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Q86YS7

- C2CD5_HUMAN

UniProt

Q86YS7 - C2CD5_HUMAN

Protein

C2 domain-containing protein 5

Gene

C2CD5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM.1 Publication

    Cofactori

    Binds 2 calcium ions per subunit. The ions are bound to the C2 domains.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi13 – 27151; low affinityAdd
    BLAST
    Calcium bindingi75 – 86122; high affinityAdd
    BLAST

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to insulin stimulus Source: UniProtKB
    2. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
    3. intracellular protein transmembrane transport Source: UniProtKB
    4. positive regulation of glucose import in response to insulin stimulus Source: Ensembl
    5. positive regulation of glucose transport Source: UniProtKB
    6. positive regulation of protein targeting to membrane Source: UniProtKB
    7. positive regulation of vesicle fusion Source: UniProtKB
    8. protein localization to plasma membrane Source: Ensembl
    9. vesicle fusion Source: Ensembl

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Calcium, Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C2 domain-containing protein 5
    Alternative name(s):
    C2 domain-containing phosphoprotein of 138 kDa
    Gene namesi
    Name:C2CD5
    Synonyms:CDP138, KIAA0528
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29062. C2CD5.

    Subcellular locationi

    Cytoplasmic vesicle membrane 1 Publication. Cytoplasmcell cortex 1 Publication. Cell membrane 1 Publication. Cell projectionruffle 1 Publication
    Note: Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cytoplasmic vesicle membrane Source: UniProtKB
    3. plasma membrane Source: UniProtKB
    4. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-26; A-76; A-78 and A-84. 1 Publication
    Mutagenesisi26 – 261D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-76; A-78 and A-84. 1 Publication
    Mutagenesisi76 – 761D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-78 and A-84. 1 Publication
    Mutagenesisi78 – 781D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-84. 1 Publication
    Mutagenesisi84 – 841D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-78. 1 Publication
    Mutagenesisi197 – 1971S → A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion. 1 Publication
    Mutagenesisi200 – 2001S → A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485515.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10001000C2 domain-containing protein 5PRO_0000247450Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei197 – 1971Phosphoserine; by PKB/AKT21 Publication
    Modified residuei200 – 2001Phosphoserine1 Publication
    Modified residuei293 – 2931Phosphoserine1 Publication
    Modified residuei295 – 2951Phosphoserine2 Publications
    Modified residuei317 – 3171Phosphothreonine1 Publication
    Modified residuei601 – 6011Phosphothreonine1 Publication
    Modified residuei643 – 6431Phosphoserine5 Publications
    Modified residuei659 – 6591Phosphoserine2 Publications
    Modified residuei852 – 8521Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma membrane.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86YS7.
    PaxDbiQ86YS7.
    PRIDEiQ86YS7.

    PTM databases

    PhosphoSiteiQ86YS7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ86YS7.
    BgeeiQ86YS7.
    CleanExiHS_KIAA0528.
    GenevestigatoriQ86YS7.

    Organism-specific databases

    HPAiHPA046194.

    Interactioni

    Protein-protein interaction databases

    BioGridi115182. 6 interactions.
    IntActiQ86YS7. 2 interactions.
    STRINGi9606.ENSP00000334229.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86YS7.
    SMRiQ86YS7. Positions 3-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9090C2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C2 domain binds to calcium and membrane lipids.

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG235531.
    HOGENOMiHOG000006746.
    HOVERGENiHBG081824.
    OMAiCQPSCTG.
    OrthoDBiEOG715Q38.
    PhylomeDBiQ86YS7.
    TreeFamiTF323431.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86YS7-1) [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

    MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ     50
    WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 100
    AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 150
    SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 200
    GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 250
    PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY 300
    SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF 350
    FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK 400
    SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL 450
    EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID 500
    LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM 550
    NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK 600
    TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ 650
    RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP 700
    PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL 750
    CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ 800
    ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKAMTVEK 850
    ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI 900
    RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM 950
    ENPNKNQAQC LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT 1000
    Length:1,000
    Mass (Da):110,447
    Last modified:June 1, 2003 - v1
    Checksum:i7C51961F54CBBACD
    GO
    Isoform 2 (identifier: Q86YS7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
         845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

    Note: No experimental confirmation available.

