Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H5V8

- CDCP1_HUMAN

UniProt

Q9H5V8 - CDCP1_HUMAN

Protein

CUB domain-containing protein 1

Gene

CDCP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei368 – 3692Cleavage; by ST14/MT-SP1

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CUB domain-containing protein 1
    Alternative name(s):
    Membrane glycoprotein gp140
    Subtractive immunization M plus HEp3-associated 135 kDa protein
    Short name:
    SIMA135
    Transmembrane and associated with src kinases
    CD_antigen: CD318
    Gene namesi
    Name:CDCP1
    Synonyms:TRASK
    ORF Names:UNQ2486/PRO5773
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:24357. CDCP1.

    Subcellular locationi

    Isoform 1 : Cell membrane Curated; Single-pass membrane protein Curated
    Note: Shedding may also lead to a soluble peptide.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi734 – 7341Y → F: Impaired association with SRC. 1 Publication
    Mutagenesisi762 – 7621Y → F: Impaired association with protein kinase PRKCG but not with SRC. 1 Publication

    Organism-specific databases

    PharmGKBiPA142672140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29292 PublicationsAdd
    BLAST
    Chaini30 – 836807CUB domain-containing protein 1PRO_0000226249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi476 ↔ 499By similarity
    Modified residuei707 – 7071Phosphotyrosine
    Modified residuei734 – 7341Phosphotyrosine1 Publication

    Post-translational modificationi

    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-5.4 Publications
    N-glycosylated.3 Publications
    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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H5V8.
    PaxDbiQ9H5V8.
    PRIDEiQ9H5V8.

    PTM databases

    PhosphoSiteiQ9H5V8.

    Expressioni

    Tissue specificityi

    Highly expressed in mitotic cells with low expression during interphase. Detected at highest levels in skeletal muscle and colon with lower levels in kidney, small intestine, placenta and lung. Up-regulated in a number of human tumor cell lines, as well as in colorectal cancer, breast carcinoma and lung cancer. Also expressed in cells with phenotypes reminiscent of mesenchymal stem cells and neural stem cells.4 Publications

    Gene expression databases

    BgeeiQ9H5V8.
    CleanExiHS_CDCP1.
    GenevestigatoriQ9H5V8.

    Organism-specific databases

    HPAiCAB025637.
    HPA010978.
    HPA010979.

    Interactioni

    Subunit structurei

    Interacts with CDH2/N-cadherin, CDH3/P-cadherin, SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. Also interacts with SRC and PRKCG/protein kinase C gamma.2 Publications

    Protein-protein interaction databases

    BioGridi122336. 2 interactions.
    DIPiDIP-33861N.
    IntActiQ9H5V8. 5 interactions.
    MINTiMINT-1346387.
    STRINGi9606.ENSP00000296129.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H5V8.
    SMRiQ9H5V8. Positions 122-213, 231-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 667638ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini689 – 836148CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei668 – 68821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini417 – 544128CUBAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CUB domain.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG27234.
    HOVERGENiHBG081070.
    InParanoidiQ9H5V8.
    KOiK06732.
    OMAiSIKRLCI.
    OrthoDBiEOG72RMXC.
    PhylomeDBiQ9H5V8.
    TreeFamiTF331392.

    Family and domain databases

    Gene3Di2.60.120.290. 1 hit.
    InterProiIPR000859. CUB_dom.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 1 hit.

