392 – 3932QL → HV in AAC72361. 1 Publication
Sequence conflicti594 – 5941R → S in AAC72361. 1 Publication
Sequence conflicti645 – 6451V → G in CAD38803. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3189.1. [Q9NTJ3-1]
PIRiT46486.
RefSeqiNP_001002800.1. NM_001002800.2. [Q9NTJ3-1]
NP_001275682.1. NM_001288753.1.
NP_005487.3. NM_005496.3. [Q9NTJ3-1]
UniGeneiHs.58992.

Genome annotation databases

EnsembliENST00000344722; ENSP00000341382; ENSG00000113810. [Q9NTJ3-1]
ENST00000357388; ENSP00000349961; ENSG00000113810. [Q9NTJ3-1]
ENST00000360111; ENSP00000353225; ENSG00000113810. [Q9NTJ3-2]
ENST00000462787; ENSP00000420734; ENSG00000113810. [Q9NTJ3-2]
GeneIDi10051.
KEGGihsa:10051.
UCSCiuc003fdh.3. human. [Q9NTJ3-1]
uc010hwd.3. human. [Q9NTJ3-2]

Polymorphism databases

DMDMi30173386.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3189.1. [Q9NTJ3-1 ]
PIRi T46486.
RefSeqi NP_001002800.1. NM_001002800.2. [Q9NTJ3-1 ]
NP_001275682.1. NM_001288753.1.
NP_005487.3. NM_005496.3. [Q9NTJ3-1 ]
UniGenei Hs.58992.

3D structure databases

ProteinModelPortali Q9NTJ3.
SMRi Q9NTJ3. Positions 91-338, 597-754, 1096-1267.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115362. 36 interactions.
DIPi DIP-32946N.
IntActi Q9NTJ3. 18 interactions.
MINTi MINT-5005675.
STRINGi 9606.ENSP00000341382.

PTM databases

PhosphoSitei Q9NTJ3.

Polymorphism databases

DMDMi 30173386.

Proteomic databases

MaxQBi Q9NTJ3.
PaxDbi Q9NTJ3.
PeptideAtlasi Q9NTJ3.
PRIDEi Q9NTJ3.

Protocols and materials databases

DNASUi 10051.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344722 ; ENSP00000341382 ; ENSG00000113810 . [Q9NTJ3-1 ]
ENST00000357388 ; ENSP00000349961 ; ENSG00000113810 . [Q9NTJ3-1 ]
ENST00000360111 ; ENSP00000353225 ; ENSG00000113810 . [Q9NTJ3-2 ]
ENST00000462787 ; ENSP00000420734 ; ENSG00000113810 . [Q9NTJ3-2 ]
GeneIDi 10051.
KEGGi hsa:10051.
UCSCi uc003fdh.3. human. [Q9NTJ3-1 ]
uc010hwd.3. human. [Q9NTJ3-2 ]

Organism-specific databases

CTDi 10051.
GeneCardsi GC03P160117.
HGNCi HGNC:14013. SMC4.
HPAi CAB055509.
HPA029449.
MIMi 605575. gene.
neXtProti NX_Q9NTJ3.
PharmGKBi PA37834.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1196.
HOGENOMi HOG000184777.
HOVERGENi HBG106696.
InParanoidi Q9NTJ3.
KOi K06675.
OMAi PSEEIDN.
OrthoDBi EOG7RJPQJ.
PhylomeDBi Q9NTJ3.
TreeFami TF101158.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii SMC4.
GenomeRNAii 10051.
NextBioi 37969.
PROi Q9NTJ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NTJ3.
Bgeei Q9NTJ3.
CleanExi HS_SMC4.
Genevestigatori Q9NTJ3.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view ]
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. 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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiSMC4_HUMAN
AccessioniPrimary (citable) accession number: Q9NTJ3
Secondary accession number(s): A6NLT9
, D3DNL8, O95752, Q8NDL4, Q9UNT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: September 3, 2014
This is version 132 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 3
    Human chromosome 3: 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

Similar proteinsi