Detail Information for IndEnz0002004598
IED ID IndEnz0002004598
Enzyme Type ID protease004598
Protein Name CUB domain-containing protein 1
Membrane glycoprotein gp140
Subtractive immunization M plus HEp3-associated 135 kDa protein
SIMA135
Transmembrane and associated with src kinases
CD antigen CD318
Gene Name CDCP1 TRASK UNQ2486/PRO5773
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAGLNCGVSIALLGVLLLGAARLPRGAEAFEIALPRESNITVLIKLGTPTLLAKPCYIVISKRHITMLSIKSGERIVFTFSCQSPENHFVIEIQKNIDCMSGPCPFGEVQLQPSTSLLPTLNRTFIWDVKAHKSIGLELQFSIPRLRQIGPGESCPDGVTHSISGRIDATVVRIGTFCSNGTVSRIKMQEGVKMALHLPWFHPRNVSGFSIANRSSIKRLCIIESVFEGEGSATLMSANYPEGFPEDELMTWQFVVPAHLRASVSFLNFNLSNCERKEERVEYYIPGSTTNPEVFKLEDKQPGNMAGNFNLSLQGCDQDAQSPGILRLQFQVLVQHPQNESNKIYVVDLSNERAMSLTIEPRPVKQSRKFVPGCFVCLESRTCSSNLTLTSGSKHKISFLCDDLTRLWMNVEKTISCTDHRYCQRKSYSLQVPSDILHLPVELHDFSWKLLVPKDRLSLVLVPAQKLQQHTHEKPCNTSFSYLVASAIPSQDLYFGSFCPGGSIKQIQVKQNISVTLRTFAPSFQQEASRQGLTVSFIPYFKEEGVFTVTPDTKSKVYLRTPNWDRGLPSLTSVSWNISVPRDQVACLTFFKERSGVVCQTGRAFMIIQEQRTRAEEIFSLDEDVLPKPSFHHHSFWVNISNCSPTSGKQLDLLFSVTLTPRTVDLTVILIAAVGGGVLLLSALGLIICCVKKKKKKTNKGPAVGIYNDNINTEMPRQPKKFQKGRKDNDSHVYAVIEDTMVYGHLLQDSSGSFLQPEVDTYRPFQGTMGVCPPSPPTICSRAPTAKLATEEPPPRSPPESESEPYTFSHPNNGDVSSKDTDIPLLNTQEPMEPAE
Enzyme Length 836
Uniprot Accession Number Q9H5V8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis. {ECO:0000269|PubMed:11466621, ECO:0000269|PubMed:12799299, ECO:0000269|PubMed:15153610, ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16404722, ECO:0000269|PubMed:8647901}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (7); Modified residue (1); Mutagenesis (2); Natural variant (3); Region (1); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Membrane;Phosphoprotein;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix
Interact With O00560; P12931; P07947
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Shedding may also lead to a soluble peptide.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
Modified Residue MOD_RES 734; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:14739293
Post Translational Modification PTM: Phosphorylated on tyrosine by kinases of the SRC family such as SRC and YES as well as by the protein kinase C gamma/PRKCG. Dephosphorylated by phosphotyrosine phosphatases. Also phosphorylated by suramin, a heparin analog. Tyrosine phosphorylated in response to dissociation of integrin alpha-6 beta-4 from laminin-5. {ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14739293, ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:8647901}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14739293, ECO:0000269|PubMed:16007225}.; PTM: A soluble form may also be produced by proteolytic cleavage at the cell surface (shedding). Another peptide of 80 kDa (p80) is present in cultured keratinocytes probably due to tryptic cleavage at an unidentified site on its N-terminal side. Converted to p80 by plasmin, a trypsin-like protease.
Signal Peptide SIGNAL 1..29; /evidence="ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:16007225"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15174051; 15657067; 16926850; 17785447; 18269919; 18467693; 18483259; 18483744; 19077003; 19318475; 19463016; 19671673; 19916495; 20372833; 20501830; 20551327; 21189288; 21220330; 21233420; 21490433; 21559459; 21617380; 21706059; 21725358; 21812858; 21994943; 22315226; 22457534; 23208492; 23300860; 23378636; 23439492; 23510015; 23747337; 24384474; 24681947; 24849519; 24939643; 25275584; 25301083; 25416956; 25728678; 25775948; 25820997; 25876044; 25892239; 25893298; 26307391; 26497208; 26553452; 26876198; 26956052; 27495374; 27626701; 27685922; 28537886; 28739932; 29351434; 29433983; 29447112; 29511352; 29574172; 29792166; 30396925; 31364124; 31471585; 31965270; 32226543; 32250342; 32983115; 33060289; 33260155; 33267838; 33674603; 33859413;
Motif
Gene Encoded By
Mass 92,932
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda