Q14247 (SRC8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Src substrate cortactin

Alternative name(s):
Amplaxin
Oncogene EMS1

Gene names

Name:	CTTN
Synonyms:	EMS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Contributes to the organization of the actin cytoskeleton and cell structure. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases. Ref.30 Ref.32
Subunit structure	Interacts with SHANK2 and SHANK3 (via its SH3 domain). Also interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN By similarity. 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. Binds to MYLK. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Ref.4 Ref.5 Ref.7 Ref.25 Ref.28 Ref.30 Ref.32
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cell projection › ruffle. Note: Associated with membrane ruffles and lamellipodia. Ref.2 Ref.4 Ref.30 Ref.32
Domain	The SH3 motif may mediate binding to the cytoskeleton.
Post-translational modification	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 associates with filamentous actin By similarity. Phosphorylated by FER. Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated in response to FGR activation. Phosphorylation by SRC promotes MYLK binding. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26
Sequence similarities	Contains 7 cortactin repeats. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cell cortex Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Traceable author statement. Source: ProtInc lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction Ref.25. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Srcin1	Q9QWI6-2	2	EBI-351886,EBI-775607	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 550

550

Src substrate cortactin

PRO_0000072189

Regions

Repeat

80 – 116

37

Cortactin 1

Repeat

117 – 153

37

Cortactin 2

Repeat

154 – 190

37

Cortactin 3

Repeat

191 – 227

37

Cortactin 4

Repeat

228 – 264

37

Cortactin 5

Repeat

265 – 301

37

Cortactin 6

Repeat

302 – 324

23

Cortactin 7; truncated

Domain

492 – 550

59

SH3

Amino acid modifications

Modified residue

87

1

N6-acetyllysine Ref.27

Modified residue

113

1

Phosphoserine Ref.17

Modified residue

117

1

Phosphoserine Ref.17

Modified residue

141

1

Phosphotyrosine Ref.16

Modified residue

154

1

Phosphotyrosine Ref.24

Modified residue

198

1

N6-acetyllysine Ref.27

Modified residue

215

1

Phosphotyrosine Ref.12

Modified residue

218

1

N6-acetyllysine Ref.27

Modified residue

235

1

N6-acetyllysine Ref.27

Modified residue

272

1

N6-acetyllysine Ref.27

Modified residue

304

1

N6-acetyllysine Ref.27

Modified residue

309

1

N6-acetyllysine Ref.27

Modified residue

334

1

Phosphotyrosine Ref.10

Modified residue

399

1

Phosphothreonine Ref.17 Ref.20 Ref.22 Ref.23

Modified residue

401

1

Phosphothreonine Ref.8 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Modified residue

405

1

Phosphoserine Ref.8 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26

Modified residue

411

1

Phosphothreonine Ref.22

Modified residue

417

1

Phosphoserine Ref.17 Ref.22 Ref.23

Modified residue

418

1

Phosphoserine Ref.8 Ref.14 Ref.15 Ref.19 Ref.20 Ref.22 Ref.23 Ref.26

Modified residue

421

1

Phosphotyrosine; by SRC Ref.6 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.26

Modified residue

446

1

Phosphotyrosine Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 Ref.24 Ref.26

Modified residue

453

1

Phosphotyrosine Ref.10 Ref.12

Experimental info

Sequence conflict

495

1

I → Y in AAA58455. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

550

Helix Strand Turn

Details...

