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Q60598 (SRC8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Src substrate cortactin
Gene names
Name:Cttn
Synonyms:Ems1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the organization of the actin cytoskeleton and cell structure. 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. Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density By similarity. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases. Ref.7 Ref.10

Subunit structure

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 with DNM2 and FER. Forms a complex with ABL1 and MYLK By similarity. Interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2. 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. Ref.5 Ref.6 Ref.10 Ref.11 Ref.13

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle. Cytoplasmcell cortex. Cell projectiondendritic spine By similarity. Cell projectiondendrite By similarity. Note: 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 By similarity. Ref.6 Ref.10 Ref.11

Tissue specificity

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

Domain

The SH3 motif may mediate binding to the cytoskeleton.

Post-translational modification

Phosphorylated by FER. Phosphorylated in response to FGR activation. Phosphorylation by SRC promotes MYLK binding 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. Ref.7 Ref.9

Sequence similarities

Contains 7 cortactin repeats.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Src substrate cortactin
PRO_0000072190

Regions

Repeat80 – 11637Cortactin 1
Repeat117 – 15337Cortactin 2
Repeat154 – 19037Cortactin 3
Repeat191 – 22737Cortactin 4
Repeat228 – 26437Cortactin 5
Repeat265 – 30137Cortactin 6
Repeat302 – 32423Cortactin 7; truncated
Domain488 – 54659SH3

Amino acid modifications

Modified residue871N6-acetyllysine Ref.12
Modified residue1241N6-acetyllysine Ref.12
Modified residue1441N6-acetyllysine Ref.12
Modified residue1611N6-acetyllysine Ref.12
Modified residue1811N6-acetyllysine Ref.12
Modified residue1981N6-acetyllysine Ref.12
Modified residue2351N6-acetyllysine Ref.12
Modified residue2721N6-acetyllysine Ref.12
Modified residue2951N6-acetyllysine Ref.12
Modified residue3041N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine Ref.12
Modified residue3461N6-acetyllysine Ref.12
Modified residue4011Phosphothreonine Ref.8
Modified residue4051Phosphoserine Ref.8
Modified residue4071Phosphoserine Ref.8
Modified residue4171Phosphoserine By similarity
Modified residue4181Phosphoserine By similarity
Modified residue4211Phosphotyrosine By similarity
Modified residue4421Phosphotyrosine By similarity
Modified residue4821Phosphotyrosine; by SRC Ref.9
Modified residue4851Phosphotyrosine; by SRC Ref.9

Experimental info

Sequence conflict91A → R AA sequence Ref.2
Sequence conflict2981S → P in AAA19689. Ref.1

Secondary structure

........... 546
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60598 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 8F5CA026ACCD6D4F

FASTA54661,250
        10         20         30         40         50         60 
MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE 

        70         80         90        100        110        120 
NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDRSAV GHEYQSKLSK HCSQVDSVRG 

       130        140        150        160        170        180 
FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG 

       190        200        210        220        230        240 
KTEKHESQKD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT 

       250        260        270        280        290        300 
DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSSAVGFDYK ERLAKHESQQ 

       310        320        330        340        350        360 
DYAKGFGGKY GVQKDRMDKN ASTFEEVVQV PSAYQKTVPI EAVTSKTSNI RANFENLAKE 

       370        380        390        400        410        420 
REQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKKQ TPPASPSPQP IEDRPPSSPI 

       430        440        450        460        470        480 
YEDAAPFKAE PSYRGSEPEP EYSIEAAGIP EAGSQQGLTY TSEPVYETTE APGHYQAEDD 

       490        500        510        520        530        540 
TYDGYESDLG ITAIALYDYQ AAGDDEISFD PDDIITNIEM IDDGWWRGVC KGRYGLFPAN 


YVELRQ 

« Hide

References

« Hide 'large scale' references
[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.
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin."
Mukherjee M., Chow S.Y., Yusoff P., Seetharaman J., Ng C., Sinniah S., Koh X.W., Asgar N.F., Li D., Yim D., Jackson R.A., Yew J., Qian J., Iyu A., Lim Y.P., Zhou X., Sze S.K., Guy G.R., Sivaraman J.
EMBO J. 31:1308-1319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-482 AND TYR-485.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI48899.
RefSeqNP_031829.2. NM_007803.5.
XP_006508535.1. XM_006508472.1.
UniGeneMm.205601.
Mm.490123.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9Xmodel-A1-546[»]
3ULRX-ray1.65B487-546[»]
ProteinModelPortalQ60598.
SMRQ60598. Positions 487-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198978. 7 interactions.
DIPDIP-31562N.
IntActQ60598. 38 interactions.
MINTMINT-100616.

PTM databases

PhosphoSiteQ60598.

Proteomic databases

PaxDbQ60598.
PRIDEQ60598.

Protocols and materials databases

DNASU13043.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103079; ENSMUSP00000099368; ENSMUSG00000031078.
GeneID13043.
KEGGmmu:13043.
UCSCuc009kqh.2. mouse.

Organism-specific databases

CTD2017.
MGIMGI:99695. Cttn.

Phylogenomic databases

eggNOGNOG123488.
GeneTreeENSGT00530000062953.
HOGENOMHOG000006523.
HOVERGENHBG005994.
InParanoidQ3UGC2.
KOK06106.
OMAHESQQDY.
OrthoDBEOG7V49ZC.
TreeFamTF318935.

Gene expression databases

ArrayExpressQ60598.
BgeeQ60598.
CleanExMM_CTTN.
GenevestigatorQ60598.

Family and domain databases

InterProIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10829:SF4. PTHR10829:SF4. 1 hit.
PfamPF02218. HS1_rep. 7 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282940.
PROQ60598.
SOURCESearch...

Entry information

Entry nameSRC8_MOUSE
AccessionPrimary (citable) accession number: Q60598
Secondary accession number(s): Q3UGC2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot