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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases. Ref.26 Ref.29
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. Interacts with ABL2 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. Forms a complex made of ABL1 and MYLK. 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.7 Ref.8 Ref.10 Ref.20 Ref.23 Ref.26 Ref.29
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cell projection › ruffle. Cell projection › dendrite By similarity. Cell projection › dendritic spine By similarity. Note: Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers By similarity. In the presence of CTTNBP2, localizes at the cell cortex By similarity. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft By similarity. Ref.2 Ref.7 Ref.26 Ref.29
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.7 Ref.8 Ref.11
Sequence similarities	Contains 7 cortactin repeats. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
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 PubMed 9054437. Source: ProtInc lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Srcin1	Q9QWI6-2	2	EBI-351886,EBI-775607	From a different organism.
WAS	P42768	3	EBI-351886,EBI-346375

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14247-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q14247-2)

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.
     538-550: YGLFPANYVELRQ → FRELAFSCVR...CLGTWVPECP

Note: No experimental confirmation available.

Isoform 3 (identifier: Q14247-3)

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.

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.22

Modified residue

198

1

N6-acetyllysine Ref.22

Modified residue

235

1

N6-acetyllysine Ref.22

Modified residue

272

1

N6-acetyllysine Ref.22

Modified residue

304

1

N6-acetyllysine Ref.22

Modified residue

309

1

N6-acetyllysine Ref.22

Modified residue

399

1

Phosphothreonine Ref.24

Modified residue

401

1

Phosphothreonine Ref.24

Modified residue

405

1

Phosphoserine Ref.9 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.24

Modified residue

411

1

Phosphothreonine Ref.19

Modified residue

417

1

Phosphoserine Ref.19

Modified residue

418

1

Phosphoserine Ref.14 Ref.19 Ref.21 Ref.24 Ref.27

Modified residue

421

1

Phosphotyrosine; by SRC Ref.17 Ref.21

Modified residue

446

1

Phosphotyrosine Ref.21

Modified residue

453

1

Phosphotyrosine Ref.12

Modified residue

486

1

Phosphotyrosine; by SRC

Modified residue

489

1

Phosphotyrosine; by SRC

Natural variations

Alternative sequence

264 – 300

37

Missing in isoform 2 and isoform 3.

VSP_043120

Alternative sequence

538 – 550

13

YGLFP…VELRQ → FRELAFSCVRVALVPIKCSR DLPGQARGLRSALWRVGRKD CPRRGASSRVSLLGRRGLGL MEVNPELSHPEHRSCHVRWE ICLCHTVTARRIRKLISFLR SREAGPVPSCSQVGGVSFQK VTWKCLGTWVPECP in isoform 2.

VSP_043121

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

506 – 510

5

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)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 9F36B5AED4992281	FASTA	634	70,959
	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 SQKDYSKGFG GKYGVQKDRM DKNASTFEDV TQVSSAYQKT 310 320 330 340 350 360 VPVEAVTSKT SNIRANFENL AKEKEQEDRR KAEAERAQRM AKERQEQEEA RRKLEEQARA 370 380 390 400 410 420 KTQTPPVSPA PQPTEERLPS SPVYEDAASF KAELSYRGPV SGTEPEPVYS MEAADYREAS 430 440 450 460 470 480 SQQGLAYATE AVYESAEAPG HYPAEDSTYD EYENDLGITA VALYDYQAAG DDEISFDPDD 490 500 510 520 530 540 IITNIEMIDD GWWRGVCKGR FRELAFSCVR VALVPIKCSR DLPGQARGLR SALWRVGRKD 550 560 570 580 590 600 CPRRGASSRV SLLGRRGLGL MEVNPELSHP EHRSCHVRWE ICLCHTVTAR RIRKLISFLR 610 620 630 SREAGPVPSC SQVGGVSFQK VTWKCLGTWV PECP
	Isoform 3 [UniParc]. Checksum: 333C09D488528C40	FASTA	513	57,467
	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 SQKDYSKGFG GKYGVQKDRM DKNASTFEDV TQVSSAYQKT 310 320 330 340 350 360 VPVEAVTSKT SNIRANFENL AKEKEQEDRR KAEAERAQRM AKERQEQEEA RRKLEEQARA 370 380 390 400 410 420 KTQTPPVSPA PQPTEERLPS SPVYEDAASF KAELSYRGPV SGTEPEPVYS MEAADYREAS 430 440 450 460 470 480 SQQGLAYATE AVYESAEAPG HYPAEDSTYD EYENDLGITA VALYDYQAAG DDEISFDPDD 490 500 510 IITNIEMIDD GWWRGVCKGR YGLFPANYVE LRQ

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Mammary gland.
[3]	"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] (ISOFORM 3).
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 2 AND 3). Tissue: Placenta and Testis.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FER, PHOSPHORYLATION OF CTTN, SUBCELLULAR LOCATION.
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYLK, PHOSPHORYLATION BY SRC.
[9]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLXDC2.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453, MASS SPECTROMETRY.
[13]	"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-405, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND TYR-421, MASS SPECTROMETRY. Tissue: Platelet.
[18]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; THR-411; SER-417 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRCIN1.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-418; TYR-421 AND TYR-446, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-235; LYS-272; LYS-304 AND LYS-309, MASS SPECTROMETRY.
[23]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYLK AND ABL1.
[24]	"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 THR-399; THR-401; SER-405 AND SER-418, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SAMSN1.
[27]	"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-418, MASS SPECTROMETRY.
[28]	"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.
[29]	"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] [Europe PMC] [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.
AK291097 mRNA. Translation: BAF83786.1.
AP000487 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74766.1.
CH471076 Genomic DNA. Translation: EAW74768.1.
BC008799 mRNA. Translation: AAH08799.1.
BC033889 mRNA. Translation: AAH33889.1.

IPI

IPI00029601.
IPI00062884.
IPI01013939.

PIR

A48063.

RefSeq

NP_001171669.1. NM_001184740.1.
NP_005222.2. NM_005231.3.
NP_612632.1. NM_138565.2.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14247. 11 interactions.

MINT

MINT-5001258.

STRING

9606.ENSP00000301843.

PTM databases

PhosphoSite

Q14247.

Polymorphism databases

DMDM

215273892.

2D gel databases

OGP

Q14247.

Proteomic databases

PaxDb

Q14247.

PRIDE

Q14247.

Protocols and materials databases

DNASU

2017.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301843; ENSP00000301843; ENSG00000085733.
ENST00000346329; ENSP00000317189; ENSG00000085733.
ENST00000376561; ENSP00000365745; ENSG00000085733.

GeneID

2017.

KEGG

hsa:2017.

UCSC

uc001opv.4. human.

Organism-specific databases

CTD

2017.

GeneCards

GC11P070244.

HGNC

HGNC:3338. CTTN.

HPA

CAB011235.

MIM

164765. gene.

neXtProt

NX_Q14247.

PharmGKB

PA27775.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG123488.

HOGENOM

HOG000006523.

HOVERGEN

HBG005994.

KO

K06106.

OMA

SQQDYSK.

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]

PANTHER

PTHR10829:SF4. PTHR10829:SF4. 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

ChiTaRS

CTTN. human.

EvolutionaryTrace

Q14247.

GenomeRNAi

2017.

NextBio

8171.

SOURCE

Search...

Entry information

Entry name

SRC8_HUMAN

Accession

Primary (citable) accession number: Q14247
Secondary accession number(s): Q8N707, Q96H99

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 136 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.