Reviewed, UniProtKB/Swiss-Prot Q9P2M7 (CING_HUMAN)

Names and origin

Protein names

Recommended name:
    Cingulin

Gene names

Name:	CGN
Synonyms:	KIAA1319

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier.
Subunit structure	Homodimer By similarity. Interacts with TJP1/ZO-1.
Subcellular location	Cell junction › tight junctionBy similarity. Note= Localizes to the apical junction complex composed of tight and adherens junctions By similarity.
Tissue specificity	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.
Domain	Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1.
Sequence similarities	Belongs to the cingulin family.

Ontologies

Keywords
Cellular component	Cell junction Tight junction
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	tight junction Non-traceable author statement. Source: UniProtKB
Molecular function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TJP1	Q07157	1	EBI-79537,EBI-79553
Tjp1	P39447	1	EBI-79537,EBI-79508	From a different organism.
YWHAB	P31946	1	EBI-79537,EBI-359815
YWHAG	P61981	1	EBI-79537,EBI-359832

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1197	1197	Cingulin
Regions
	Region	1 – 351	351	Head
	Region	106 – 400	295	Interacts with ZO-2
	Region	1155 – 1197	43	Tail
	Coiled coil	352 – 1154	803	Potential
	Motif	42 – 56	15	ZIM
	Compositional bias	363 – 836	474	Glu-rich
Amino acid modifications
	Modified residue	111	1	Phosphoserine By similarity
	Modified residue	112	1	Phosphoserine By similarity
	Modified residue	129	1	Phosphoserine By similarity
	Modified residue	131	1	Phosphoserine
	Modified residue	134	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	Q9P2M7-1 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: 0C9375283ABAAF3D	FASTA	1,197	136,386
	10 20 30 40 50 60 MAEPRGPVDH GVQIRFITEP VSGAEMGTLR RGGRRPAKDA RASTYGVAVR VQGIAGQPFV 70 80 90 100 110 120 VLNSGEKGGD SFGVQIKGAN DQGASGALSS DLELPENPYS QVKGFPAPSQ SSTSDEEPGA 130 140 150 160 170 180 YWNGKLLRSH SQASLAGPGP VDPSNRSNSM LELAPKVASP GSTIDTAPLS SVDSLINKFD 190 200 210 220 230 240 SQLGGQARGR TGRRTRMLPP EQRKRSKSLD SRLPRDTFEE RERQSTNHWT SSTKYDNHVG 250 260 270 280 290 300 TSKQPAQSQN LSPLSGFSRS RQTQDWVLQS FEEPRRSAQD PTMLQFKSTP DLLRDQQEAA 310 320 330 340 350 360 PPGSVDHMKA TIYGILREGS SESETSVRRK VSLVLEKMQP LVMVSSGSTK AVAGQGELTR 370 380 390 400 410 420 KVEELQRKLD EEVKKRQKLE PSQVGLERQL EEKTEECSRL QELLERRKGE AQQSNKELQN 430 440 450 460 470 480 MKRLLDQGED LRHGLETQVM ELQNKLKHVQ GPEPAKEVLL KDLLETRELL EEVLEGKQRV 490 500 510 520 530 540 EEQLRLRERE LTALKGALKE EVASRDQEVE HVRQQYQRDT EQLRRSMQDA TQDHAVLEAE 550 560 570 580 590 600 RQKMSALVRG LQRELEETSE ETGHWQSMFQ KNKEDLRATK QELLQLRMEK EEMEEELGEK 610 620 630 640 650 660 IEVLQRELEQ ARASAGDTRQ VEVLKKELLR TQEELKELQA ERQSQEVAGR HRDRELEKQL 670 680 690 700 710 720 AVLRVEADRG RELEEQNLQL QKTLQQLRQD CEEASKAKMV AEAEATVLGQ RRAAVETTLR 730 740 750 760 770 780 ETQEENDEFR RRILGLEQQL KETRGLVDGG EAVEARLRDK LQRLEAEKQQ LEEALNASQE 790 800 810 820 830 840 EEGSLAAAKR ALEARLEEAQ RGLARLGQEQ QTLNRALEEE GKQREVLRRG KAELEEQKRL 850 860 870 880 890 900 LDRTVDRLNK ELEKIGEDSK QALQQLQAQL EDYKEKARRE VADAQRQAKD WASEAEKTSG 910 920 930 940 950 960 GLSRLQDEIQ RLRQALQASQ AERDTARLDK ELLAQRLQGL EQEAENKKRS QDDRARQLKG 970 980 990 1000 1010 1020 LEEKVSRLET ELDEEKNTVE LLTDRVNRGR DQVDQLRTEL MQERSARQDL ECDKISLERQ 1030 1040 1050 1060 1070 1080 NKDLKTRLAS SEGFQKPSAS LSQLESQNQL LQERLQAEER EKTVLQSTNR KLERKVKELS 1090 1100 1110 1120 1130 1140 IQIEDERQHV NDQKDQLSLR VKALKRQVDE AEEEIERLDG LRKKAQREVE EQHEVNEQLQ 1150 1160 1170 1180 1190 ARIKSLEKDS WRKASRSAAE SALKNEGLSS DEEFDSVYDP SSIASLLTES NLQTSSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11042084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 10718198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 368-376. Tissue: Platelet.
[5]	"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: 12023291] [Abstract] Cited for: INTERACTION WITH TJP1.
[6]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, MASS SPECTROMETRY.
[7]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF263462 mRNA. Translation: AAF74498.1. Different initiation. AB037740 mRNA. Translation: BAA92557.1. Different initiation. AL365436 Genomic DNA. Translation: CAI16590.1. Different initiation.
RefSeq	NP_065821.1.
UniGene	Hs.591464
3D structure databases
HSSP	HSSP built from PDB template 1L4A based on UniProtKB O46345.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P2M7.
PTM databases
PhosphoSite	Q9P2M7.
Genome annotation databases
Ensembl	ENSG00000143375. Homo sapiens. [Contig view]
GeneID	57530.
Organism-specific databases
H-InvDB	HIX0001061.
HGNC	HGNC:17429. CGN.
HPA	CAB017193.
MIM	609473. gene.
PharmGKB	PA134938123.
HUGE	Search...
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q9P2M7.
Gene expression databases
ArrayExpress	Q9P2M7.
CleanEx	HS_CGN.
GermOnline	ENSG00000143375. Homo sapiens.
Family and domain databases
InterPro	IPR002928. Myosin_tail. [Graphical view]
Pfam	PF01576. Myosin_tail_1. 1 hit. [Graphical view]
ProDom	Q9P2M7. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

CING_HUMAN

Accession

Primary (citable) accession number: Q9P2M7
Secondary accession number(s): Q5T386, Q9NR25

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	September 23, 2008
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)