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Q9P2M7

- CING_HUMAN

UniProt

Q9P2M7 - CING_HUMAN

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Protein

Cingulin

Gene

CGN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

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

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
Complete GO annotation...

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

BgeeiQ9P2M7.
CleanExiHS_CGN.
ExpressionAtlasiQ9P2M7. baseline and differential.
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.
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.
GeneTreeiENSGT00730000110843.
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

        10         20         30         40         50
MAEPRGPVDH GVQIRFITEP VSGAEMGTLR RGGRRPAKDA RASTYGVAVR
60 70 80 90 100
VQGIAGQPFV VLNSGEKGGD SFGVQIKGAN DQGASGALSS DLELPENPYS
110 120 130 140 150
QVKGFPAPSQ SSTSDEEPGA YWNGKLLRSH SQASLAGPGP VDPSNRSNSM
160 170 180 190 200
LELAPKVASP GSTIDTAPLS SVDSLINKFD SQLGGQARGR TGRRTRMLPP
210 220 230 240 250
EQRKRSKSLD SRLPRDTFEE RERQSTNHWT SSTKYDNHVG TSKQPAQSQN
260 270 280 290 300
LSPLSGFSRS RQTQDWVLQS FEEPRRSAQD PTMLQFKSTP DLLRDQQEAA
310 320 330 340 350
PPGSVDHMKA TIYGILREGS SESETSVRRK VSLVLEKMQP LVMVSSGSTK
360 370 380 390 400
AVAGQGELTR KVEELQRKLD EEVKKRQKLE PSQVGLERQL EEKTEECSRL
410 420 430 440 450
QELLERRKGE AQQSNKELQN MKRLLDQGED LRHGLETQVM ELQNKLKHVQ
460 470 480 490 500
GPEPAKEVLL KDLLETRELL EEVLEGKQRV EEQLRLRERE LTALKGALKE
510 520 530 540 550
EVASRDQEVE HVRQQYQRDT EQLRRSMQDA TQDHAVLEAE RQKMSALVRG
560 570 580 590 600
LQRELEETSE ETGHWQSMFQ KNKEDLRATK QELLQLRMEK EEMEEELGEK
610 620 630 640 650
IEVLQRELEQ ARASAGDTRQ VEVLKKELLR TQEELKELQA ERQSQEVAGR
660 670 680 690 700
HRDRELEKQL AVLRVEADRG RELEEQNLQL QKTLQQLRQD CEEASKAKMV
710 720 730 740 750
AEAEATVLGQ RRAAVETTLR ETQEENDEFR RRILGLEQQL KETRGLVDGG
760 770 780 790 800
EAVEARLRDK LQRLEAEKQQ LEEALNASQE EEGSLAAAKR ALEARLEEAQ
810 820 830 840 850
RGLARLGQEQ QTLNRALEEE GKQREVLRRG KAELEEQKRL LDRTVDRLNK
860 870 880 890 900
ELEKIGEDSK QALQQLQAQL EDYKEKARRE VADAQRQAKD WASEAEKTSG
910 920 930 940 950
GLSRLQDEIQ RLRQALQASQ AERDTARLDK ELLAQRLQGL EQEAENKKRS
960 970 980 990 1000
QDDRARQLKG LEEKVSRLET ELDEEKNTVE LLTDRVNRGR DQVDQLRTEL
1010 1020 1030 1040 1050
MQERSARQDL ECDKISLERQ NKDLKTRLAS SEGFQKPSAS LSQLESQNQL
1060 1070 1080 1090 1100
LQERLQAEER EKTVLQSTNR KLERKVKELS IQIEDERQHV NDQKDQLSLR
1110 1120 1130 1140 1150
VKALKRQVDE AEEEIERLDG LRKKAQREVE EQHEVNEQLQ ARIKSLEKDS
1160 1170 1180 1190
WRKASRSAAE SALKNEGLSS DEEFDSVYDP SSIASLLTES NLQTSSC
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.
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.
GeneTreei ENSGT00730000110843.
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

Bgeei Q9P2M7.
CleanExi HS_CGN.
ExpressionAtlasi Q9P2M7. baseline and differential.
Genevestigatori Q9P2M7.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 108 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