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Q9P2M7

- CING_HUMAN

UniProt

Q9P2M7 - CING_HUMAN

Protein

Cingulin

Gene

CGN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (27 Jan 2003)
      Previous versions | rss
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    Functioni

    Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier.

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. motor activity Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. transforming growth factor beta receptor signaling pathway Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cingulin
    Gene namesi
    Name:CGN
    Synonyms:KIAA1319
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17429. CGN.

    Subcellular locationi

    Cell junctiontight junction By similarity
    Note: Localizes to the apical junction complex composed of tight and adherens junctions.By similarity

    GO - Cellular componenti

    1. cell junction Source: Reactome
    2. myosin complex Source: InterPro
    3. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Tight junction

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134938123.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11971197CingulinPRO_0000089763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei134 – 1341Phosphoserine3 Publications
    Modified residuei149 – 1491Phosphoserine1 Publication
    Modified residuei159 – 1591Phosphoserine3 Publications
    Modified residuei208 – 2081Phosphoserine1 Publication
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei252 – 2521Phosphoserine2 Publications
    Modified residuei332 – 3321PhosphoserineBy similarity
    Modified residuei573 – 5731N6-acetyllysine1 Publication
    Modified residuei706 – 7061Phosphothreonine1 Publication
    Modified residuei1176 – 11761Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9P2M7.
    PaxDbiQ9P2M7.
    PRIDEiQ9P2M7.

    PTM databases

    PhosphoSiteiQ9P2M7.

    Expressioni

    Tissue specificityi

    Localized on the cytoplasmic face of tight junctions of polarized epithelia and some endothelia. Expressed in pancreas, kidney, liver and lung, but not in skeletal muscle, placenta, brain or heart.

    Gene expression databases

    ArrayExpressiQ9P2M7.
    BgeeiQ9P2M7.
    CleanExiHS_CGN.
    GenevestigatoriQ9P2M7.

    Organism-specific databases

    HPAiCAB017193.
    HPA027586.
    HPA027587.
    HPA027657.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with TJP1/ZO-1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi121589. 13 interactions.
    DIPiDIP-30947N.
    IntActiQ9P2M7. 9 interactions.
    MINTiMINT-1681123.
    STRINGi9606.ENSP00000271636.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2M7.
    SMRiQ9P2M7. Positions 1102-1152.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 351351HeadAdd
    BLAST
    Regioni106 – 400295Interacts with ZO-2Add
    BLAST
    Regioni1155 – 119743TailAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili352 – 1154803Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi42 – 5615ZIMAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi363 – 836474Glu-richAdd
    BLAST

    Domaini

    Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1.

    Sequence similaritiesi

    Belongs to the cingulin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG149500.
    HOVERGENiHBG031389.
    InParanoidiQ9P2M7.
    KOiK06102.
    OrthoDBiEOG7BKCSV.
    PhylomeDBiQ9P2M7.
    TreeFamiTF332247.

    Family and domain databases

    InterProiIPR002928. Myosin_tail.
    [Graphical view]
    PfamiPF01576. Myosin_tail_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P2M7-1) [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

    MAEPRGPVDH GVQIRFITEP VSGAEMGTLR RGGRRPAKDA RASTYGVAVR     50
    VQGIAGQPFV VLNSGEKGGD SFGVQIKGAN DQGASGALSS DLELPENPYS 100
    QVKGFPAPSQ SSTSDEEPGA YWNGKLLRSH SQASLAGPGP VDPSNRSNSM 150
    LELAPKVASP GSTIDTAPLS SVDSLINKFD SQLGGQARGR TGRRTRMLPP 200
    EQRKRSKSLD SRLPRDTFEE RERQSTNHWT SSTKYDNHVG TSKQPAQSQN 250
    LSPLSGFSRS RQTQDWVLQS FEEPRRSAQD PTMLQFKSTP DLLRDQQEAA 300
    PPGSVDHMKA TIYGILREGS SESETSVRRK VSLVLEKMQP LVMVSSGSTK 350
    AVAGQGELTR KVEELQRKLD EEVKKRQKLE PSQVGLERQL EEKTEECSRL 400
    QELLERRKGE AQQSNKELQN MKRLLDQGED LRHGLETQVM ELQNKLKHVQ 450
    GPEPAKEVLL KDLLETRELL EEVLEGKQRV EEQLRLRERE LTALKGALKE 500
    EVASRDQEVE HVRQQYQRDT EQLRRSMQDA TQDHAVLEAE RQKMSALVRG 550
    LQRELEETSE ETGHWQSMFQ KNKEDLRATK QELLQLRMEK EEMEEELGEK 600
    IEVLQRELEQ ARASAGDTRQ VEVLKKELLR TQEELKELQA ERQSQEVAGR 650
    HRDRELEKQL AVLRVEADRG RELEEQNLQL QKTLQQLRQD CEEASKAKMV 700
    AEAEATVLGQ RRAAVETTLR ETQEENDEFR RRILGLEQQL KETRGLVDGG 750
    EAVEARLRDK LQRLEAEKQQ LEEALNASQE EEGSLAAAKR ALEARLEEAQ 800
    RGLARLGQEQ QTLNRALEEE GKQREVLRRG KAELEEQKRL LDRTVDRLNK 850
    ELEKIGEDSK QALQQLQAQL EDYKEKARRE VADAQRQAKD WASEAEKTSG 900
    GLSRLQDEIQ RLRQALQASQ AERDTARLDK ELLAQRLQGL EQEAENKKRS 950
    QDDRARQLKG LEEKVSRLET ELDEEKNTVE LLTDRVNRGR DQVDQLRTEL 1000
    MQERSARQDL ECDKISLERQ NKDLKTRLAS SEGFQKPSAS LSQLESQNQL 1050
    LQERLQAEER EKTVLQSTNR KLERKVKELS IQIEDERQHV NDQKDQLSLR 1100
    VKALKRQVDE AEEEIERLDG LRKKAQREVE EQHEVNEQLQ ARIKSLEKDS 1150
    WRKASRSAAE SALKNEGLSS DEEFDSVYDP SSIASLLTES NLQTSSC 1197
    Length:1,197
    Mass (Da):136,386
    Last modified:January 27, 2003 - v2
    Checksum:i0C9375283ABAAF3D
    GO
    Isoform 2 (identifier: Q9P2M7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         698-771: KMVAEAEATV...QRLEAEKQQL → RGVGTGLRRW...KRLAGGSCSL
         772-1197: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:771
    Mass (Da):87,047
    Checksum:iF289EA3694E4CEC1
    GO

    Sequence cautioni

    The sequence AAF74498.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAI52446.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA92557.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAF82696.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI16590.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW53434.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti479 – 4791R → Q.
    Corresponds to variant rs12038198 [ dbSNP | Ensembl ].
    VAR_057809

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei698 – 77174KMVAE…EKQQL → RGVGTGLRRWRLRVSGGLRS QRVWKVTCHGYVLTSSWVLG MWFKEARIWQGEDTCICVGV GFSEKRLAGGSCSL in isoform 2. 1 PublicationVSP_037039Add
    BLAST
    Alternative sequencei772 – 1197426Missing in isoform 2. 1 PublicationVSP_037040Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263462 mRNA. Translation: AAF74498.1. Different initiation.
    AB037740 mRNA. Translation: BAA92557.1. Different initiation.
    AK290007 mRNA. Translation: BAF82696.1. Different initiation.
    AL365436 Genomic DNA. Translation: CAI16590.1. Different initiation.
    CH471121 Genomic DNA. Translation: EAW53434.1. Different initiation.
    BC146657 mRNA. Translation: AAI46658.1.
    BC152445 mRNA. Translation: AAI52446.1. Different initiation.
    RefSeqiNP_065821.1. NM_020770.2.
    XP_005245422.1. XM_005245365.2.
    UniGeneiHs.591464.

