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P42338 (PK3CB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform

Short name=PI3-kinase subunit beta
Short name=PI3K-beta
Short name=PI3Kbeta
Short name=PtdIns-3-kinase subunit beta
EC=2.7.1.153
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta
Short name=PtdIns-3-kinase subunit p110-beta
Short name=p110beta
Gene names
Name:PIK3CB
Synonyms:PIK3C1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1070 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. Ref.6 Ref.7 Ref.9 Ref.11

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.

Pathway

Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.

Subunit structure

Heterodimer of a catalytic subunit PIK3CB and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interaction with PIK3R2 is required for nuclear localization and nuclear export. Part of a complex with PIK3R1 and PTEN. Binding to PTEN may antagonize the lipid kinase activity under normal growth conditions. Part of a complex involved in autophagosome formation composed of PIK3C3 and PIK3R4 By similarity. Interacts with BECN1, ATG14 and RAB5A By similarity. Ref.8 Ref.11

Subcellular location

Cytoplasm. Nucleus. Note: Interaction with PIK3R2 is required for nuclear localization and export. Ref.11

Tissue specificity

Expressed ubiquitously.

Domain

The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1; the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1; and the PI3K/PI4K kinase domain with the cSH2 (C-terminal SH2) region of PIK3R1. The inhibitory interaction between the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1 is weak. The nuclear localization signal (NLS) is required for its function in cell survival.

Post-translational modification

Phosphorylation at Ser-1070 down-regulates lipid kinase activity.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K-ABD domain.

Contains 1 PI3K-RBD domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Ontologies

Keywords
   Biological processAutophagy
Cell adhesion
Endocytosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

G-protein coupled receptor signaling pathway

Traceable author statement Ref.12. Source: UniProtKB

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement PubMed 10570282. Source: ProtInc

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

cell migration

Traceable author statement Ref.13Ref.12. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

chemotaxis

Traceable author statement PubMed 10570282. Source: ProtInc

embryonic cleavage

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

homophilic cell adhesion

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol 3-kinase signaling

Traceable author statement Ref.12. Source: UniProtKB

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement Ref.13. Source: UniProtKB

platelet aggregation

Traceable author statement Ref.13. Source: UniProtKB

positive regulation of autophagy

Traceable author statement Ref.12. Source: UniProtKB

regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of clathrin-mediated endocytosis

Traceable author statement Ref.12. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 10570282. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement Ref.13. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phosphatidylinositol 3-kinase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

1-phosphatidylinositol-4-phosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol 3-kinase activity

Traceable author statement Ref.13. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 19380743PubMed 22402981PubMed 23397142. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10701070Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
PRO_0000088787

Regions

Domain26 – 11590PI3K-ABD
Domain194 – 28592PI3K-RBD
Domain327 – 496170C2 PI3K-type
Domain524 – 701178PIK helical
Domain800 – 1067268PI3K/PI4K
Motif410 – 4189Nuclear localization signal Ref.11

Amino acid modifications

Modified residue10701Phosphoserine; by autocatalysis Ref.5

Natural variations

Natural variant6721Q → H.
Corresponds to variant rs2230462 [ dbSNP | Ensembl ].
VAR_050530

Experimental info

Mutagenesis3421K → N: Enhanced inhibition by PIK3R1 leading to reduced lipid kinase activity and reduced oncogenicity. Does not modify regulation by GPCRs. Ref.9
Mutagenesis8051K → R: Loss of lipid kinase activity. May not affect insulin signaling and cell proliferation. Partially affects oncogene-induced trasformation. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P42338 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 81135FE93452C00E

FASTA1,070122,762
        10         20         30         40         50         60 
MCFSFIMPPA MADILDIWAV DSQIASDGSI PVDFLLPTGI YIQLEVPREA TISYIKQMLW 

        70         80         90        100        110        120 
KQVHNYPMFN LLMDIDSYMF ACVNQTAVYE ELEDETRRLC DVRPFLPVLK LVTRSCDPGE 

       130        140        150        160        170        180 
KLDSKIGVLI GKGLHEFDSL KDPEVNEFRR KMRKFSEEKI LSLVGLSWMD WLKQTYPPEH 

       190        200        210        220        230        240 
EPSIPENLED KLYGGKLIVA VHFENCQDVF SFQVSPNMNP IKVNELAIQK RLTIHGKEDE 

       250        260        270        280        290        300 
VSPYDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRALPH FILVECCKIK KMYEQEMIAI 

       310        320        330        340        350        360 
EAAINRNSSN LPLPLPPKKT RIISHVWENN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG 

       370        380        390        400        410        420 
TELLCKTIVS SEVSGKNDHI WNEPLEFDIN ICDLPRMARL CFAVYAVLDK VKTKKSTKTI 

       430        440        450        460        470        480 
NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG QLRTGDIILH SWSSFPDELE EMLNPMGTVQ 

       490        500        510        520        530        540 
TNPYTENATA LHVKFPENKK QPYYYPPFDK IIEKAAEIAS SDSANVSSRG GKKFLPVLKE 

       550        560        570        580        590        600 
ILDRDPLSQL CENEMDLIWT LRQDCREIFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK 

       610        620        630        640        650        660 
LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP FLDCALSRFL 

       670        680        690        700        710        720 
LERALGNRRI GQFLFWHLRS EVHIPAVSVQ FGVILEAYCR GSVGHMKVLS KQVEALNKLK 

       730        740        750        760        770        780 
TLNSLIKLNA VKLNRAKGKE AMHTCLKQSA YREALSDLQS PLNPCVILSE LYVEKCKYMD 

       790        800        810        820        830        840 
SKMKPLWLVY NNKVFGEDSV GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG 

       850        860        870        880        890        900 
CLATGDRSGL IEVVSTSETI ADIQLNSSNV AAAAAFNKDA LLNWLKEYNS GDDLDRAIEE 

       910        920        930        940        950        960 
FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG IKRERVPFIL 

       970        980        990       1000       1010       1020 
TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF ITLFALMLTA GLPELTSVKD 

      1030       1040       1050       1060       1070 
IQYLKDSLAL GKSEEEALKQ FKQKFDEALR ESWTTKVNWM AHTVRKDYRS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85."
Hu P., Mondino A., Skolnik E.Y., Schlessinger J.
Mol. Cell. Biol. 13:7677-7688(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Gene encoding the catalytic subunit p110beta of human phosphatidylinositol 3-kinase: cloning, genomic structure, and screening for variants in patients with type 2 diabetes."
Kossila M., Sinkovic M., Karkkainen P., Laukkanen M.O., Miettinen R., Rissanen J., Kekalainen P., Kuusisto J., Yla-Herttuala S., Laakso M.
Diabetes 49:1740-1743(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
[5]"Identification and characterization of the autophosphorylation sites of phosphoinositide 3-kinase isoforms beta and gamma."
Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K., Krause E., Nurnberg B.
J. Biol. Chem. 278:11536-11545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1070.
[6]"Essential roles of PI(3)K-p110beta in cell growth, metabolism and tumorigenesis."
Jia S., Liu Z., Zhang S., Liu P., Zhang L., Lee S.H., Zhang J., Signoretti S., Loda M., Roberts T.M., Zhao J.J.
Nature 454:776-779(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-805.
[7]"PTEN-deficient cancers depend on PIK3CB."
Wee S., Wiederschain D., Maira S.-M., Loo A., Miller C., deBeaumont R., Stegmeier F., Yao Y.-M., Lengauer C.
Proc. Natl. Acad. Sci. U.S.A. 105:13057-13062(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ONCOGENIC SIGNALING.
[8]"p85 Associates with unphosphorylated PTEN and the PTEN-associated complex."
Rabinovsky R., Pochanard P., McNear C., Brachmann S.M., Duke-Cohan J.S., Garraway L.A., Sellers W.R.
Mol. Cell. Biol. 29:5377-5388(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PIK3R1 AND PTEN.
[9]"A biochemical mechanism for the oncogenic potential of the p110beta catalytic subunit of phosphoinositide 3-kinase."
Dbouk H.A., Pang H., Fiser A., Backer J.M.
Proc. Natl. Acad. Sci. U.S.A. 107:19897-19902(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-342.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Nuclear but not cytosolic phosphoinositide 3-kinase beta has an essential function in cell survival."
Kumar A., Redondo-Munoz J., Perez-Garcia V., Cortes I., Chagoyen M., Carrera A.C.
Mol. Cell. Biol. 31:2122-2133(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PIK3R2, SUBCELLULAR LOCATION, MOTIF NUCLEAR LOCALIZATION SIGNAL.
[12]"A beta version of life: p110beta takes center stage."
Dbouk H.A., Backer J.M.
Oncotarget 1:729-733(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[13]"Regulation and roles of PI3Kbeta, a major actor in platelet signaling and functions."
Gratacap M.-P., Guillermet-Guibert J., Martin V., Chicanne G., Tronchere H., Gaits-Iacovoni F., Payrastre B.
Adv. Enzyme Regul. 51:106-116(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S67334 mRNA. Translation: AAB29081.1.
AJ297549 expand/collapse EMBL AC list , AJ297550, AJ297551, AJ297552, AJ297553, AJ297554, AJ297555, AJ297556, AJ297557, AJ297558, AJ297559, AJ297560 Genomic DNA. Translation: CAC21449.1.
CH471052 Genomic DNA. Translation: EAW79053.1.
CH471052 Genomic DNA. Translation: EAW79055.1.
BC114432 mRNA. Translation: AAI14433.1.
CCDSCCDS3104.1.
PIRA54600.
RefSeqNP_006210.1. NM_006219.2.
XP_005247587.1. XM_005247530.1.
XP_005247588.1. XM_005247531.1.
XP_006713722.1. XM_006713659.1.
UniGeneHs.239818.

3D structure databases

ProteinModelPortalP42338.
SMRP42338. Positions 123-1067.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111309. 16 interactions.
DIPDIP-44775N.
IntActP42338. 13 interactions.
MINTMINT-1505441.
STRING9606.ENSP00000289153.

Chemistry

BindingDBP42338.
ChEMBLCHEMBL3145.
GuidetoPHARMACOLOGY2154.

PTM databases

PhosphoSiteP42338.

Polymorphism databases

DMDM1171955.

Proteomic databases

MaxQBP42338.
PaxDbP42338.
PeptideAtlasP42338.
PRIDEP42338.

Protocols and materials databases

DNASU5291.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289153; ENSP00000289153; ENSG00000051382.
ENST00000477593; ENSP00000418143; ENSG00000051382.
GeneID5291.
KEGGhsa:5291.
UCSCuc011bmq.3. human.

Organism-specific databases

CTD5291.
GeneCardsGC03M138372.
HGNCHGNC:8976. PIK3CB.
HPACAB031938.
MIM602925. gene.
neXtProtNX_P42338.
PharmGKBPA33309.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000252911.
HOVERGENHBG052721.
InParanoidP42338.
KOK00922.
OMAAMHTCLK.
OrthoDBEOG70CR65.
PhylomeDBP42338.
TreeFamTF102031.

Enzyme and pathway databases

BioCycMetaCyc:HS00644-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP42338.
UniPathwayUPA00220.

Gene expression databases

ArrayExpressP42338.
BgeeP42338.
CleanExHS_PIK3CB.
GenevestigatorP42338.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF02192. PI3K_p85B. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTSM00142. PI3K_C2. 1 hit.
SM00143. PI3K_p85B. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPIK3CB.
GenomeRNAi5291.
NextBio20446.
PROP42338.
SOURCESearch...

Entry information

Entry namePK3CB_HUMAN
AccessionPrimary (citable) accession number: P42338
Secondary accession number(s): D3DNF0, Q24JU2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM