Q9P2M7 (CING_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cingulin

Gene names

Name:	CGN
Synonyms:	KIAA1319

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1197 AA.
Sequence status	Complete.
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. Ref.8
Subcellular location	Cell junction › tight junction By 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.
Sequence caution	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.

Ontologies

Keywords
Cellular component	Cell junction Tight junction
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	myosin complex Inferred from electronic annotation. Source: InterPro tight junction Non-traceable author statement PubMed 12529927. Source: UniProtKB
Molecular_function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9P2M7-1)

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.

Isoform 2 (identifier: Q9P2M7-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1197	1197	Cingulin		PRO_0000089763
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 Ref.14
	Modified residue	134	1	Phosphoserine Ref.10 Ref.11 Ref.14
	Modified residue	149	1	Phosphoserine Ref.14
	Modified residue	159	1	Phosphoserine Ref.11 Ref.13 Ref.14
	Modified residue	208	1	Phosphoserine Ref.14
	Modified residue	211	1	Phosphoserine Ref.14
	Modified residue	252	1	Phosphoserine Ref.13 Ref.14
	Modified residue	573	1	N6-acetyllysine Ref.12
	Modified residue	706	1	Phosphothreonine Ref.14
	Modified residue	1176	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	698 – 771	74	KMVAE…EKQQL → RGVGTGLRRWRLRVSGGLRS QRVWKVTCHGYVLTSSWVLG MWFKEARIWQGEDTCICVGV GFSEKRLAGGSCSL in isoform 2.		VSP_037039
	Alternative sequence	772 – 1197	426	Missing in isoform 2.		VSP_037040
	Natural variant	479	1	R → Q. Corresponds to variant rs12038198 [ dbSNP | Ensembl ].		VAR_057809

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: F289EA3694E4CEC1	FASTA	771	87,047
	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 CEEASKARGV GTGLRRWRLR VSGGLRSQRV 730 740 750 760 770 WKVTCHGYVL TSSWVLGMWF KEARIWQGED TCICVGVGFS EKRLAGGSCS L

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] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-1176, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00844508. IPI00929635.
RefSeq	NP_065821.1. NM_020770.2.
UniGene	Hs.591464.
3D structure databases
ProteinModelPortal	Q9P2M7.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-30947N.
IntAct	Q9P2M7. 4 interactions.
MINT	MINT-1681123.
STRING	9606.ENSP00000271636.
PTM databases
PhosphoSite	Q9P2M7.
Polymorphism databases
DMDM	27923755.
Proteomic databases
PaxDb	Q9P2M7.
PRIDE	Q9P2M7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271636; ENSP00000271636; ENSG00000143375.
GeneID	57530.
KEGG	hsa:57530.
UCSC	uc009wmw.3. human.
Organism-specific databases
CTD	57530.
GeneCards	GC01P151483.
HGNC	HGNC:17429. CGN.
HPA	CAB017193. HPA027586. HPA027587. HPA027657.
MIM	609473. gene.
neXtProt	NX_Q9P2M7.
PharmGKB	PA134938123.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG149500.
HOVERGEN	HBG031389.
InParanoid	Q9P2M7.
KO	K06102.
OrthoDB	EOG4C87RN.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q9P2M7.
Bgee	Q9P2M7.
CleanEx	HS_CGN.
Genevestigator	Q9P2M7.
GermOnline	ENSG00000143375. Homo sapiens.
Family and domain databases
InterPro	IPR002928. Myosin_tail. [Graphical view]
Pfam	PF01576. Myosin_tail_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57530.
NextBio	63932.
SOURCE	Search...

Entry information

Entry name

CING_HUMAN

Accession

Primary (citable) accession number: Q9P2M7
Secondary accession number(s): A6H8L3 , A7MD22, Q5T386, Q9NR25

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.