SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9P2B4

- CT2NL_HUMAN

UniProt

Q9P2B4 - CT2NL_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

CTTNBP2 N-terminal-like protein

Gene
CTTNBP2NL, KIAA1433
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
CTTNBP2 N-terminal-like protein
Gene namesi
Synonyms:KIAA1433
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:25330. CTTNBP2NL.

Subcellular locationi

Cytoplasmcytoskeleton By similarity
Note: Colocalizes with stress fibers By similarity.

GO - Cellular componenti

  1. actin cytoskeleton Source: LIFEdb
  2. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639CTTNBP2 N-terminal-like proteinPRO_0000226997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei488 – 4881Phosphoserine4 Publications
Modified residuei523 – 5231Phosphoserine3 Publications
Modified residuei527 – 5271Phosphoserine1 Publication
Modified residuei560 – 5601Phosphoserine3 Publications
Modified residuei563 – 5631Phosphoserine2 Publications
Modified residuei570 – 5701Phosphothreonine1 Publication
Modified residuei590 – 5901Phosphothreonine2 Publications
Modified residuei592 – 5921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P2B4.
PaxDbiQ9P2B4.
PRIDEiQ9P2B4.

PTM databases

PhosphoSiteiQ9P2B4.

Expressioni

Gene expression databases

ArrayExpressiQ9P2B4.
BgeeiQ9P2B4.
CleanExiHS_CTTNBP2NL.
GenevestigatoriQ9P2B4.

Organism-specific databases

HPAiHPA007301.

Interactioni

Subunit structurei

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 STRIP2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MOB4Q9Y3A36EBI-1774273,EBI-713935
MST4Q9P2894EBI-1774273,EBI-618239
STK24Q9Y6E04EBI-1774273,EBI-740175
STRIP1Q5VSL94EBI-1774273,EBI-1773588
STRNO438155EBI-1774273,EBI-1046642
STRN3Q130337EBI-1774273,EBI-1053857

Protein-protein interaction databases

BioGridi121000. 26 interactions.
IntActiQ9P2B4. 23 interactions.
MINTiMINT-4725988.
STRINGi9606.ENSP00000271277.

Structurei

3D structure databases

ProteinModelPortaliQ9P2B4.
SMRiQ9P2B4. Positions 5-35, 124-276.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili87 – 285199 Reviewed predictionAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG301745.
HOGENOMiHOG000112036.
HOVERGENiHBG081371.
InParanoidiQ9P2B4.
OMAiFTSQQGP.
OrthoDBiEOG77M8NN.
PhylomeDBiQ9P2B4.
TreeFamiTF325130.

Family and domain databases

InterProiIPR019131. Cortactin-binding_p2_N.
[Graphical view]
PfamiPF09727. CortBP2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P2B4-1 [UniParc]FASTAAdd to Basket

« Hide

MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI    50
SDPLMALQRD FETLKEKNDG EKQPVCTNPL SILKVVMKQC KNMQERMLSQ 100
LAAAESRHRK VILDLEEERQ RHAQDTAEGD DVTYMLEKER ERLTQQLEFE 150
KSQVKKFEKE QKKLSSQLEE ERSRHKQLSS MLVLECKKAT NKAAEEGQKA 200
GELSLKLEKE KSRVSKLEEE LAAERKRGLQ TEAQVEKQLS EFDIEREQLR 250
AKLNREENRT KTLKEEMESL KKIVKDLEAS HQHSSPNEQL KKPVTVSKGT 300
ATEPLMLMSV FCQTESFPAE RTHGSNIAKM TNTGLPGPAT PAYSYAKTNG 350
HCDPEIQTTR ELTAGNNVEN QVPPREKSVA LAQEKPVENG GCPVGIETPV 400
PMPSPLSSSG SSLSPSSTAS SSLTSSPCSS PVLTKRLLGS SASSPGYQSS 450
YQVGINQRFH AARHKFQSQA DQDQQASGLQ SPPSRDLSPT LIDNSAAKQL 500
ARNTVTQVLS RFTSQQGPIK PVSPNSSPFG TDYRNLANTA NPRGDTSHSP 550
TPGKVSSPLS PLSPGIKSPT IPRAERGNPP PIPPKKPGLT PSPSATTPLT 600
KTHSQAASLT TAEDLASSCS SNTVVANGKD VELLLPTSS 639
Length:639
Mass (Da):70,158
Last modified:March 7, 2006 - v2
Checksum:i63F1D27C50623564
GO

Sequence cautioni

The sequence BAA92671.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti296 – 2961V → M.
Corresponds to variant rs1175640 [ dbSNP | Ensembl ].
VAR_050925
Natural varianti409 – 4091S → G.
Corresponds to variant rs12137578 [ dbSNP | Ensembl ].
VAR_050926

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381D → V in BAG51087. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB037854 mRNA. Translation: BAA92671.1. Different initiation.
AK022544 mRNA. Translation: BAG51087.1.
AL354760 Genomic DNA. Translation: CAI22308.1.
BC016029 mRNA. Translation: AAH16029.1.
CCDSiCCDS845.1.
RefSeqiNP_061174.1. NM_018704.2.
UniGeneiHs.744100.

Genome annotation databases

EnsembliENST00000271277; ENSP00000271277; ENSG00000143079.
GeneIDi55917.
KEGGihsa:55917.
UCSCiuc001ebx.3. human.

Polymorphism databases

DMDMi92087169.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB037854 mRNA. Translation: BAA92671.1 . Different initiation.
AK022544 mRNA. Translation: BAG51087.1 .
AL354760 Genomic DNA. Translation: CAI22308.1 .
BC016029 mRNA. Translation: AAH16029.1 .
CCDSi CCDS845.1.
RefSeqi NP_061174.1. NM_018704.2.
UniGenei Hs.744100.

3D structure databases

ProteinModelPortali Q9P2B4.
SMRi Q9P2B4. Positions 5-35, 124-276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121000. 26 interactions.
IntActi Q9P2B4. 23 interactions.
MINTi MINT-4725988.
STRINGi 9606.ENSP00000271277.

PTM databases

PhosphoSitei Q9P2B4.

Polymorphism databases

DMDMi 92087169.

Proteomic databases

MaxQBi Q9P2B4.
PaxDbi Q9P2B4.
PRIDEi Q9P2B4.

Protocols and materials databases

DNASUi 55917.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000271277 ; ENSP00000271277 ; ENSG00000143079 .
GeneIDi 55917.
KEGGi hsa:55917.
UCSCi uc001ebx.3. human.

Organism-specific databases

CTDi 55917.
GeneCardsi GC01P112938.
HGNCi HGNC:25330. CTTNBP2NL.
HPAi HPA007301.
MIMi 615100. gene.
neXtProti NX_Q9P2B4.
PharmGKBi PA142672062.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301745.
HOGENOMi HOG000112036.
HOVERGENi HBG081371.
InParanoidi Q9P2B4.
OMAi FTSQQGP.
OrthoDBi EOG77M8NN.
PhylomeDBi Q9P2B4.
TreeFami TF325130.

Miscellaneous databases

ChiTaRSi CTTNBP2NL. human.
GeneWikii CTTNBP2NL.
GenomeRNAii 55917.
NextBioi 35468922.
PROi Q9P2B4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9P2B4.
Bgeei Q9P2B4.
CleanExi HS_CTTNBP2NL.
Genevestigatori Q9P2B4.

Family and domain databases

InterProi IPR019131. Cortactin-binding_p2_N.
[Graphical view ]
Pfami PF09727. CortBP2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. 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. 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].

Entry informationi

Entry nameiCT2NL_HUMAN
AccessioniPrimary (citable) accession number: Q9P2B4
Secondary accession number(s): B3KMS5, Q96B40
Entry historyi
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 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, 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

External Data

Dasty 3

Similar proteinsi