    Show »
    Length:1,042
    Mass (Da):114,994
    Checksum:i23C91754C1A61236
    GO
    Isoform 3 (identifier: Q86YS7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

    Note: No experimental confirmation available.

    Show »
    Length:1,051
    Mass (Da):116,027
    Checksum:i2C4D059D41F01BE8
    GO
    Isoform 4 (identifier: Q86YS7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
         345-345: Q → QRGGSPHRFCRR
         845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,053
    Mass (Da):116,305
    Checksum:iF27416DC231838AA
    GO
    Isoform 5 (identifier: Q86YS7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
         382-382: P → PAFVGIMGNTRSYKLLDWNSFNS
         845-845: A → EHLESASSNSGIPAAQRDRCSSWIELIKLKAQTIRRGSIKTT

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,054
    Mass (Da):116,468
    Checksum:i2514DE8DDDBDB3A7
    GO

    Sequence cautioni

    The sequence BAG58665.1 differs from that shown. Reason: Frameshift at position 33.
    The sequence BAA25454.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti997 – 9971E → G in BAG58665. (PubMed:14702039)Curated
    Isoform 4 (identifier: Q86YS7-4)
    Sequence conflicti895 – 8951I → F in AAI43879. (PubMed:15489334)Curated
    Isoform 5 (identifier: Q86YS7-5)
    Sequence conflicti895 – 8951S → P in BAG58665. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei268 – 31649IPFNE…SLTPK → SPLVHPPSHGCRSTHNSPIH TATGSRLTQNFSVSVPTLIY in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_028255Add
    BLAST
    Alternative sequencei345 – 3451Q → QRGGSPHRFCRR in isoform 4. 1 PublicationVSP_055638
    Alternative sequencei382 – 3821P → PAFVGIMGNTRSYKLLDWNS FNS in isoform 5. 1 PublicationVSP_055639
    Alternative sequencei845 – 8451A → EHLESASSNSGIPAAQRATS VDYSSFADRCSSWIELIKLK AQTIRRGSIKTT in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_028256
    Alternative sequencei845 – 8451A → EHLESASSNSGIPAAQRDRC SSWIELIKLKAQTIRRGSIK TT in isoform 5. 1 PublicationVSP_055640

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011100 mRNA. Translation: BAA25454.3. Different initiation.
    AY166851 mRNA. Translation: AAO17290.1.
    AK295862 mRNA. Translation: BAG58665.1. Frameshift.
    AK299353 mRNA. Translation: BAG61349.1.
    AC053513 Genomic DNA. No translation available.
    BC042498 mRNA. Translation: AAH42498.2.
    BC053885 mRNA. Translation: AAH53885.1.
    BC117143 mRNA. Translation: AAI17144.1.
    BC143878 mRNA. Translation: AAI43879.1.
    CCDSiCCDS31758.1. [Q86YS7-1]
    CCDS66337.1. [Q86YS7-3]
    CCDS66338.1. [Q86YS7-2]
    PIRiT00072.
    RefSeqiNP_001273102.1. NM_001286173.1.
    NP_001273103.1. NM_001286174.1. [Q86YS7-3]
    NP_001273104.1. NM_001286175.1.
    NP_001273105.1. NM_001286176.1. [Q86YS7-3]
    NP_001273106.1. NM_001286177.1. [Q86YS7-2]
    NP_055617.1. NM_014802.2. [Q86YS7-1]
    UniGeneiHs.271014.

    Genome annotation databases

    EnsembliENST00000333957; ENSP00000334229; ENSG00000111731. [Q86YS7-1]
    ENST00000396028; ENSP00000379345; ENSG00000111731. [Q86YS7-2]
    ENST00000446597; ENSP00000388756; ENSG00000111731. [Q86YS7-3]
    ENST00000536386; ENSP00000439392; ENSG00000111731. [Q86YS7-4]
    ENST00000542676; ENSP00000441951; ENSG00000111731. [Q86YS7-3]
    ENST00000545552; ENSP00000443204; ENSG00000111731. [Q86YS7-5]
    GeneIDi9847.
    KEGGihsa:9847.
    UCSCiuc001rfq.3. human. [Q86YS7-1]
    uc001rfr.3. human. [Q86YS7-2]