    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: Q9H5V8-1) [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

    MAGLNCGVSI ALLGVLLLGA ARLPRGAEAF EIALPRESNI TVLIKLGTPT    50
    LLAKPCYIVI SKRHITMLSI KSGERIVFTF SCQSPENHFV IEIQKNIDCM 100
    SGPCPFGEVQ LQPSTSLLPT LNRTFIWDVK AHKSIGLELQ FSIPRLRQIG 150
    PGESCPDGVT HSISGRIDAT VVRIGTFCSN GTVSRIKMQE GVKMALHLPW 200
    FHPRNVSGFS IANRSSIKRL CIIESVFEGE GSATLMSANY PEGFPEDELM 250
    TWQFVVPAHL RASVSFLNFN LSNCERKEER VEYYIPGSTT NPEVFKLEDK 300
    QPGNMAGNFN LSLQGCDQDA QSPGILRLQF QVLVQHPQNE SNKIYVVDLS 350
    NERAMSLTIE PRPVKQSRKF VPGCFVCLES RTCSSNLTLT SGSKHKISFL 400
    CDDLTRLWMN VEKTISCTDH RYCQRKSYSL QVPSDILHLP VELHDFSWKL 450
    LVPKDRLSLV LVPAQKLQQH THEKPCNTSF SYLVASAIPS QDLYFGSFCP 500
    GGSIKQIQVK QNISVTLRTF APSFQQEASR QGLTVSFIPY FKEEGVFTVT 550
    PDTKSKVYLR TPNWDRGLPS LTSVSWNISV PRDQVACLTF FKERSGVVCQ 600
    TGRAFMIIQE QRTRAEEIFS LDEDVLPKPS FHHHSFWVNI SNCSPTSGKQ 650
    LDLLFSVTLT PRTVDLTVIL IAAVGGGVLL LSALGLIICC VKKKKKKTNK 700
    GPAVGIYNDN INTEMPRQPK KFQKGRKDND SHVYAVIEDT MVYGHLLQDS 750
    SGSFLQPEVD TYRPFQGTMG VCPPSPPTIC SRAPTAKLAT EEPPPRSPPE 800
    SESEPYTFSH PNNGDVSSKD TDIPLLNTQE PMEPAE 836
    Length:836
    Mass (Da):92,932
    Last modified:January 11, 2011 - v3
    Checksum:i544FFDBBDD371518
    GO
    Isoform 2 (identifier: Q9H5V8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-187: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:649
    Mass (Da):72,723
    Checksum:iCA14C5F721CDCD49
    GO
    Isoform 3 (identifier: Q9H5V8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         342-343: NK → SE
         344-836: Missing.

    Show »
    Length:343
    Mass (Da):37,818
    Checksum:i3E4E13379DD94D1B
    GO

    Sequence cautioni

    The sequence BAB15388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521W → C in BAB14695. (PubMed:14702039)Curated
    Sequence conflicti284 – 2841Y → D in BAB15388. (PubMed:14702039)Curated
    Sequence conflicti434 – 4341S → G in BAB14695. (PubMed:14702039)Curated
    Sequence conflicti466 – 4661K → R in BAB15388. (PubMed:14702039)Curated
    Sequence conflicti827 – 8271N → S in AAO33397. (PubMed:12660814)Curated
    Sequence conflicti827 – 8271N → S in BAB15511. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti525 – 5251Q → R.3 Publications
    Corresponds to variant rs3749191 [ dbSNP | Ensembl ].
    VAR_025498
    Natural varianti673 – 6731A → V.1 Publication
    Corresponds to variant rs35428731 [ dbSNP | Ensembl ].
    VAR_055095
    Natural varianti709 – 7091D → G.3 Publications
    Corresponds to variant rs9874077 [ dbSNP | Ensembl ].
    VAR_025499

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 187187Missing in isoform 2. 1 PublicationVSP_017432Add
    BLAST
    Alternative sequencei342 – 3432NK → SE in isoform 3. 2 PublicationsVSP_017433
    Alternative sequencei344 – 836493Missing in isoform 3. 2 PublicationsVSP_017434Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY026461 mRNA. Translation: AAK02058.1.
    AF468010 mRNA. Translation: AAO33397.1.
    AY167484 mRNA. Translation: AAO34538.1.
    AY358779 mRNA. Translation: AAQ89139.1.
    AK023834 mRNA. Translation: BAB14695.1.
    AK026187 mRNA. Translation: BAB15388.1. Different initiation.
    AK026622 mRNA. Translation: BAB15511.1.
    AC104165 Genomic DNA. No translation available.
    AC105902 Genomic DNA. No translation available.
    BC021099 mRNA. Translation: AAH21099.1.
    BC069254 mRNA. Translation: AAH69254.1.
    AY375452 mRNA. Translation: AAR21289.1.
    CCDSiCCDS2727.1. [Q9H5V8-1]
    CCDS46812.1. [Q9H5V8-3]
    RefSeqiNP_073753.3. NM_022842.4. [Q9H5V8-1]
    NP_835488.1. NM_178181.2. [Q9H5V8-3]
    UniGeneiHs.476093.

    Genome annotation databases

    EnsembliENST00000296129; ENSP00000296129; ENSG00000163814. [Q9H5V8-1]
    ENST00000425231; ENSP00000399342; ENSG00000163814. [Q9H5V8-3]
    GeneIDi64866.
    KEGGihsa:64866.
    UCSCiuc003com.3. human. [Q9H5V8-1]
    uc003con.3. human. [Q9H5V8-3]

    Polymorphism databases

    DMDMi317373455.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY026461 mRNA. Translation: AAK02058.1 .
    AF468010 mRNA. Translation: AAO33397.1 .
    AY167484 mRNA. Translation: AAO34538.1 .
    AY358779 mRNA. Translation: AAQ89139.1 .
    AK023834 mRNA. Translation: BAB14695.1 .
    AK026187 mRNA. Translation: BAB15388.1 . Different initiation.
    AK026622 mRNA. Translation: BAB15511.1 .
    AC104165 Genomic DNA. No translation available.
    AC105902 Genomic DNA. No translation available.
    BC021099 mRNA. Translation: AAH21099.1 .
    BC069254 mRNA. Translation: AAH69254.1 .
    AY375452 mRNA. Translation: AAR21289.1 .
    CCDSi CCDS2727.1. [Q9H5V8-1 ]
    CCDS46812.1. [Q9H5V8-3 ]
    RefSeqi NP_073753.3. NM_022842.4. [Q9H5V8-1 ]
    NP_835488.1. NM_178181.2. [Q9H5V8-3 ]
    UniGenei Hs.476093.

    3D structure databases

    ProteinModelPortali Q9H5V8.
    SMRi Q9H5V8. Positions 122-213, 231-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122336. 2 interactions.
    DIPi DIP-33861N.
    IntActi Q9H5V8. 5 interactions.
    MINTi MINT-1346387.
    STRINGi 9606.ENSP00000296129.

    PTM databases

    PhosphoSitei Q9H5V8.

    Polymorphism databases

    DMDMi 317373455.

    Proteomic databases

    MaxQBi Q9H5V8.
    PaxDbi Q9H5V8.
    PRIDEi Q9H5V8.

    Protocols and materials databases

    DNASUi 64866.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296129 ; ENSP00000296129 ; ENSG00000163814 . [Q9H5V8-1 ]
    ENST00000425231 ; ENSP00000399342 ; ENSG00000163814 . [Q9H5V8-3 ]
    GeneIDi 64866.
    KEGGi hsa:64866.
    UCSCi uc003com.3. human. [Q9H5V8-1 ]
    uc003con.3. human. [Q9H5V8-3 ]

    Organism-specific databases

    CTDi 64866.
    GeneCardsi GC03M045123.
    H-InvDB HIX0003238.
    HGNCi HGNC:24357. CDCP1.
    HPAi CAB025637.
    HPA010978.
    HPA010979.
    MIMi 611735. gene.
    neXtProti NX_Q9H5V8.
    PharmGKBi PA142672140.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG27234.
    HOVERGENi HBG081070.
    InParanoidi Q9H5V8.
    KOi K06732.
    OMAi SIKRLCI.
    OrthoDBi EOG72RMXC.
    PhylomeDBi Q9H5V8.
    TreeFami TF331392.

