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Protein

Src substrate cortactin

Gene

Cttn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:17403031). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (PubMed:22262902). Plays a role in the invasiveness of cancer cells, and the formation of metastases (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (By similarity).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actin filament polymerization Source: InterPro
  • cell motility Source: UniProtKB
  • dendritic spine maintenance Source: MGI
  • focal adhesion assembly Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • lamellipodium organization Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • neuron projection morphogenesis Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of smooth muscle contraction Source: MGI
  • receptor-mediated endocytosis Source: UniProtKB
  • regulation of axon extension Source: UniProtKB
  • regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  • substrate-dependent cell migration, cell extension Source: MGI
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

ReactomeiREACT_359280. RHO GTPases activate PAKs.

Names & Taxonomyi

Protein namesi
Recommended name:
Src substrate cortactin
Gene namesi
Name:Cttn
Synonyms:Ems1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99695. Cttn.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Cell projectionlamellipodium
  • Cell projectionruffle
  • Cytoplasmcell cortex
  • Cell projection By similarity
  • Cell projectionpodosome By similarity
  • Cell projectiondendritic spine By similarity
  • Cell projectiondendrite By similarity
  • Cell membrane By similarity; Peripheral membrane protein Curated; Cytoplasmic side Curated
  • Cell junction By similarity
  • Membraneclathrin-coated pit By similarity
  • Cell junctionfocal adhesion By similarity

  • Note: Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft. Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity).By similarity

GO - Cellular componenti

  • actin filament Source: Ensembl
  • cell cortex Source: MGI
  • cell junction Source: UniProtKB
  • coated pit Source: UniProtKB
  • cortical cytoskeleton Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • dendritic spine Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: UniProtKB
  • mitotic spindle midzone Source: UniProtKB
  • podosome Source: UniProtKB-SubCell
  • ruffle Source: UniProtKB
  • voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221W → A: Abolishes cortactin-mediated endocytosis of KCNA2. 1 Publication
Mutagenesisi421 – 4211Y → F: No effect on interaction with KCNA2. 1 Publication
Mutagenesisi466 – 4661Y → F: No effect on interaction with KCNA2, but decreases KCNA2 levels at the cell membrane. 1 Publication
Mutagenesisi482 – 4821Y → F: No effect on interaction with KCNA2, but decreases KCNA2 levels at the cell membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Src substrate cortactinPRO_0000072190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871N6-acetyllysine1 Publication
Modified residuei124 – 1241N6-acetyllysine1 Publication
Modified residuei144 – 1441N6-acetyllysine1 Publication
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei161 – 1611N6-acetyllysine1 Publication
Modified residuei181 – 1811N6-acetyllysine1 Publication
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysine1 Publication
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-acetyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysineBy similarity
Modified residuei309 – 3091N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine1 Publication
Modified residuei401 – 4011Phosphothreonine1 Publication
Modified residuei405 – 4051Phosphoserine1 Publication
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei417 – 4171PhosphoserineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei421 – 4211PhosphotyrosineBy similarity
Modified residuei442 – 4421PhosphotyrosineBy similarity
Modified residuei443 – 4431PhosphoserineBy similarity
Modified residuei466 – 4661Phosphotyrosine; by FAK1By similarity
Modified residuei482 – 4821Phosphotyrosine; by SRC1 Publication
Modified residuei485 – 4851Phosphotyrosine; by SRC1 Publication

Post-translational modificationi

Phosphorylated by FER. Phosphorylated in response to FGR activation (PubMed:7693700). Phosphorylation by SRC promotes MYLK binding (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation (By similarity). Phosphorylated by PTK2/FAK1 in response to cell adhesion (By similarity). Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associate with filamentous actin.By similarity3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ60598.
PaxDbiQ60598.
PRIDEiQ60598.

PTM databases

PhosphoSiteiQ60598.

Expressioni

Tissue specificityi

Expressed in most tissues, except in B-lymphocytes or plasma cells.

Gene expression databases

BgeeiQ60598.
CleanExiMM_CTTN.
ExpressionAtlasiQ60598. baseline and differential.
GenevisibleiQ60598. MM.