    Genome annotation databases

    EnsembliENST00000271636; ENSP00000271636; ENSG00000143375.
    GeneIDi57530.
    KEGGihsa:57530.
    UCSCiuc009wmw.3. human. [Q9P2M7-1]

    Polymorphism databases

    DMDMi27923755.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263462 mRNA. Translation: AAF74498.1 . Different initiation.
    AB037740 mRNA. Translation: BAA92557.1 . Different initiation.
    AK290007 mRNA. Translation: BAF82696.1 . Different initiation.
    AL365436 Genomic DNA. Translation: CAI16590.1 . Different initiation.
    CH471121 Genomic DNA. Translation: EAW53434.1 . Different initiation.
    BC146657 mRNA. Translation: AAI46658.1 .
    BC152445 mRNA. Translation: AAI52446.1 . Different initiation.
    RefSeqi NP_065821.1. NM_020770.2.
    XP_005245422.1. XM_005245365.2.
    UniGenei Hs.591464.

    3D structure databases

    ProteinModelPortali Q9P2M7.
    SMRi Q9P2M7. Positions 1102-1152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121589. 13 interactions.
    DIPi DIP-30947N.
    IntActi Q9P2M7. 9 interactions.
    MINTi MINT-1681123.
    STRINGi 9606.ENSP00000271636.

    PTM databases

    PhosphoSitei Q9P2M7.

    Polymorphism databases

    DMDMi 27923755.

    Proteomic databases

    MaxQBi Q9P2M7.
    PaxDbi Q9P2M7.
    PRIDEi Q9P2M7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271636 ; ENSP00000271636 ; ENSG00000143375 .
    GeneIDi 57530.
    KEGGi hsa:57530.
    UCSCi uc009wmw.3. human. [Q9P2M7-1 ]

    Organism-specific databases

    CTDi 57530.
    GeneCardsi GC01P151483.
    HGNCi HGNC:17429. CGN.
    HPAi CAB017193.
    HPA027586.
    HPA027587.
    HPA027657.
    MIMi 609473. gene.
    neXtProti NX_Q9P2M7.
    PharmGKBi PA134938123.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149500.
    HOVERGENi HBG031389.
    InParanoidi Q9P2M7.
    KOi K06102.
    OrthoDBi EOG7BKCSV.
    PhylomeDBi Q9P2M7.
    TreeFami TF332247.

    Enzyme and pathway databases

    Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).

    Miscellaneous databases

    GeneWikii Cingulin.
    GenomeRNAii 57530.
    NextBioi 63932.
    PROi Q9P2M7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2M7.
    Bgeei Q9P2M7.
    CleanExi HS_CGN.
    Genevestigatori Q9P2M7.

    Family and domain databases

    InterProi IPR002928. Myosin_tail.
    [Graphical view ]
    Pfami PF01576. Myosin_tail_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human and Xenopus cingulin share a modular organization of the coiled-coil rod domain: predictions for intra- and intermolecular assembly."
      Citi S., D'Atri F., Parry D.A.D.
      J. Struct. Biol. 131:135-145(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Neuroepithelium.
    2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hippocampus.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 368-376.
      Tissue: Platelet.
    8. "Evidence for a functional interaction between cingulin and ZO-1 in cultured cells."
      D'Atri F., Nadalutti F., Citi S.
      J. Biol. Chem. 277:27757-27764(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TJP1.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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-134 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-159 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-134; SER-149; SER-159; SER-208; SER-211; SER-252 AND THR-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCING_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2M7
    Secondary accession number(s): A6H8L3
    , A7MD22, Q5T386, Q9NR25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: January 27, 2003
    Last modified: October 1, 2014
    This is version 107 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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