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Q86YS7

- C2CD5_HUMAN

UniProt

Q86YS7 - C2CD5_HUMAN

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Protein
C2 domain-containing protein 5
Gene
C2CD5, CDP138, KIAA0528
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 affinity1 Publication
Add
BLAST
Calcium bindingi75 – 86122; high affinity1 Publication
Add
BLAST

GO - Molecular functioni

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

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

GO - Cellular componenti

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

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 5
PRO_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.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090C2
Add
BLAST

Domaini

The C2 domain binds to calcium and membrane lipids.

Sequence similaritiesi

Contains 1 C2 domain.

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.

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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei268 – 31649IPFNE…SLTPK → SPLVHPPSHGCRSTHNSPIH TATGSRLTQNFSVSVPTLIY in isoform 2, isoform 4 and isoform 5.
VSP_028255Add
BLAST
Alternative sequencei345 – 3451Q → QRGGSPHRFCRR in isoform 4.
VSP_055638
Alternative sequencei382 – 3821P → PAFVGIMGNTRSYKLLDWNS FNS in isoform 5.
VSP_055639
Alternative sequencei845 – 8451A → EHLESASSNSGIPAAQRATS VDYSSFADRCSSWIELIKLK AQTIRRGSIKTT in isoform 2, isoform 3 and isoform 4.
VSP_028256
Alternative sequencei845 – 8451A → EHLESASSNSGIPAAQRDRC SSWIELIKLKAQTIRRGSIK TT in isoform 5.
VSP_055640

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti997 – 9971E → G in BAG58665. 1 Publication
Isoform 4 (identifier: Q86YS7-4)
Sequence conflicti895 – 8951I → F in AAI43879. 1 Publication
Isoform 5 (identifier: Q86YS7-5)
Sequence conflicti895 – 8951S → P in BAG58665. 1 Publication

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.
ENST00000536386; ENSP00000439392; ENSG00000111731.
ENST00000545552; ENSP00000443204; ENSG00000111731.
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 .
ENST00000536386 ; ENSP00000439392 ; ENSG00000111731 .
ENST00000545552 ; ENSP00000443204 ; ENSG00000111731 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 95 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

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