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Protein

CTTNBP2 N-terminal-like protein

Gene

Cttnbp2nl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1933137. Cttnbp2nl.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication
Note: Colocalizes with stress fibers.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638CTTNBP2 N-terminal-like proteinPRO_0000226998Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei526 – 5261PhosphoserineBy similarity
Modified residuei559 – 5591PhosphoserineBy similarity
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei569 – 5691PhosphothreonineBy similarity
Modified residuei589 – 5891PhosphothreonineBy similarity
Modified residuei591 – 5911PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99LJ0.
PaxDbiQ99LJ0.
PRIDEiQ99LJ0.

PTM databases

PhosphoSiteiQ99LJ0.

Expressioni

Tissue specificityi

Predominantly expressed in skin, also detectable in spleen and lung (at protein level). Very low levels, if any, in brain (at protein level).

Gene expression databases

BgeeiQ99LJ0.
CleanExiMM_CTTNBP2NL.
GenevestigatoriQ99LJ0.

Interactioni

Subunit structurei

May form homomers (By similarity). May interact with MOB4, PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2 (By similarity). Interacts with CTTN/cortactin; this interaction may redistribute CTTN to stress fibers.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096359.

Structurei

3D structure databases

ProteinModelPortaliQ99LJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili87 – 284198Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG301745.
GeneTreeiENSGT00680000099614.
HOGENOMiHOG000112036.
HOVERGENiHBG081371.
InParanoidiQ99LJ0.
OMAiFTSQQGP.
OrthoDBiEOG77M8NN.
PhylomeDBiQ99LJ0.
TreeFamiTF325130.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q99LJ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI
60 70 80 90 100
SDPLMALQRD FETLKEKNDS EKQPVCTNPL SVLKAVMKQC KNMQERMLSQ
110 120 130 140 150
LAAAESRHRK VILDLEEERQ RHAQDTAEGD DVTYMLEKER ERLTQQLEFE
160 170 180 190 200
KSQVKKFEKE QKKLSSQLEE ERTRHKQLSS MLVLECRKAT SKAAEEGQKA
210 220 230 240 250
GELSLKLDKE KSRASKLEEE LAAERKRGLQ TEAQVEKQLS EFDIEREQLR
260 270 280 290 300
AKLNREENRT RALKEEVESL KKLVKDLEAA QQHRSTSEQG REPVTMSRGT
310 320 330 340 350
ATEPPMRVSA FCQTESVQTE RSHGSVITKL TDTGLPGPTT AAYSYAKANG
360 370 380 390 400
HCDPEIQTTR ELTSDSSTEN QGPPREKSAV AAQEKPVENG GCPVGTETPV
410 420 430 440 450
TMPSHLPSSG SSLSPSSTAS SSLTSSPCSS PVLTKRLLGS AASSPGYQSS
460 470 480 490 500
YQVGINQRFH AARHKFQSQA DQDQQASGLQ SPPSRDLSPT LLDNSAAKQL
510 520 530 540 550
ARNTVTQVLS RFTNQGPIKP VSPNSSPFGT DYRNLASTAS PRGDTSHSPT
560 570 580 590 600
PGKVSSPLSP LSPGIKSPTI PRAERGNPPP IPPKKPGLTP SQSATTPVTK
610 620 630
THSQASSLAA TEDLASSCSP SAVVANGKDV EILLPTSS
Length:638
Mass (Da):69,841
Last modified:June 1, 2001 - v1
Checksum:i9E3CC4364E73972C
GO

Sequence cautioni

The sequence BAC98169.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921N → D in BAC26964. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129359 mRNA. Translation: BAC98169.1. Different initiation.
AK029901 mRNA. Translation: BAC26666.1.
AK030438 mRNA. Translation: BAC26964.1.
BC003236 mRNA. Translation: AAH03236.1.
BC006952 mRNA. Translation: AAH06952.1.
CCDSiCCDS17707.1.
RefSeqiNP_001156804.1. NM_001163332.1.
NP_001156805.1. NM_001163333.1.
NP_084525.1. NM_030249.4.
UniGeneiMm.200327.

Genome annotation databases

EnsembliENSMUST00000077548; ENSMUSP00000076751; ENSMUSG00000062127.
ENSMUST00000098763; ENSMUSP00000096359; ENSMUSG00000062127.
GeneIDi80281.
KEGGimmu:80281.
UCSCiuc008quv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129359 mRNA. Translation: BAC98169.1. Different initiation.
AK029901 mRNA. Translation: BAC26666.1.
AK030438 mRNA. Translation: BAC26964.1.
BC003236 mRNA. Translation: AAH03236.1.
BC006952 mRNA. Translation: AAH06952.1.
CCDSiCCDS17707.1.
RefSeqiNP_001156804.1. NM_001163332.1.
NP_001156805.1. NM_001163333.1.
NP_084525.1. NM_030249.4.
UniGeneiMm.200327.

3D structure databases

ProteinModelPortaliQ99LJ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096359.

PTM databases

PhosphoSiteiQ99LJ0.

Proteomic databases

MaxQBiQ99LJ0.
PaxDbiQ99LJ0.
PRIDEiQ99LJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077548; ENSMUSP00000076751; ENSMUSG00000062127.
ENSMUST00000098763; ENSMUSP00000096359; ENSMUSG00000062127.
GeneIDi80281.
KEGGimmu:80281.
UCSCiuc008quv.2. mouse.

Organism-specific databases

CTDi55917.
MGIiMGI:1933137. Cttnbp2nl.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG301745.
GeneTreeiENSGT00680000099614.
HOGENOMiHOG000112036.
HOVERGENiHBG081371.
InParanoidiQ99LJ0.
OMAiFTSQQGP.
OrthoDBiEOG77M8NN.
PhylomeDBiQ99LJ0.
TreeFamiTF325130.

Miscellaneous databases

ChiTaRSiCttnbp2nl. mouse.
NextBioi349965.
PROiQ99LJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LJ0.
CleanExiMM_CTTNBP2NL.
GenevestigatoriQ99LJ0.

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 mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pituitary and Testis.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic distribution of the striatin-PP2A complex."
    Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.
    Mol. Biol. Cell 23:4383-4392(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTN, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCT2NL_MOUSE
AccessioniPrimary (citable) accession number: Q99LJ0
Secondary accession number(s): Q6ZPR0, Q8BSV1, Q922L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) 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.