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Q9NTJ3

- SMC4_HUMAN

UniProt

Q9NTJ3 - SMC4_HUMAN

Protein

Structural maintenance of chromosomes protein 4

Gene

SMC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
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    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 – 1208ATPSequence Analysis

    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

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

    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-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili272 – 588317Sequence AnalysisAdd
    BLAST
    Coiled coili767 – 1020254Sequence AnalysisAdd
    BLAST
    Coiled coili1109 – 112921Sequence AnalysisAdd
    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.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti272 – 2721R → Q in AAC72361. (PubMed:9789013)Curated
    Sequence conflicti283 – 2831E → D in CAB66811. (PubMed:11230166)Curated
    Sequence conflicti392 – 3932QL → HV in AAC72361. (PubMed:9789013)Curated
    Sequence conflicti594 – 5941R → S in AAC72361. (PubMed:9789013)Curated
    Sequence conflicti645 – 6451V → G in CAD38803. (PubMed:17974005)Curated

    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. 1 PublicationVSP_007245Add
    BLAST

    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]
    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 ]
    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

    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: October 1, 2014
    This is version 133 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