    Miscellaneous databases

    ChiTaRSi CDCP1. human.
    GeneWikii CDCP1.
    GenomeRNAii 64866.
    NextBioi 67027.
    PROi Q9H5V8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H5V8.
    CleanExi HS_CDCP1.
    Genevestigatori Q9H5V8.

    Family and domain databases

    Gene3Di 2.60.120.290. 1 hit.
    InterProi IPR000859. CUB_dom.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel gene, CDCP1, overexpressed in human colorectal cancer."
      Scherl-Mostageer M., Sommergruber W., Abseher R., Hauptmann R., Ambros P., Schweifer N.
      Oncogene 20:4402-4408(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT GLY-709.
    2. "Subtractive immunization using highly metastatic human tumor cells identifies SIMA135/CDCP1, a 135 kDa cell surface phosphorylated glycoprotein antigen."
      Hooper J.D., Zijlstra A., Aimes R.T., Liang H., Claassen G.F., Tarin D., Testa J.E., Quigley J.P.
      Oncogene 22:1783-1794(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-48; 281-293 AND 427-438, GLYCOSYLATION, PHOSPHORYLATION, SHEDDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ARG-525 AND GLY-709.
    3. "Adhesion signaling by a novel mitotic substrate of src kinases."
      Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.
      Oncogene 24:5333-5343(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-34 AND 369-375, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH CDH2; CDH3; SDC1; SDC4 AND ST14, FUNCTION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. "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] (ISOFORMS 1 AND 2), VARIANTS ARG-525 AND GLY-709.
      Tissue: Placenta.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-697 (ISOFORM 1), VARIANT VAL-673.
      Tissue: Kidney.
    8. "Adhesion or plasmin regulates tyrosine phosphorylation of a novel membrane glycoprotein p80/gp140/CUB domain-containing protein 1 in epithelia."
      Brown T.A., Yang T.M., Zaitsevskaia T., Xia Y., Dunn C.A., Sigle R.O., Knudsen B., Carter W.G.
      J. Biol. Chem. 279:14772-14783(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-691 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-734, GLYCOSYLATION, TRYPTIC CLEAVAGE, VARIANT ARG-525.
      Tissue: Epidermis.
    9. "Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane-associated 80-kD protein."
      Xia Y., Gil S.G., Carter W.G.
      J. Cell Biol. 132:727-740(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
      Tissue: Epidermis.
    10. Cited for: FUNCTION.
    11. "CDCP1 identifies a broad spectrum of normal and malignant stem/progenitor cell subsets of hematopoietic and nonhematopoietic origin."
      Buehring H.-J., Kuci S., Conze T., Rathke G., Bartolovic K., Gruenebach F., Scherl-Mostageer M., Bruemmendorf T.H., Schweifer N., Lammers R.
      Stem Cells 22:334-343(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. "The C2 domain of PKCdelta is a phosphotyrosine binding domain."
      Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.
      Cell 121:271-280(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SRC AND PRKCG, MUTAGENESIS OF TYR-734 AND TYR-762.
    13. "Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-FTICR-MS."
      Andre M., Le Caer J.-P., Greco C., Planchon S., El Nemer W., Boucheix C., Rubinstein E., Chamot-Rooke J., Le Naour F.
      Proteomics 6:1437-1449(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    14. "Expression of the CUB domain containing protein 1 (CDCP1) gene in colorectal tumour cells."
      Perry S.E., Robinson P., Melcher A., Quirke P., Buehring H.-J., Cook G.P., Blair G.E.
      FEBS Lett. 581:1137-1142(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCDCP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H5V8
    Secondary accession number(s): Q49UB4
    , Q6NT71, Q6U9Y2, Q8WU91, Q96QU7, Q9H676, Q9H8C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3