Interactioni

Subunit structurei

Interacts with SHANK2 and SHANK3 (via its SH3 domain). Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2. Interacts with ACTN1 (By similarity). Interacts with FER. Forms a complex with ABL1 and MYLK (By similarity). Interacts with KCNA2 (via non-phosphorylated C-terminus). Interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2 (PubMed:22297987). Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Interacts with KCNH1 (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR3P611574EBI-397955,EBI-351419From a different organism.
Actr3Q99JY95EBI-397955,EBI-773994
Cbll1Q9JIY24EBI-397955,EBI-7644904
Cfl1P455922EBI-397955,EBI-917556From a different organism.
Dnm2P390542EBI-397955,EBI-642337
HDAC6Q9UBN73EBI-397955,EBI-301697From a different organism.
Kcnma1Q084602EBI-397955,EBI-1633915
MTSS1O433122EBI-397955,EBI-473954From a different organism.
WASLQ951072EBI-397955,EBI-6162776From a different organism.
WaslQ91YD94EBI-397955,EBI-642417
WIPF1O435163EBI-397955,EBI-346356From a different organism.

Protein-protein interaction databases

BioGridi198978. 8 interactions.
DIPiDIP-31562N.
IntActiQ60598. 38 interactions.
MINTiMINT-100616.
STRINGi10090.ENSMUSP00000099368.

Structurei

Secondary structure

1
546
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi493 – 4953Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi522 – 5309Combined sources
Beta strandi533 – 5386Combined sources
Helixi539 – 5413Combined sources
Beta strandi542 – 5443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9Xmodel-A1-546[»]
3ULRX-ray1.65B487-546[»]
ProteinModelPortaliQ60598.
SMRiQ60598. Positions 487-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati80 – 11637Cortactin 1Add
BLAST
Repeati117 – 15337Cortactin 2Add
BLAST
Repeati154 – 19037Cortactin 3Add
BLAST
Repeati191 – 22737Cortactin 4Add
BLAST
Repeati228 – 26437Cortactin 5Add
BLAST
Repeati265 – 30137Cortactin 6Add
BLAST
Repeati302 – 32423Cortactin 7; truncatedAdd
BLAST
Domaini488 – 54659SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili348 – 40154Sequence AnalysisAdd
BLAST

Domaini

The SH3 motif may mediate binding to the cytoskeleton.Curated

Sequence similaritiesi

Contains 7 cortactin repeats.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ60598.
KOiK06106.
OMAiWKATAGH.
OrthoDBiEOG7V49ZC.
TreeFamiTF318935.

Family and domain databases

InterProiIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF15. PTHR10829:SF15. 1 hit.
PfamiPF02218. HS1_rep. 7 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ
60 70 80 90 100
EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDRSAV
110 120 130 140 150
GHEYQSKLSK HCSQVDSVRG FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS
160 170 180 190 200
QKDYSSGFGG KYGVQADRVD KSAVGFDYQG KTEKHESQKD YSKGFGGKYG
210 220 230 240 250
IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT DRQDKCALGW
260 270 280 290 300
DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSSAVGFDYK ERLAKHESQQ
310 320 330 340 350
DYAKGFGGKY GVQKDRMDKN ASTFEEVVQV PSAYQKTVPI EAVTSKTSNI
360 370 380 390 400
RANFENLAKE REQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKKQ
410 420 430 440 450
TPPASPSPQP IEDRPPSSPI YEDAAPFKAE PSYRGSEPEP EYSIEAAGIP
460 470 480 490 500
EAGSQQGLTY TSEPVYETTE APGHYQAEDD TYDGYESDLG ITAIALYDYQ
510 520 530 540
AAGDDEISFD PDDIITNIEM IDDGWWRGVC KGRYGLFPAN YVELRQ
Length:546
Mass (Da):61,250
Last modified:July 27, 2011 - v2
Checksum:i8F5CA026ACCD6D4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91A → R AA sequence (PubMed:7693700).Curated
Sequence conflicti298 – 2981S → P in AAA19689 (PubMed:7516062).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03184 mRNA. Translation: AAA19689.1.
AK146856 mRNA. Translation: BAE27485.1.
AK148010 mRNA. Translation: BAE28287.1.
AK168699 mRNA. Translation: BAE40543.1.
CH466531 Genomic DNA. Translation: EDL18251.1.
CCDSiCCDS22049.1.
PIRiI48899.
RefSeqiNP_031829.2. NM_007803.5.
UniGeneiMm.205601.
Mm.490123.