Beta strand

497 – 499

3

Beta strand

518 – 523

6

Beta strand

526 – 534

9

Beta strand

537 – 542

6

Helix

543 – 545

3

Beta strand

546 – 548

3

Sequences

	Sequence		Length	Mass (Da)
	Q14247 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 7799326C2B4383BB	FASTA	550	61,586
	10 20 30 40 50 60 MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE 70 80 90 100 110 120 NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV GHEYQSKLSK HCSQVDSVRG 130 140 150 160 170 180 FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG 190 200 210 220 230 240 KTEKHESQRD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT 250 260 270 280 290 300 DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ 310 320 330 340 350 360 DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI RANFENLAKE 370 380 390 400 410 420 KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ TPPVSPAPQP TEERLPSSPV 430 440 450 460 470 480 YEDAASFKAE LSYRGPVSGT EPEPVYSMEA ADYREASSQQ GLAYATEAVY ESAEAPGHYP 490 500 510 520 530 540 AEDSTYDEYE NDLGITAVAL YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL 550 FPANYVELRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and cloning of two overexpressed genes, U21B31/PRAD1 and EMS1, within the amplified chromosome 11q13 region in human carcinomas." Schuuring E.M.D., Verhoeven E., Mooi W.J., Michalides R.J.A. Oncogene 7:355-361(1992) [PubMed: 1532244] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	"The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites." Schuuring E.M.D., Verhoeven E., Litvinov S., Michalides R.J.A. Mol. Cell. Biol. 13:2891-2898(1993) [PubMed: 8474448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Mammary gland.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER." Kim L., Wong T.W. J. Biol. Chem. 273:23542-23548(1998) [PubMed: 9722593] [Abstract] Cited for: INTERACTION WITH FER, PHOSPHORYLATION OF CTTN, SUBCELLULAR LOCATION.
[5]	"Novel interaction of cortactin with endothelial cell myosin light chain kinase." Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N. Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed: 12408982] [Abstract] Cited for: INTERACTION WITH MYLK, PHOSPHORYLATION BY SRC.
[6]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421, MASS SPECTROMETRY.
[7]	"Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R." Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P., Shankara S., Nacht M., Teicher B., Stampfl J., Singh S., Vogelstein B., Kinzler K.W., St Croix B. Cancer Res. 64:8507-8511(2004) [PubMed: 15574754] [Abstract] Cited for: INTERACTION WITH PLXDC2.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization." Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G. Exp. Cell Res. 302:253-269(2005) [PubMed: 15561106] [Abstract] Cited for: PHOSPHORYLATION.
[10]	"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)." Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A. J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334; TYR-446 AND TYR-453, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215; TYR-446 AND TYR-453, MASS SPECTROMETRY.
[13]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-117; THR-399; THR-401; SER-405; SER-417 AND TYR-421, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421 AND TYR-446, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; SER-418 AND TYR-421, MASS SPECTROMETRY. Tissue: Platelet.
[21]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-405, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; THR-411; SER-417 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; SER-417; SER-418 AND TYR-421, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154; TYR-421 AND TYR-446, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[25]	"Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity." Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S., Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J., Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C. Neuron 61:85-100(2009) [PubMed: 19146815] [Abstract] Cited for: INTERACTION WITH SRCIN1.
[26]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-418; TYR-421 AND TYR-446, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-218; LYS-235; LYS-272; LYS-304 AND LYS-309, MASS SPECTROMETRY.
[28]	"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function." Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N. Mol. Biol. Cell 21:4042-4056(2010) [PubMed: 20861316] [Abstract] Cited for: INTERACTION WITH MYLK AND ABL1.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"The immunoinhibitory adapter protein SRC homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading." von Holleben M., Gohla A., Janssen K.P., Iritani B.M., Beer-Hammer S. J. Biol. Chem. 286:13489-13501(2011) [PubMed: 21296879] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SAMSN1.
[31]	"Solution structures of the SH3 domain of human Src substrate cortactin." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 485-550.
[32]	"Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis." Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H. Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed: 16636290] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 490-550 IN COMPLEX WITH ASAP1, FUNCTION, INTERACTION WITH ASAP1 AND DNM2, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Web resources

Wikipedia

Cortactin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M98343 mRNA. Translation: AAA58455.1.
AP000487 Genomic DNA. No translation available.

IPI

IPI00029601.

PIR

A48063.

RefSeq

NP_005222.2. NM_005231.3.

UniGene

Hs.596164.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X69	NMR	-	A	485-550	[»]
2D1X	X-ray	1.90	A/B/C/D	490-550	[»]

ProteinModelPortal

Q14247.

SMR

Q14247. Positions 485-550.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14247. 7 interactions.

MINT

MINT-5001258.

STRING

Q14247.

PTM databases

PhosphoSite

Q14247.

Polymorphism databases

DMDM

215273892.

2D gel databases

OGP

Q14247.

Proteomic databases

PRIDE

Q14247.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301843; ENSP00000301843; ENSG00000085733.

GeneID

2017.

KEGG

hsa:2017.

Organism-specific databases

CTD

2017.

GeneCards

GC11P070244.

H-InvDB

HIX0009895.

HGNC

HGNC:3338. CTTN.

HPA

CAB011235.

MIM

164765. gene.

neXtProt

NX_Q14247.

PharmGKB

PA27775.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07378.

HOVERGEN

HBG005994.

OrthoDB

EOG4RNB86.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.
syndecan_3_pathway. Syndecan-3-mediated signaling events.

Gene expression databases

ArrayExpress

Q14247.

Bgee

Q14247.

CleanEx

HS_CTTN.

Genevestigator

Q14247.

GermOnline

ENSG00000085733. Homo sapiens.

Family and domain databases

InterPro

IPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR000108. p67phox.
IPR001452. SH3_domain.
[Graphical view]

KO

K06106.

PANTHER

PTHR10829:SF4. Cortactin. 1 hit.

Pfam

PF02218. HS1_rep. 7 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

SRC8_HUMAN

Accession

Primary (citable) accession number: Q14247

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.