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Q9P2B4

- CT2NL_HUMAN

UniProt

Q9P2B4 - CT2NL_HUMAN

Protein

CTTNBP2 N-terminal-like protein

Gene

CTTNBP2NL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase 2A binding Source: MGI

    GO - Biological processi

    1. negative regulation of transmembrane transport Source: MGI
    2. negative regulation of transporter activity Source: MGI
    3. protein dephosphorylation Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTTNBP2 N-terminal-like protein
    Gene namesi
    Name:CTTNBP2NL
    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

    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.By similarity1 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili87 – 285199Sequence AnalysisAdd
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381D → V in BAG51087. (PubMed:14702039)Curated

    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 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

    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: October 1, 2014
    This is version 98 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