Q9P2B4 (CT2NL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CTTNBP2 N-terminal-like protein

Gene names

Name:	CTTNBP2NL
Synonyms:	KIAA1433

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	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Interacts with CTTN/cortactin; this interaction may redistribute CTTN to stress fibers By similarity. May form homomers. May interact with MOB4, MST4, PPP2R1A, PPP2CB, STK24, STK25, STRN4, STRIP1 and STRIP2. Ref.8
Subcellular location	Cytoplasm › cytoskeleton By similarity. Note: Colocalizes with stress fibers By similarity.
Sequence caution	The sequence BAA92671.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: LIFEdb
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MOB4	Q9Y3A3	5	EBI-1774273,EBI-713935
MST4	Q9P289	4	EBI-1774273,EBI-618239
STK24	Q9Y6E0	4	EBI-1774273,EBI-740175
STRIP1	Q5VSL9	3	EBI-1774273,EBI-1773588
STRN	O43815	3	EBI-1774273,EBI-1046642
STRN3	Q13033	4	EBI-1774273,EBI-1053857

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 639	639	CTTNBP2 N-terminal-like protein		PRO_0000226997
Regions
	Coiled coil	87 – 285	199	Potential
Amino acid modifications
	Modified residue	481	1	Phosphoserine Ref.7
	Modified residue	488	1	Phosphoserine Ref.6 Ref.7 Ref.9 Ref.11
	Modified residue	523	1	Phosphoserine Ref.6 Ref.7 Ref.9
	Modified residue	527	1	Phosphoserine Ref.7
	Modified residue	560	1	Phosphoserine Ref.5 Ref.9 Ref.11
	Modified residue	563	1	Phosphoserine Ref.9 Ref.11
	Modified residue	570	1	Phosphothreonine Ref.11
	Modified residue	590	1	Phosphothreonine Ref.7 Ref.9
	Modified residue	592	1	Phosphoserine Ref.9
Natural variations
	Natural variant	296	1	V → M. Corresponds to variant rs1175640 [ dbSNP | Ensembl ].		VAR_050925
	Natural variant	409	1	S → G. Corresponds to variant rs12137578 [ dbSNP | Ensembl ].		VAR_050926
Experimental info
	Sequence conflict	38	1	D → V in BAG51087. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9P2B4 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 63F1D27C50623564	FASTA	639	70,158
	10 20 30 40 50 60 MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI SDPLMALQRD 70 80 90 100 110 120 FETLKEKNDG EKQPVCTNPL SILKVVMKQC KNMQERMLSQ LAAAESRHRK VILDLEEERQ 130 140 150 160 170 180 RHAQDTAEGD DVTYMLEKER ERLTQQLEFE KSQVKKFEKE QKKLSSQLEE ERSRHKQLSS 190 200 210 220 230 240 MLVLECKKAT NKAAEEGQKA GELSLKLEKE KSRVSKLEEE LAAERKRGLQ TEAQVEKQLS 250 260 270 280 290 300 EFDIEREQLR AKLNREENRT KTLKEEMESL KKIVKDLEAS HQHSSPNEQL KKPVTVSKGT 310 320 330 340 350 360 ATEPLMLMSV FCQTESFPAE RTHGSNIAKM TNTGLPGPAT PAYSYAKTNG HCDPEIQTTR 370 380 390 400 410 420 ELTAGNNVEN QVPPREKSVA LAQEKPVENG GCPVGIETPV PMPSPLSSSG SSLSPSSTAS 430 440 450 460 470 480 SSLTSSPCSS PVLTKRLLGS SASSPGYQSS YQVGINQRFH AARHKFQSQA DQDQQASGLQ 490 500 510 520 530 540 SPPSRDLSPT LIDNSAAKQL ARNTVTQVLS RFTSQQGPIK PVSPNSSPFG TDYRNLANTA 550 560 570 580 590 600 NPRGDTSHSP TPGKVSSPLS PLSPGIKSPT IPRAERGNPP PIPPKKPGLT PSPSATTPLT 610 620 630 KTHSQAASLT TAEDLASSCS SNTVVANGKD VELLLPTSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Brain.
[2]	"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]. Tissue: Teratocarcinoma.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Skin.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-523, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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-481; SER-488; SER-523; SER-527 AND THR-590, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein." Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C. Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MOB4; MST4; PPP2R1A; PPP2CB; STK24; STK25; STRN4; STRIP1 AND STRIP2, HOMOMERIZATION.
[9]	"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-488; SER-523; SER-560; SER-563; THR-590 AND SER-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"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-488; SER-560; SER-563 AND THR-570, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB037854 mRNA. Translation: BAA92671.1. Different initiation. AK022544 mRNA. Translation: BAG51087.1. AL354760 Genomic DNA. Translation: CAI22308.1. BC016029 mRNA. Translation: AAH16029.1.
IPI	IPI00514311.
RefSeq	NP_061174.1. NM_018704.2.
UniGene	Hs.731817.
3D structure databases
ProteinModelPortal	Q9P2B4.
SMR	Q9P2B4. Positions 5-35.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P2B4. 19 interactions.
STRING	9606.ENSP00000271277.
PTM databases
PhosphoSite	Q9P2B4.
Polymorphism databases
DMDM	92087169.
Proteomic databases
PaxDb	Q9P2B4.
PRIDE	Q9P2B4.
Protocols and materials databases
DNASU	55917.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271277; ENSP00000271277; ENSG00000143079.
GeneID	55917.
KEGG	hsa:55917.
UCSC	uc001ebx.3. human.
Organism-specific databases
CTD	55917.
GeneCards	GC01P112938.
HGNC	HGNC:25330. CTTNBP2NL.
HPA	HPA007301.
MIM	615100. gene.
neXtProt	NX_Q9P2B4.
PharmGKB	PA142672062.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG301745.
HOGENOM	HOG000112036.
HOVERGEN	HBG081371.
InParanoid	Q9P2B4.
OMA	FTSQQGP.
OrthoDB	EOG45TCN9.
Gene expression databases
ArrayExpress	Q9P2B4.
Bgee	Q9P2B4.
CleanEx	HS_CTTNBP2NL.
Genevestigator	Q9P2B4.
GermOnline	ENSG00000143079. Homo sapiens.
Family and domain databases
InterPro	IPR019131. Cortactin-binding_p2_N. [Graphical view]
Pfam	PF09727. CortBP2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CTTNBP2NL. human.
GenomeRNAi	55917.
NextBio	61319.
SOURCE	Search...

Entry information

Entry name

CT2NL_HUMAN

Accession

Primary (citable) accession number: Q9P2B4
Secondary accession number(s): B3KMS5, Q96B40

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 85 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.