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Q9P2B4 (CT2NL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTTNBP2 N-terminal-like protein
Gene names
Name:CTTNBP2NL
Synonyms:KIAA1433
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9

Subcellular location

Cytoplasmcytoskeleton 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 componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: LIFEdb

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction Ref.9PubMed 19156129PubMed 23455922PubMed 24255178PubMed 24366813. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639CTTNBP2 N-terminal-like protein
PRO_0000226997

Regions

Coiled coil87 – 285199 Potential

Amino acid modifications

Modified residue4811Phosphoserine Ref.7
Modified residue4881Phosphoserine Ref.6 Ref.7 Ref.10 Ref.12
Modified residue5231Phosphoserine Ref.6 Ref.7 Ref.10
Modified residue5271Phosphoserine Ref.7
Modified residue5601Phosphoserine Ref.5 Ref.10 Ref.12
Modified residue5631Phosphoserine Ref.10 Ref.12
Modified residue5701Phosphothreonine Ref.12
Modified residue5901Phosphothreonine Ref.7 Ref.10
Modified residue5921Phosphoserine Ref.10

Natural variations

Natural variant2961V → M.
Corresponds to variant rs1175640 [ dbSNP | Ensembl ].
VAR_050925
Natural variant4091S → G.
Corresponds to variant rs12137578 [ dbSNP | Ensembl ].
VAR_050926

Experimental info

Sequence conflict381D → V in BAG51087. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9P2B4 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 63F1D27C50623564

FASTA63970,158
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"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.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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.
CCDSCCDS845.1.
RefSeqNP_061174.1. NM_018704.2.
UniGeneHs.744100.

3D structure databases

ProteinModelPortalQ9P2B4.
SMRQ9P2B4. Positions 5-35, 124-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121000. 26 interactions.
IntActQ9P2B4. 23 interactions.
MINTMINT-4725988.
STRING9606.ENSP00000271277.

PTM databases

PhosphoSiteQ9P2B4.

Polymorphism databases

DMDM92087169.

Proteomic databases

MaxQBQ9P2B4.
PaxDbQ9P2B4.
PRIDEQ9P2B4.

Protocols and materials databases

DNASU55917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271277; ENSP00000271277; ENSG00000143079.
GeneID55917.
KEGGhsa:55917.
UCSCuc001ebx.3. human.

Organism-specific databases

CTD55917.
GeneCardsGC01P112938.
HGNCHGNC:25330. CTTNBP2NL.
HPAHPA007301.
MIM615100. gene.
neXtProtNX_Q9P2B4.
PharmGKBPA142672062.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301745.
HOGENOMHOG000112036.
HOVERGENHBG081371.
InParanoidQ9P2B4.
OMAFTSQQGP.
OrthoDBEOG77M8NN.
PhylomeDBQ9P2B4.
TreeFamTF325130.

Gene expression databases

ArrayExpressQ9P2B4.
BgeeQ9P2B4.
CleanExHS_CTTNBP2NL.
GenevestigatorQ9P2B4.

Family and domain databases

InterProIPR019131. Cortactin-binding_p2_N.
[Graphical view]
PfamPF09727. CortBP2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTTNBP2NL. human.
GeneWikiCTTNBP2NL.
GenomeRNAi55917.
NextBio35468922.
PROQ9P2B4.
SOURCESearch...

Entry information

Entry nameCT2NL_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM