Q14511 (CASL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enhancer of filamentation 1
Short name=hEF1

Alternative name(s):
CRK-associated substrate-related protein
Short name=CAS-L
Short name=CasL
Cas scaffolding protein family member 2
Neural precursor cell expressed developmentally down-regulated protein 9
Short name=NEDD-9
Renal carcinoma antigen NY-REN-12
p105

Cleaved into the following chain:

1. Enhancer of filamentation 1 p55

Gene names

Name:	NEDD9
Synonyms:	CASL, CASS2

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	834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May function in transmitting growth control signals between focal adhesions at the cell periphery and the mitotic spindle in response to adhesion or growth factor signals initiating cell proliferation. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRK, NCK and SHPTP2 to the tyrosine phosphorylated form.
Subunit structure	Interacts with BCAR3 and SH2D3C By similarity. Homodimer. Can heterodimerize with HLH proteins ID2, E12, E47 and also with p130cas. Forms complexes in vivo with related adhesion focal tyrosine kinase (RAFTK), adapter protein CRKL and LYN kinase. Interacts with MICAL and TXNL4/DIM1. Ref.13 Ref.14
Subcellular location	Cytoplasm › cell cortex. Nucleus. Golgi apparatus. Cell projection › lamellipodium. Cytoplasm. Cell junction › focal adhesion. Note: Localizes to both the cell nucleus and the cell periphery and is differently localized in fibroblasts and epithelial cells. In fibroblasts is predominantly nuclear and in some cells is present in the Golgi apparatus. In epithelial cells localized predominantly in the cell periphery with particular concentration in lamellipodia but is also found in the nucleus. Isoforms p105 and p115 are predominantly cytoplasmic and associate with focal adhesions while p55 associates with mitotic spindle. Enhancer of filamentation 1 p55: Cytoplasm › cytoskeleton › spindle.
Tissue specificity	Widely expressed. Higher levels detected in kidney, lung, and placenta. Also detected in T-cells, B-cells and diverse cell lines. The protein has been detected in lymphocytes, in diverse cell lines, and in lung tissues.
Induction	Activated upon induction of cell growth.
Domain	Contains a central domain containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif confers specific interaction with the HLH proteins ID2, E12 and E47. It is absolutely required for the induction of pseudohyphal growth in yeast and mediates homodimerization and heterodimerization with p130cas. Ref.12 The SH3 domain interacts with two proline-rich regions of PTK2/FAK1. Ref.12
Post-translational modification	Cell cycle-regulated processing produces four isoforms: p115, p105, p65, and p55. Isoform p115 arises from p105 phosphorylation and appears later in the cell cycle. Isoform p55 arises from p105 as a result of cleavage at a caspase cleavage-related site and it appears specifically at mitosis. The p65 isoform is poorly detected. PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Ligation of either integrin beta-1 or B-cell antigen receptor on tonsillar B-cells and B-cell lines promotes tyrosine phosphorylation and both integrin and BCR-mediated tyrosine phosphorylation requires an intact actin network. In fibroblasts transformation with oncogene v-ABL results in an increase in tyrosine phosphorylation. Transiently phosphorylated following CD3 cross-linking and this phosphorylated form binds to CRK and C3G. A mutant lacking the SH3 domain is phosphorylated upon CD3 cross-linking but not upon integrin beta-1 cross-linking. Tyrosine phosphorylation occurs upon stimulation of the G-protein coupled C1a calcitonin receptor. Calcitonin-stimulated tyrosine phosphorylation is mediated by calcium- and protein kinase C-dependent mechanisms and requires the integrity of the actin cytoskeleton. Phosphorylation at Ser-369 induces proteasomal degradation. Ref.7 Ref.8 Ref.10 Ref.17
Sequence similarities	Belongs to the CAS family. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cell adhesion Cell cycle Cell division Growth regulation Mitosis
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Golgi apparatus Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Non-traceable author statement Ref.14. Source: UniProtKB cell adhesion Non-traceable author statement Ref.9. Source: ProtInc cell division Inferred from electronic annotation. Source: UniProtKB-KW integrin-mediated signaling pathway Non-traceable author statement Ref.14. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Traceable author statement Ref.9. Source: ProtInc focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.1. Source: ProtInc spindle Traceable author statement Ref.9. Source: ProtInc spindle pole Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q14511-1)

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: Q14511-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-174: ITPVRTGHGYVYEYPSRYQK → FQRDGQVSYFLVRASKQTSL
     175-834: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q14511-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MKYK → MWTR

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 834

834

Enhancer of filamentation 1

PRO_0000089328

Chain

1 – ?

Enhancer of filamentation 1 p55

PRO_0000296242

Regions

Domain

3 – 65

63

SH3

Region

102 – 229

128

Interacts strongly with spindle-regulatory protein D1M1

Region

710 – 760

51

Divergent helix-loop-helix motif

Motif

360 – 363

4

Caspase cleavage related site

Amino acid modifications

Modified residue

92

1

Phosphotyrosine By similarity

Modified residue

177

1

Phosphotyrosine By similarity

Modified residue

189

1

Phosphotyrosine By similarity

Modified residue

296

1

Phosphoserine Ref.8 Ref.10 Ref.17

Modified residue

369

1

Phosphoserine Ref.8 Ref.10 Ref.17

Natural variations

Alternative sequence

1 – 4

4

MKYK → MWTR in isoform 3.

VSP_044579

Alternative sequence

155 – 174

20

ITPVR…SRYQK → FQRDGQVSYFLVRASKQTSL in isoform 2.

VSP_042835

Alternative sequence

175 – 834

660

Missing in isoform 2.

VSP_042836

Natural variant

178

1

D → N.
Corresponds to variant rs11546959 [ dbSNP | Ensembl ].

VAR_054082

Natural variant

304

1

P → L.
Corresponds to variant rs34184473 [ dbSNP | Ensembl ].

VAR_054083

Natural variant

577

1

T → M.
Corresponds to variant rs3734401 [ dbSNP | Ensembl ].

VAR_021857

Experimental info

Sequence conflict

139

1

Q → R in BAF85371. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

834

Helix Strand Turn

Details...

Helix

406 – 430

25

Helix

438 – 442

5

Turn

443 – 446

4

Helix

447 – 473

27

Helix

480 – 508

29

Turn

509 – 511

3

Helix

513 – 516

4

Helix

527 – 535

9

Helix

538 – 551

14

Helix

553 – 556

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C54DEC36C8C8E9E6	FASTA	834	92,861
	10 20 30 40 50 60 MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV 70 80 90 100 110 120 KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPP SYQNQGIYQV 130 140 150 160 170 180 PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV GKKVITPVRT GHGYVYEYPS RYQKDVYDIP 190 200 210 220 230 240 PSHTTQGVYD IPPSSAKGPV FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD 250 260 270 280 290 300 YDFPPPMRQA GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN 310 320 330 340 350 360 HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH NPPDAKGSRD 370 380 390 400 410 420 LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK RLFLDPDTAI ERLQRLQQAL 430 440 450 460 470 480 EMGVSSLMAL VTTDWRCYGY MERHINEIRT AVDKVELFLK EYLHFVKGAV ANAACLPELI 490 500 510 520 530 540 LHNKMKRELQ RVEDSHQILS QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD 550 560 570 580 590 600 DAKQLTTTIN TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN 610 620 630 640 650 660 KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK ENIMKQNKMQ 670 680 690 700 710 720 LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV SAQDRQLLCF YYDQCETHFI 730 740 750 760 770 780 SLLNAIDALF SCVSSAQPPR IFVAHSKFVI LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS 790 800 810 820 830 NQLCEQLKTI VMATKMAALH YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF
	Isoform 2 [UniParc]. Checksum: D7C42D0C07FCECC0	FASTA	174	19,285
	10 20 30 40 50 60 MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV 70 80 90 100 110 120 KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPP SYQNQGIYQV 130 140 150 160 170 PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV GKKVFQRDGQ VSYFLVRASK QTSL
	Isoform 3 [UniParc]. Checksum: C6895E14FA35AE86	FASTA	834	92,885
	10 20 30 40 50 60 MWTRNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV 70 80 90 100 110 120 KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPP SYQNQGIYQV 130 140 150 160 170 180 PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV GKKVITPVRT GHGYVYEYPS RYQKDVYDIP 190 200 210 220 230 240 PSHTTQGVYD IPPSSAKGPV FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD 250 260 270 280 290 300 YDFPPPMRQA GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN 310 320 330 340 350 360 HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH NPPDAKGSRD 370 380 390 400 410 420 LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK RLFLDPDTAI ERLQRLQQAL 430 440 450 460 470 480 EMGVSSLMAL VTTDWRCYGY MERHINEIRT AVDKVELFLK EYLHFVKGAV ANAACLPELI 490 500 510 520 530 540 LHNKMKRELQ RVEDSHQILS QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD 550 560 570 580 590 600 DAKQLTTTIN TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN 610 620 630 640 650 660 KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK ENIMKQNKMQ 670 680 690 700 710 720 LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV SAQDRQLLCF YYDQCETHFI 730 740 750 760 770 780 SLLNAIDALF SCVSSAQPPR IFVAHSKFVI LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS 790 800 810 820 830 NQLCEQLKTI VMATKMAALH YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae." Law S.F., Estojak J., Wang B., Mysliwiec T., Kruh G., Golemis E.A. Mol. Cell. Biol. 16:3327-3337(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes." Minegishi M., Tachibana K., Sato T., Iwata S., Nojima Y., Morimoto C. J. Exp. Med. 184:1365-1375(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lymphoma.
[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). Tissue: Thymus.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.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 1 AND 2). Tissue: Brain and Lung.
[7]	"Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells." Manie S.N., Beck A.R.P., Astier A., Law S.F., Canty T., Hirai H., Druker B.J., Avraham H., Haghayeghi N., Sattler M., Salgia R., Griffin J.D., Golemis E.A., Freedman A.S. J. Biol. Chem. 272:4230-4236(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INCREASED TYROSINE PHOSPHORYLATION BY LIGATION OF INTEGRIN-B1 AND BCR.
[8]	"Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates." Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S., Hirai H., Morimoto C. J. Biol. Chem. 272:29083-29090(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.
[9]	"Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments." Law S.F., Zhang Y.-Z., Klein-Szanto A.J.P., Golemis E.A. Mol. Cell. Biol. 18:3540-3551(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[10]	"T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G." Ohashi Y., Tachibana K., Kamiguchi K., Fujita H., Morimoto C. J. Biol. Chem. 273:6446-6451(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES UPON CD3 CROSS-LINKING.
[11]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[12]	"Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain." Law S.F., Zhang Y.-Z., Fashena S.J., Toby G., Estojak J., Golemis E.A. Exp. Cell Res. 252:224-235(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF CARBOXY-TERMINAL DOMAIN.
[13]	"Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for Dim1 interactions with hnRNP F and Npw38/PQBP-1." Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A. Gene 257:33-43(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TXNL4.
[14]	"MICAL, a novel CasL interacting molecule, associates with vimentin." Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., Hirai H. J. Biol. Chem. 277:14933-14941(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MICAL.
[15]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"Phosphorylation of human enhancer of filamentation (HEF1) on serine 369 induces its proteasomal degradation." Hivert V., Pierre J., Raingeaud J. Biochem. Pharmacol. 78:1017-1025(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-296 AND SER-369.
[18]	"Northeast structural genomics consortium target HR5554A." Northeast structural genomics consortium (NESG) Submitted (FEB-2011) to the PDB data bank Cited for: STRUCTURE BY NMR OF 399-563.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L43821 mRNA. Translation: AAA98770.1.
U64317 mRNA. Translation: AAB53696.1.
AK292682 mRNA. Translation: BAF85371.1.
AL022098 Genomic DNA. No translation available.
AL136139, AL139807 Genomic DNA. Translation: CAI22676.1.
AL136139, AL139807 Genomic DNA. Translation: CAI22677.1.
AL139807, AL136139 Genomic DNA. Translation: CAI21579.1.
AL139807, AL136139 Genomic DNA. Translation: CAI21580.1.
AL512382 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55299.1.
CH471087 Genomic DNA. Translation: EAW55301.1.
BC020686 mRNA. Translation: AAH20686.1.
BC040207 mRNA. Translation: AAH40207.1.

IPI

IPI00031407.
IPI00514103.
IPI00965935.

RefSeq

NP_001135865.1. NM_001142393.1.
NP_001257962.1. NM_001271033.1.
NP_006394.1. NM_006403.3.
NP_892011.2. NM_182966.3.

UniGene

Hs.37982.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L81	NMR	-	A	399-563	[»]

ProteinModelPortal

Q14511.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14511. 7 interactions.

MINT

MINT-1175514.

STRING

9606.ENSP00000368759.

PTM databases

PhosphoSite

Q14511.

Polymorphism databases

DMDM

8134360.

Proteomic databases

PaxDb

Q14511.

PRIDE

Q14511.

Protocols and materials databases

DNASU

4739.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379433; ENSP00000368745; ENSG00000111859.
ENST00000379446; ENSP00000368759; ENSG00000111859.
ENST00000504387; ENSP00000422871; ENSG00000111859.

GeneID

4739.

KEGG

hsa:4739.

UCSC

uc003mzv.2. human.

Organism-specific databases

CTD

4739.

GeneCards

GC06M011183.

HGNC

HGNC:7733. NEDD9.

HPA

CAB009720.

MIM

602265. gene.

neXtProt

NX_Q14511.

PharmGKB

PA31538.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG82196.

HOGENOM

HOG000261698.

HOVERGEN

HBG004354.

InParanoid

Q14511.

KO

K16832.

OMA

VGAQDRQ.

OrthoDB

EOG43XV2X.

PhylomeDB

Q14511.

Gene expression databases

ArrayExpress

Q14511.

Bgee

Q14511.

CleanEx

HS_NEDD9.

Genevestigator

Q14511.

GermOnline

ENSG00000111859. Homo sapiens.

Family and domain databases

InterPro

IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

4739.

NextBio

18276.

PMAP-CutDB

Q14511.

SOURCE

Search...

Entry information

Entry name

CASL_HUMAN

Accession

Primary (citable) accession number: Q14511
Secondary accession number(s): A8K9G7 , A8MSJ9, G5E9Y9, Q5T9R4, Q5XKI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 140 of the entry and version 1 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.