    Polymorphism databases

    DMDMi74750574.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011100 mRNA. Translation: BAA25454.3 . Different initiation.
    AY166851 mRNA. Translation: AAO17290.1 .
    AK295862 mRNA. Translation: BAG58665.1 . Frameshift.
    AK299353 mRNA. Translation: BAG61349.1 .
    AC053513 Genomic DNA. No translation available.
    BC042498 mRNA. Translation: AAH42498.2 .
    BC053885 mRNA. Translation: AAH53885.1 .
    BC117143 mRNA. Translation: AAI17144.1 .
    BC143878 mRNA. Translation: AAI43879.1 .
    CCDSi CCDS31758.1. [Q86YS7-1 ]
    CCDS66337.1. [Q86YS7-3 ]
    CCDS66338.1. [Q86YS7-2 ]
    PIRi T00072.
    RefSeqi NP_001273102.1. NM_001286173.1.
    NP_001273103.1. NM_001286174.1. [Q86YS7-3 ]
    NP_001273104.1. NM_001286175.1.
    NP_001273105.1. NM_001286176.1. [Q86YS7-3 ]
    NP_001273106.1. NM_001286177.1. [Q86YS7-2 ]
    NP_055617.1. NM_014802.2. [Q86YS7-1 ]
    UniGenei Hs.271014.

    3D structure databases

    ProteinModelPortali Q86YS7.
    SMRi Q86YS7. Positions 3-128.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115182. 6 interactions.
    IntActi Q86YS7. 2 interactions.
    STRINGi 9606.ENSP00000334229.

    PTM databases

    PhosphoSitei Q86YS7.

    Polymorphism databases

    DMDMi 74750574.

    Proteomic databases

    MaxQBi Q86YS7.
    PaxDbi Q86YS7.
    PRIDEi Q86YS7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333957 ; ENSP00000334229 ; ENSG00000111731 . [Q86YS7-1 ]
    ENST00000396028 ; ENSP00000379345 ; ENSG00000111731 . [Q86YS7-2 ]
    ENST00000446597 ; ENSP00000388756 ; ENSG00000111731 . [Q86YS7-3 ]
    ENST00000536386 ; ENSP00000439392 ; ENSG00000111731 . [Q86YS7-4 ]
    ENST00000542676 ; ENSP00000441951 ; ENSG00000111731 . [Q86YS7-3 ]
    ENST00000545552 ; ENSP00000443204 ; ENSG00000111731 . [Q86YS7-5 ]
    GeneIDi 9847.
    KEGGi hsa:9847.
    UCSCi uc001rfq.3. human. [Q86YS7-1 ]
    uc001rfr.3. human. [Q86YS7-2 ]

    Organism-specific databases

    CTDi 9847.
    GeneCardsi GC12M022602.
    HGNCi HGNC:29062. C2CD5.
    HPAi HPA046194.
    neXtProti NX_Q86YS7.
    PharmGKBi PA143485515.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235531.
    HOGENOMi HOG000006746.
    HOVERGENi HBG081824.
    OMAi CQPSCTG.
    OrthoDBi EOG715Q38.
    PhylomeDBi Q86YS7.
    TreeFami TF323431.

    Miscellaneous databases

    GenomeRNAii 9847.
    NextBioi 35474430.

    Gene expression databases

    ArrayExpressi Q86YS7.
    Bgeei Q86YS7.
    CleanExi HS_KIAA0528.
    Genevestigatori Q86YS7.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Ohara O., Nagase T., Ishikawa K.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Guo J.H., Yu L.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "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 3 AND 5).
      Tissue: Hippocampus.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      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; 2 AND 4).
      Tissue: Brain, Cerebellum and Lung carcinoma.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-643 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643; SER-659 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-643 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-643 AND SER-659, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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 SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
      Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
      Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "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-293; SER-295 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiC2CD5_HUMAN
    AccessioniPrimary (citable) accession number: Q86YS7
    Secondary accession number(s): B4DJ03
    , B4DRN7, B7ZLL0, F5H2A1, F5H5R1, O60280, Q17RY7, Q7Z619, Q86SU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 96 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3