Genome annotation databases

EnsembliENSMUST00000103079; ENSMUSP00000099368; ENSMUSG00000031078.
GeneIDi13043.
KEGGimmu:13043.
UCSCiuc009kqh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03184 mRNA. Translation: AAA19689.1.
AK146856 mRNA. Translation: BAE27485.1.
AK148010 mRNA. Translation: BAE28287.1.
AK168699 mRNA. Translation: BAE40543.1.
CH466531 Genomic DNA. Translation: EDL18251.1.
CCDSiCCDS22049.1.
PIRiI48899.
RefSeqiNP_031829.2. NM_007803.5.
UniGeneiMm.205601.
Mm.490123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9Xmodel-A1-546[»]
3ULRX-ray1.65B487-546[»]
ProteinModelPortaliQ60598.
SMRiQ60598. Positions 487-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198978. 8 interactions.
DIPiDIP-31562N.
IntActiQ60598. 38 interactions.
MINTiMINT-100616.
STRINGi10090.ENSMUSP00000099368.

PTM databases

PhosphoSiteiQ60598.

Proteomic databases

MaxQBiQ60598.
PaxDbiQ60598.
PRIDEiQ60598.

Protocols and materials databases

DNASUi13043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103079; ENSMUSP00000099368; ENSMUSG00000031078.
GeneIDi13043.
KEGGimmu:13043.
UCSCiuc009kqh.2. mouse.

Organism-specific databases

CTDi2017.
MGIiMGI:99695. Cttn.

Phylogenomic databases

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ60598.
KOiK06106.
OMAiWKATAGH.
OrthoDBiEOG7V49ZC.
TreeFamiTF318935.

Enzyme and pathway databases

ReactomeiREACT_359280. RHO GTPases activate PAKs.

Miscellaneous databases

ChiTaRSiCttn. mouse.
NextBioi282940.
PROiQ60598.
SOURCEiSearch...

Gene expression databases

BgeeiQ60598.
CleanExiMM_CTTN.
ExpressionAtlasiQ60598. baseline and differential.
GenevisibleiQ60598. MM.

Family and domain databases

InterProiIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF15. PTHR10829:SF15. 1 hit.
PfamiPF02218. HS1_rep. 7 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The protein tyrosine kinase substrate cortactin is differentially expressed in murine B lymphoid tumors."
    Miglarese M.R., Mannion-Henderson J., Wu H., Parsons J.T., Bender T.P.
    Oncogene 9:1989-1997(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Murine cortactin is phosphorylated in response to fibroblast growth factor-1 on tyrosine residues late in the G1 phase of the BALB/c 3T3 cell cycle."
    Zhan X., Hu X., Hampton B., Burgess W.H., Friesel R., Maciag T.
    J. Biol. Chem. 268:24427-24431(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 125-138; 273-289 AND 534-543, PHOSPHORYLATION.
  3. "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: Amnion and Heart.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
    Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
    Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1; FGFR4 AND GAP43.
  6. "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly interacts with cortactin and mAbp1 to modulate cell shape."
    Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B., Gorski J.L.
    Hum. Mol. Genet. 12:1981-1993(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FGD1.
  7. "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
    Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
    J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIN BUNDLE FORMATION, PHOSPHORYLATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "An essential role for cortactin in the modulation of the potassium channel Kv1.2."
    Williams M.R., Markey J.C., Doczi M.A., Morielli A.D.
    Proc. Natl. Acad. Sci. U.S.A. 104:17412-17417(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA2, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-22; TYR-421; TYR-466 AND TYR-482.
  10. Cited for: PHOSPHORYLATION AT TYR-482 AND TYR-485.
  11. "Cortactin-binding protein 2 modulates the mobility of cortactin and regulates dendritic spine formation and maintenance."
    Chen Y.K., Hsueh Y.P.
    J. Neurosci. 32:1043-1055(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTTNBP2, SUBCELLULAR LOCATION.
  12. "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 CTTNBP2NL, SUBCELLULAR LOCATION.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-124; LYS-144; LYS-161; LYS-181; LYS-198; LYS-235; LYS-272; LYS-295; LYS-309 AND LYS-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  14. "Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex."
    Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.
    Acta Crystallogr. F 68:154-158(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 487-546 IN COMPLEX WITH ABL2, INTERACTION WITH ABL2.

Entry informationi

Entry nameiSRC8_MOUSE
AccessioniPrimary (citable) accession number: Q60598
Secondary accession number(s): Q3UGC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.