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Q14511

- CASL_HUMAN

UniProt

Q14511 - CASL_HUMAN

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Protein

Enhancer of filamentation 1

Gene

NEDD9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  1. actin filament bundle assembly Source: UniProtKB
  2. cell adhesion Source: ProtInc
  3. cytoskeleton organization Source: UniProtKB
  4. integrin-mediated signaling pathway Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB-KW
  6. regulation of growth Source: UniProtKB-KW
  7. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Cell cycle, Cell division, Growth regulation, Mitosis

Enzyme and pathway databases

SignaLinkiQ14511.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:NEDD9
Synonyms:CASL, CASS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7733. NEDD9.

Subcellular locationi

Cytoplasmcell cortex. Nucleus. Golgi apparatus. Cell projectionlamellipodium. Cytoplasm. Cell junctionfocal 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.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: ProtInc
  4. Golgi apparatus Source: UniProtKB-KW
  5. nucleus Source: ProtInc
  6. spindle Source: ProtInc
  7. spindle pole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 834834Enhancer of filamentation 1PRO_0000089328Add
BLAST
Chaini1 – ?Enhancer of filamentation 1 p55PRO_0000296242

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei369 – 3691Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14511.
PaxDbiQ14511.
PRIDEiQ14511.

PTM databases

PhosphoSiteiQ14511.

Miscellaneous databases

PMAP-CutDBQ14511.

Expressioni

Tissue specificityi

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.

Inductioni

Activated upon induction of cell growth.

Gene expression databases

BgeeiQ14511.
CleanExiHS_NEDD9.
ExpressionAtlasiQ14511. baseline and differential.
GenevestigatoriQ14511.

Organism-specific databases

HPAiCAB009720.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi110816. 29 interactions.
IntActiQ14511. 16 interactions.
MINTiMINT-1175514.
STRINGi9606.ENSP00000368759.

Structurei

Secondary structure

1
834
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi406 – 43025
Helixi438 – 4425
Turni443 – 4464
Helixi447 – 47327
Helixi480 – 50829
Turni509 – 5113
Helixi513 – 5164
Helixi527 – 5359
Helixi538 – 55114
Helixi553 – 5564

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L81NMR-A399-563[»]
ProteinModelPortaliQ14511.
SMRiQ14511. Positions 5-65, 399-563, 704-832.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6563SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 229128Interacts strongly with spindle-regulatory protein D1M1Add
BLAST
Regioni710 – 76051Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 3634Caspase cleavage related site

Domaini

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.
The SH3 domain interacts with two proline-rich regions of PTK2/FAK1.

Sequence similaritiesi

Belongs to the CAS family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG82196.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiQ14511.
KOiK16832.
OMAiYEYPSRY.
OrthoDBiEOG7QRQTD.
PhylomeDBiQ14511.
TreeFamiTF328782.

Family and domain databases

InterProiIPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14511-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG
60 70 80 90 100
RQGIVPGNRV KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA
110 120 130 140 150
PRDTIYQVPP SYQNQGIYQV PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV
160 170 180 190 200
GKKVITPVRT GHGYVYEYPS RYQKDVYDIP PSHTTQGVYD IPPSSAKGPV
210 220 230 240 250
FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD YDFPPPMRQA
260 270 280 290 300
GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN
310 320 330 340 350
HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH
360 370 380 390 400
NPPDAKGSRD LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK
410 420 430 440 450
RLFLDPDTAI ERLQRLQQAL EMGVSSLMAL VTTDWRCYGY MERHINEIRT
460 470 480 490 500
AVDKVELFLK EYLHFVKGAV ANAACLPELI LHNKMKRELQ RVEDSHQILS
510 520 530 540 550
QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD DAKQLTTTIN
560 570 580 590 600
TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN
610 620 630 640 650
KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK
660 670 680 690 700
ENIMKQNKMQ LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV
710 720 730 740 750
SAQDRQLLCF YYDQCETHFI SLLNAIDALF SCVSSAQPPR IFVAHSKFVI
760 770 780 790 800
LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS NQLCEQLKTI VMATKMAALH
810 820 830
YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF
Length:834
Mass (Da):92,861
Last modified:November 1, 1996 - v1
Checksum:iC54DEC36C8C8E9E6
GO
Isoform 2 (identifier: Q14511-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:174
Mass (Da):19,285
Checksum:iD7C42D0C07FCECC0
GO
Isoform 3 (identifier: Q14511-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:834
Mass (Da):92,885
Checksum:iC6895E14FA35AE86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391Q → R in BAF85371. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781D → N.
Corresponds to variant rs11546959 [ dbSNP | Ensembl ].
VAR_054082
Natural varianti304 – 3041P → L.
Corresponds to variant rs34184473 [ dbSNP | Ensembl ].
VAR_054083
Natural varianti577 – 5771T → M.
Corresponds to variant rs3734401 [ dbSNP | Ensembl ].
VAR_021857

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MKYK → MWTR in isoform 3. 1 PublicationVSP_044579
Alternative sequencei155 – 17420ITPVR…SRYQK → FQRDGQVSYFLVRASKQTSL in isoform 2. 1 PublicationVSP_042835Add
BLAST
Alternative sequencei175 – 834660Missing in isoform 2. 1 PublicationVSP_042836Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34340.1. [Q14511-2]
CCDS4520.1. [Q14511-1]
CCDS47373.1. [Q14511-3]
RefSeqiNP_001135865.1. NM_001142393.1. [Q14511-3]
NP_001257962.1. NM_001271033.1.
NP_006394.1. NM_006403.3. [Q14511-1]
NP_892011.2. NM_182966.3. [Q14511-2]
UniGeneiHs.37982.

Genome annotation databases

EnsembliENST00000379433; ENSP00000368745; ENSG00000111859. [Q14511-2]
ENST00000379446; ENSP00000368759; ENSG00000111859. [Q14511-1]
ENST00000504387; ENSP00000422871; ENSG00000111859. [Q14511-3]
GeneIDi4739.
KEGGihsa:4739.
UCSCiuc003mzv.2. human. [Q14511-1]
uc003mzx.3. human. [Q14511-2]
uc010joz.2. human.

Polymorphism databases

DMDMi8134360.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34340.1. [Q14511-2 ]
CCDS4520.1. [Q14511-1 ]
CCDS47373.1. [Q14511-3 ]
RefSeqi NP_001135865.1. NM_001142393.1. [Q14511-3 ]
NP_001257962.1. NM_001271033.1.
NP_006394.1. NM_006403.3. [Q14511-1 ]
NP_892011.2. NM_182966.3. [Q14511-2 ]
UniGenei Hs.37982.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L81 NMR - A 399-563 [» ]
ProteinModelPortali Q14511.
SMRi Q14511. Positions 5-65, 399-563, 704-832.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110816. 29 interactions.
IntActi Q14511. 16 interactions.
MINTi MINT-1175514.
STRINGi 9606.ENSP00000368759.

PTM databases

PhosphoSitei Q14511.

Polymorphism databases

DMDMi 8134360.

Proteomic databases

MaxQBi Q14511.
PaxDbi Q14511.
PRIDEi Q14511.

Protocols and materials databases

DNASUi 4739.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379433 ; ENSP00000368745 ; ENSG00000111859 . [Q14511-2 ]
ENST00000379446 ; ENSP00000368759 ; ENSG00000111859 . [Q14511-1 ]
ENST00000504387 ; ENSP00000422871 ; ENSG00000111859 . [Q14511-3 ]
GeneIDi 4739.
KEGGi hsa:4739.
UCSCi uc003mzv.2. human. [Q14511-1 ]
uc003mzx.3. human. [Q14511-2 ]
uc010joz.2. human.

Organism-specific databases

CTDi 4739.
GeneCardsi GC06M011183.
HGNCi HGNC:7733. NEDD9.
HPAi CAB009720.
MIMi 602265. gene.
neXtProti NX_Q14511.
PharmGKBi PA31538.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82196.
GeneTreei ENSGT00490000043324.
HOGENOMi HOG000261698.
HOVERGENi HBG004354.
InParanoidi Q14511.
KOi K16832.
OMAi YEYPSRY.
OrthoDBi EOG7QRQTD.
PhylomeDBi Q14511.
TreeFami TF328782.

Enzyme and pathway databases

SignaLinki Q14511.

Miscellaneous databases

GeneWikii NEDD9.
GenomeRNAii 4739.
NextBioi 18276.
PMAP-CutDB Q14511.
PROi Q14511.
SOURCEi Search...

Gene expression databases

Bgeei Q14511.
CleanExi HS_NEDD9.
ExpressionAtlasi Q14511. baseline and differential.
Genevestigatori Q14511.

Family and domain databases

InterProi IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.

Entry informationi

Entry nameiCASL_HUMAN
AccessioniPrimary (citable) accession number: Q14511
Secondary accession number(s): A8K9G7
, A8MSJ9, G5E9Y9, Q5T9R4, Q5XKI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3