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Protein

CTTNBP2 N-terminal-like protein

Gene

CTTNBP2NL

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

Functioni

GO - Molecular functioni

  1. 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
Complete GO annotation...

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
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

BgeeiQ9P2B4.
CleanExiHS_CTTNBP2NL.
ExpressionAtlasiQ9P2B4. baseline and differential.
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, PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MOB4Q9Y3A36EBI-1774273,EBI-713935
STK24Q9Y6E04EBI-1774273,EBI-740175
STK26Q9P2894EBI-1774273,EBI-618239
STRIP1Q5VSL94EBI-1774273,EBI-1773588
STRNO438155EBI-1774273,EBI-1046642
STRN3Q130337EBI-1774273,EBI-1053857

Protein-protein interaction databases

BioGridi121000. 28 interactions.
IntActiQ9P2B4. 23 interactions.
MINTiMINT-4725988.
STRINGi9606.ENSP00000271277.

Structurei

3D structure databases

ProteinModelPortaliQ9P2B4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG301745.
GeneTreeiENSGT00680000099614.
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

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9P2B4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121000. 28 interactions.
IntActiQ9P2B4. 23 interactions.
MINTiMINT-4725988.
STRINGi9606.ENSP00000271277.

PTM databases

PhosphoSiteiQ9P2B4.

Polymorphism databases

DMDMi92087169.

Proteomic databases

MaxQBiQ9P2B4.
PaxDbiQ9P2B4.
PRIDEiQ9P2B4.

Protocols and materials databases

DNASUi55917.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55917.
GeneCardsiGC01P112938.
HGNCiHGNC:25330. CTTNBP2NL.
HPAiHPA007301.
MIMi615100. gene.
neXtProtiNX_Q9P2B4.
PharmGKBiPA142672062.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG301745.
GeneTreeiENSGT00680000099614.
HOGENOMiHOG000112036.
HOVERGENiHBG081371.
InParanoidiQ9P2B4.
OMAiFTSQQGP.
OrthoDBiEOG77M8NN.
PhylomeDBiQ9P2B4.
TreeFamiTF325130.

Miscellaneous databases

ChiTaRSiCTTNBP2NL. human.
GeneWikiiCTTNBP2NL.
GenomeRNAii55917.
NextBioi35468922.
PROiQ9P2B4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2B4.
CleanExiHS_CTTNBP2NL.
ExpressionAtlasiQ9P2B4. baseline and differential.
GenevestigatoriQ9P2B4.

Family and domain databases

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

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; PPP2R1A; PPP2CB; STK24; STK25; STK26; 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: March 4, 2015
This is version 103 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.