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UniProtKB - O00443 (P3C2A_HUMAN)

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Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Gene

PIK3C2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function.7 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.

Cofactori

Ca2+2 Publications, Mg2+2 PublicationsNote: Ca2+ or Mg2+. Mn2+ cannot be used.2 Publications

Enzyme regulationi

Activated by insulin (By similarity). Only slightly inhibited by wortmannin and LY294002. Activated by clathrin.By similarity3 Publications

Kineticsi

In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.
  1. KM=122 µM for PtdIns (in the absence of phosphatidylserine)1 Publication
  2. KM=64 µM for PtdIns (in the presence of phosphatidylserine)1 Publication
  3. KM=25 µM for PtdIns4P (in the presence of phosphatidylserine)1 Publication
  4. KM=15 µM for ATP (with PtdIns as substrate) (in the absence of phosphatidylserine)1 Publication
  5. KM=32 µM for ATP (with PtdIns as substrate) (in the presence of phosphatidylserine)1 Publication
  6. KM=54 µM for ATP (with PtdIns4P as substrate) (in the presence of phosphatidylserine)1 Publication
  1. Vmax=990 pmol/min/mg enzyme with PtdIns as substrate (in the absence of phosphatidylserine)1 Publication
  2. Vmax=200 pmol/min/mg enzyme with PtdIns as substrate (in the presence of phosphatidylserine)1 Publication
  3. Vmax=240 pmol/min/mg enzyme with PtdIns4P as substrate (in the presence of phosphatidylserine)1 Publication
  4. Vmax=6800 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the absence of phosphatidylserine)1 Publication
  5. Vmax=805 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the presence of phosphatidylserine)1 Publication
  6. Vmax=880 pmol/min/mg enzyme toward ATP with PtdIns4P as substrate (in the presence of phosphatidylserine)1 Publication

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: ProtInc
  • 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • phosphatidylinositol 3-kinase activity Source: UniProtKB
  • phosphatidylinositol binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  • cell migration Source: GO_Central
  • clathrin coat assembly Source: UniProtKB
  • endocytosis Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: UniProtKB
  • exocytosis Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • membrane organization Source: Reactome
  • phosphatidylinositol 3-kinase signaling Source: GO_Central
  • phosphatidylinositol biosynthetic process Source: Reactome
  • platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  • vascular smooth muscle contraction Source: UniProtKB
Complete GO annotation...

Keywordsi

Molecular functionKinase, Transferase
Biological processEndocytosis, Exocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00315-MONOMER.
BRENDAi2.7.1.154. 2681.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SABIO-RKiO00443.
SIGNORiO00443.

Chemistry databases

SwissLipidsiSLP:000000892.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (EC:2.7.1.154)
Short name:
PI3K-C2-alpha
Short name:
PtdIns-3-kinase C2 subunit alpha
Alternative name(s):
Phosphoinositide 3-kinase-C2-alpha
Gene namesi
Name:PIK3C2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8971. PIK3C2A.

Subcellular locationi

GO - Cellular componenti

  • clathrin-coated vesicle Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: HPA
  • phosphatidylinositol 3-kinase complex Source: GO_Central
  • plasma membrane Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103 – 107LLLDD → AAAAA: Reduces clathrin binding. 1 Publication5
Mutagenesisi254S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi259S → A, D or E: Abolishes phosphorylation, no change in activity. 1 Publication1
Mutagenesisi259S → A: Protects from proteolysis. 1 Publication1
Mutagenesisi262S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi266S → A: No effect on phosphorylation in vitro. 1 Publication1
Mutagenesisi1250D → A: Abolishes lipid kinase activity. Affects clathrin distribution when combined with a truncation encompassing the region of clathrin interaction. 1 Publication1
Mutagenesisi1488R → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold. 1 Publication1
Mutagenesisi1490V → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold. 1 Publication1
Mutagenesisi1491L → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 5-fold. 1 Publication1
Mutagenesisi1493R → A: Reduces affinity for PtdIns(4,5)P2-containing membranes 23-fold. 1 Publication1
Mutagenesisi1503R → A: Abolishes interaction with PtdIns(4,5)P2-containing membranes. 1 Publication1

Organism-specific databases

DisGeNETi5286.
OpenTargetsiENSG00000011405.
PharmGKBiPA33304.

Chemistry databases

ChEMBLiCHEMBL1075102.
GuidetoPHARMACOLOGYi2150.

Polymorphism and mutation databases

BioMutaiPIK3C2A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000887952 – 1686Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaAdd BLAST1685

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei108PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1 Publication1
Modified residuei327PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei1281PhosphoserineCombined sources1
Modified residuei1553PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity). Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the physiological state of the cell.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei244Not phosphorylated1 Publication1
Sitei249Not phosphorylated1 Publication1
Sitei251Not phosphorylated1 Publication1
Sitei254Not phosphorylated1 Publication1
Sitei262Not phosphorylated1 Publication1
Sitei266Not phosphorylated1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO00443.
MaxQBiO00443.
PaxDbiO00443.
PeptideAtlasiO00443.
PRIDEiO00443.

PTM databases

iPTMnetiO00443.
PhosphoSitePlusiO00443.

Expressioni

Tissue specificityi

Expressed in columnar and transitional epithelia, mononuclear cells, smooth muscle cells, and endothelial cells lining capillaries and small venules (at protein level). Ubiquitously expressed, with highest levels in heart, placenta and ovary, and lowest levels in the kidney. Detected at low levels in islets of Langerhans from type 2 diabetes mellitus individuals.3 Publications

Gene expression databases

BgeeiENSG00000011405.
CleanExiHS_PIK3C2A.
ExpressionAtlasiO00443. baseline and differential.
GenevisibleiO00443. HS.

Organism-specific databases

HPAiHPA037641.
HPA037642.

Interactioni

Subunit structurei

Part of a complex with ERBB2 and EGFR. Interacts with clathrin trimers.3 Publications

Protein-protein interaction databases

BioGridi111304. 62 interactors.
DIPiDIP-33727N.
IntActiO00443. 43 interactors.
MINTiMINT-2794824.
STRINGi9606.ENSP00000265970.

Chemistry databases

BindingDBiO00443.

Structurei

Secondary structure

11686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1418 – 1421Combined sources4
Beta strandi1422 – 1433Combined sources12
Beta strandi1437 – 1440Combined sources4
Beta strandi1443 – 1450Combined sources8
Beta strandi1457 – 1462Combined sources6
Helixi1463 – 1476Combined sources14
Helixi1479 – 1481Combined sources3
Beta strandi1491 – 1495Combined sources5
Helixi1498 – 1515Combined sources18
Helixi1519 – 1522Combined sources4
Helixi1525 – 1530Combined sources6
Turni1535 – 1537Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AR5X-ray1.80A1421-1532[»]
2IWLX-ray2.60X1405-1544[»]
2REAX-ray2.50A1421-1532[»]
2REDX-ray2.10A1421-1532[»]
ProteinModelPortaliO00443.
SMRiO00443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini421 – 509PI3K-RBDPROSITE-ProRule annotationAdd BLAST89
Domaini682 – 841C2 PI3K-typePROSITE-ProRule annotationAdd BLAST160
Domaini861 – 1037PIK helicalPROSITE-ProRule annotationAdd BLAST177
Domaini1133 – 1397PI3K/PI4KPROSITE-ProRule annotationAdd BLAST265
Domaini1422 – 1538PXPROSITE-ProRule annotationAdd BLAST117
Domaini1559 – 1662C2PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 142Interaction with clathrin; sufficient to induce clathrin assembyAdd BLAST141
Regioni1488 – 1493Interaction with PtdIns(4,5)P2-containing membranes6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1608 – 1619Nuclear localization signal1 PublicationAdd BLAST12

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0905. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000006920.
HOVERGENiHBG082099.
InParanoidiO00443.
KOiK00923.
OMAiTIQRGQW.
OrthoDBiEOG091G00FC.
PhylomeDBiO00443.
TreeFamiTF102031.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProiView protein in InterPro
IPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiView protein in Pfam
PF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
SMARTiView protein in SMART
SM00239. C2. 2 hits.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiView protein in PROSITE
PS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00443-1) [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
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD 
        60         70         80         90        100
NQRGFELSSS TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL 
       110        120        130        140        150
EKLLLDDSFE TKKTPVLPVT PILSPSFSAQ LYFRPTIQRG QWPPGLPGPS 
       160        170        180        190        200
TYALPSIYPS TYSKQAAFQN GFNPRMPTFP STEPIYLSLP GQSPYFSYPL 
       210        220        230        240        250
TPATPFHPQG SLPIYRPVVS TDMAKLFDKI ASTSEFLKNG KARTDLEITD 
       260        270        280        290        300
SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA 
       310        320        330        340        350
KDPWDAVLLE ERSTANCHLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ 
       360        370        380        390        400
GHISQKDPNG TSSLPTGSSL LQEVEVQNEE MAAFCRSITK LKTKFPYTNH 
       410        420        430        440        450
RTNPGYLLSP VTAQRNICGE NASVKVSIDI EGFQLPVTFT CDVSSTVEII 
       460        470        480        490        500
IMQALCWVHD DLNQVDVGSY VLKVCGQEEV LQNNHCLGSH EHIQNCRKWD 
       510        520        530        540        550
TEIRLQLLTF SAMCQNLART AEDDETPVDL NKHLYQIEKP CKEAMTRHPV 
       560        570        580        590        600
EELLDSYHNQ VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV 
       610        620        630        640        650
KKLKRAVNLP RSKTADVTSL FGGEDTSRSS TRGSLNPENP VQVSINQLTA 
       660        670        680        690        700
AIYDLLRLHA NSGRSPTDCA QSSKSVKEAW TTTEQLQFTI FAAHGISSNW 
       710        720        730        740        750
VSNYEKYYLI CSLSHNGKDL FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ 
       760        770        780        790        800
ISQLPLESVL HLTLFGILNQ SSGSSPDSNK QRKGPEALGK VSLPLFDFKR 
       810        820        830        840        850
FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDF PSPAFDIIYT 
       860        870        880        890        900
TPQVDRSIIQ QHNLETLEND IKGKLLDILH KDSSLGLSKE DKAFLWEKRY 
       910        920        930        940        950
YCFKHPNCLP KILASAPNWK WVNLAKTYSL LHQWPALYPL IALELLDSKF 
       960        970        980        990       1000
ADQEVRSLAV TWIEAISDDE LTDLLPQFVQ ALKYEIYLNS SLVQFLLSRA 
      1010       1020       1030       1040       1050
LGNIQIAHNL YWLLKDALHD VQFSTRYEHV LGALLSVGGK RLREELLKQT 
      1060       1070       1080       1090       1100
KLVQLLGGVA EKVRQASGSA RQVVLQRSME RVQSFFQKNK CRLPLKPSLV 
      1110       1120       1130       1140       1150
AKELNIKSCS FFSSNAVPLK VTMVNADPMG EEINVMFKVG EDLRQDMLAL 
      1160       1170       1180       1190       1200
QMIKIMDKIW LKEGLDLRMV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY 
      1210       1220       1230       1240       1250
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD 
      1260       1270       1280       1290       1300
RHNDNIMLRS TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN 
      1310       1320       1330       1340       1350
GGEKPTIRFQ LFVDLCCQAY NLIRKQTNLF LNLLSLMIPS GLPELTSIQD 
      1360       1370       1380       1390       1400
LKYVRDALQP QTTDAEATIF FTRLIESSLG SIATKFNFFI HNLAQLRFSG 
      1410       1420       1430       1440       1450
LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK HYIYVVRILR 
      1460       1470       1480       1490       1500
EGQIEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 
      1510       1520       1530       1540       1550
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSADAG 
      1560       1570       1580       1590       1600
SFSPTPGQIG GAVKLSISYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL 
      1610       1620       1630       1640       1650
LPDNHKTSKR KTKISRKTRN PTFNEMLVYS GYSKETLRQR ELQLSVLSAE 
      1660       1670       1680 
SLRENFFLGG VTLPLKDFNL SKETVKWYQL TAATYL
Length:1,686
Mass (Da):190,680
Last modified:July 10, 2007 - v2
Checksum:i904AA5470F80DAC6
GO
Isoform 2 (identifier: O00443-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     484-1686: Missing.

Note: No experimental confirmation available.
Show »
Length:483
Mass (Da):53,742
Checksum:iB63EDBEA18725E91
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5S → F in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti15S → F in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti483N → K in BAG65126 (PubMed:14702039).Curated1
Sequence conflicti796F → C in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti799K → R in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti922V → G in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1129M → L in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1450R → W in CAA73797 (PubMed:9337861).Curated1
Sequence conflicti1464D → V in CAA73797 (PubMed:9337861).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0233331415T → A. Corresponds to variant dbSNP:rs11604561Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056158484 – 1686Missing in isoform 2. 1 PublicationAdd BLAST1203

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13367 mRNA. Translation: CAA73797.1.
AK304262 mRNA. Translation: BAG65126.1.
EU332862 Genomic DNA. Translation: ABY87551.1.
AC107956 Genomic DNA. No translation available.
AC116533 Genomic DNA. No translation available.
AC126389 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68447.1.
BC113658 mRNA. Translation: AAI13659.1.
CCDSiCCDS7824.1. [O00443-1]
PIRiPC4345.
RefSeqiNP_001308307.1. NM_001321378.1. [O00443-1]
NP_002636.2. NM_002645.3. [O00443-1]
XP_016873413.1. XM_017017924.1. [O00443-1]
UniGeneiHs.175343.
Hs.736397.

Genome annotation databases

EnsembliENST00000265970; ENSP00000265970; ENSG00000011405. [O00443-1]
GeneIDi5286.
KEGGihsa:5286.
UCSCiuc001mmq.6. human. [O00443-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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 one 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.

Entry informationi

Entry nameiP3C2A_HUMAN
AccessioniPrimary (citable) accession number: O00443
Secondary accession number(s): B0LPH2, B4E2G4, Q14CQ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 10, 2007
Last modified: July 5, 2017
This is version 161 of the entry and version 2 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families