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Q86YS7 - C2CD5_HUMAN

UniProt

Q86YS7 - C2CD5_HUMAN

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Protein

C2 domain-containing protein 5

Gene

C2CD5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Ca2+Note: 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 transport Source: UniProtKB
  5. positive regulation of protein targeting to membrane Source: UniProtKB
  6. positive regulation of vesicle fusion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:29062. C2CD5.

Subcellular locationi

Cytoplasmic vesicle membrane 1 Publication. Cytoplasm › cell cortex 1 Publication. Cell membrane 1 Publication. Cell projection › ruffle 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. cytoplasm Source: HPA
  3. cytoplasmic vesicle membrane Source: UniProtKB
  4. microtubule organizing center Source: HPA
  5. plasma membrane Source: UniProtKB
  6. 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 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

BgeeiQ86YS7.
CleanExiHS_KIAA0528.
ExpressionAtlasiQ86YS7. baseline and differential.
GenevestigatoriQ86YS7.

Organism-specific databases

HPAiHPA046194.

Interactioni

Protein-protein interaction databases

BioGridi115182. 12 interactions.
IntActiQ86YS7. 2 interactions.
STRINGi9606.ENSP00000334229.

Structurei

3D structure databases

ProteinModelPortaliQ86YS7.
SMRiQ86YS7. Positions 3-125.
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.
GeneTreeiENSGT00390000000212.
HOGENOMiHOG000006746.
HOVERGENiHBG081824.
InParanoidiQ86YS7.
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

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY 
       310        320        330        340        350
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF 
       360        370        380        390        400
FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK 
       410        420        430        440        450
SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL 
       460        470        480        490        500
EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID 
       510        520        530        540        550
LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM 
       560        570        580        590        600
NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK 
       610        620        630        640        650
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ 
       660        670        680        690        700
RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP 
       710        720        730        740        750
PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL 
       760        770        780        790        800
CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ 
       810        820        830        840        850
ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKAMTVEK 
       860        870        880        890        900
ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI 
       910        920        930        940        950
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM 
       960        970        980        990       1000
ENPNKNQAQC LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT
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 BAA25454.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG58665.1 differs from that shown. Reason: Frameshift at position 33. Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS66339.1. [Q86YS7-5]
CCDS66340.1. [Q86YS7-4]
PIRiT00072.
RefSeqiNP_001273102.1. NM_001286173.1. [Q86YS7-4]
NP_001273103.1. NM_001286174.1. [Q86YS7-3]
NP_001273104.1. NM_001286175.1. [Q86YS7-5]
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]
uc010sis.2. human.

Polymorphism databases

DMDMi74750574.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS66339.1. [Q86YS7-5]
CCDS66340.1. [Q86YS7-4]
PIRiT00072.
RefSeqiNP_001273102.1. NM_001286173.1. [Q86YS7-4]
NP_001273103.1. NM_001286174.1. [Q86YS7-3]
NP_001273104.1. NM_001286175.1. [Q86YS7-5]
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.

3D structure databases

ProteinModelPortaliQ86YS7.
SMRiQ86YS7. Positions 3-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115182. 12 interactions.
IntActiQ86YS7. 2 interactions.
STRINGi9606.ENSP00000334229.

PTM databases

PhosphoSiteiQ86YS7.

Polymorphism databases

DMDMi74750574.

Proteomic databases

MaxQBiQ86YS7.
PaxDbiQ86YS7.
PRIDEiQ86YS7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
uc010sis.2. human.

Organism-specific databases

CTDi9847.
GeneCardsiGC12M022602.
HGNCiHGNC:29062. C2CD5.
HPAiHPA046194.
neXtProtiNX_Q86YS7.
PharmGKBiPA143485515.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235531.
GeneTreeiENSGT00390000000212.
HOGENOMiHOG000006746.
HOVERGENiHBG081824.
InParanoidiQ86YS7.
OMAiCQPSCTG.
OrthoDBiEOG715Q38.
PhylomeDBiQ86YS7.
TreeFamiTF323431.

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

GenomeRNAii9847.
NextBioi35472401.

Gene expression databases

BgeeiQ86YS7.
CleanExiHS_KIAA0528.
ExpressionAtlasiQ86YS7. baseline and differential.
GenevestigatoriQ86YS7.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.