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O35904 (PK3CD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=PI3-kinase subunit delta
Short name=PI3K-delta
Short name=PI3Kdelta
Short name=PtdIns-3-kinase subunit delta
EC=2.7.1.153
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
Short name=PtdIns-3-kinase subunit p110-delta
Short name=p110delta
Gene names
Name:Pik3cd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1043 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(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. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

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

Enzyme regulation

Activated by growth factors and cytokine receptors through a tyrosine-kinase-dependent mechanism. Activated by RAS. IC87114 inhibits lipid kinase activity and is selective in cells at doses up to 5-10 µM. Among other effects, IC87114 reduces allergic responses, prevents the recruitment of antigen-specific T cells into target tissue, and affects natural killer cell chemotaxis. Ref.7 Ref.9 Ref.11

Pathway

Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.

Subunit structure

Heterodimer of a catalytic subunit PIK3CD and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with ERAS and HRAS. Ref.6

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Isoform 1 is expressed in spleen and lung (at protein level). Isoform 1 is expressed predominantly in leukocytes. Ref.12

Post-translational modification

Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity By similarity.

Disruption phenotype

Null mutants are viable and fertile but display defective adaptive and innate immune responses due to signaling defects in multiple cell types including B-, T- and mast and natural killer cells. Ref.2 Ref.5 Ref.7 Ref.9 Ref.10

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 processAdaptive immunity
Chemotaxis
Differentiation
Immunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from mutant phenotype Ref.5. Source: MGI

B cell homeostasis

Inferred from mutant phenotype Ref.5. Source: MGI

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface receptor signaling pathway

Inferred from mutant phenotype Ref.5. Source: MGI

chemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from Biological aspect of Ancestor. Source: GOC

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

   Cellular_componentphosphatidylinositol 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-4,5-bisphosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pik3r1P264502EBI-6470774,EBI-641764

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35904-1)

Also known as: p110-delta;

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.
Isoform 2 (identifier: O35904-2)

The sequence of this isoform differs from the canonical sequence as follows:
     201-212: ESFTFQVSTKDM → VSPSPIPSPSSI
     213-1043: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10431043Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
PRO_0000088791

Regions

Domain16 – 10590PI3K-ABD
Domain187 – 27892PI3K-RBD
Domain319 – 476158C2 PI3K-type
Domain496 – 673178PIK helical
Domain775 – 1028254PI3K/PI4K

Amino acid modifications

Modified residue5231Phosphotyrosine By similarity
Modified residue10381Phosphoserine; by autocatalysis By similarity

Natural variations

Alternative sequence201 – 21212ESFTF…STKDM → VSPSPIPSPSSI in isoform 2.
VSP_044411
Alternative sequence213 – 1043831Missing in isoform 2.
VSP_044412

Experimental info

Mutagenesis9101D → A: Inhibits lipid kinase activity. Mice are viable and fertile but display defective adaptive and innate immune responses Signaling defects in B-cells, T-cells, mast cells and natural killer cells. Reduced B and T-cell receptor signaling. Affects development and differentiation of B -ells. Reduced memory T-cell number. Affects B- and T-cell proliferation. Attenuates immune responses in vivo. Induces inflammatory bowel disease development. Lost TCR-induced migration and localization to antigenic tissue. Affects natural killer cell maturation and cytokine production. Ref.2 Ref.7 Ref.9 Ref.10
Sequence conflict1221G → A in AAC25676. Ref.1
Sequence conflict5841F → S in AAC25676. Ref.1
Sequence conflict6511R → H in AAC25676. Ref.1

Secondary structure

......................................................................................................................................... 1043
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p110-delta) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AD8DE07D8F847795

FASTA1,043119,712
        10         20         30         40         50         60 
MPPGVDCPME FWTKEESQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQVLW HRAQYEPLFH 

        70         80         90        100        110        120 
MLSDPEAYVF TCVNQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KLINSQISLL 

       130        140        150        160        170        180 
IGKGLHEFDS LRDPEVNDFR TKMRQFCEEA AAHRQQLGWV EWLQYSFPLQ LEPSARGWRA 

       190        200        210        220        230        240 
GLLRVSNRAL LVNVKFEGSE ESFTFQVSTK DMPLALMACA LRKKATVFRQ PLVEQPEEYA 

       250        260        270        280        290        300 
LQVNGRHEYL YGNYPLCHFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR 

       310        320        330        340        350        360 
AKPPPIPAKK PSSVSLWSLE QPFSIELIEG RKVNADERMK LVVQAGLFHG NEMLCKTVSS 

       370        380        390        400        410        420 
SEVNVCSEPV WKQRLEFDIS VCDLPRMARL CFALYAVVEK AKKARSTKKK SKKADCPIAW 

       430        440        450        460        470        480 
ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPAGTVR GNPNTESAAA LVIYLPEVAP 

       490        500        510        520        530        540 
HPVYFPALEK ILELGRHGER GRITEEELQL REILERRGSG ELYEHEKDLV WKMRHEVQEH 

       550        560        570        580        590        600 
FPEALARLLL VTKWNKHEDV AQMLYLLCSW PELPVLSALE LLDFSFPDCY VGSFAIKSLR 

       610        620        630        640        650        660 
KLTDDELFQY LLQLVQVLKY ESYLDCELTK FLLGRALANR KIGHFLFWHL RSEMHVPSVA 

       670        680        690        700        710        720 
LRFGLIMEAY CRGSTHHMKV LMKQGEALSK LKALNDFVKV SSQKTTKPQT KEMMHMCMRQ 

       730        740        750        760        770        780 
ETYMEALSHL QSPLDPSTLL EEVCVEQCTF MDSKMKPLWI MYSSEEAGSA GNVGIIFKNG 

       790        800        810        820        830        840 
DDLRQDMLTL QMIQLMDVLW KQEGLDLRMT PYGCLPTGDR TGLIEVVLHS DTIANIQLNK 

       850        860        870        880        890        900 
SNMAATAAFN KDALLNWLKS KNPGEALDRA IEEFTLSCAG YCVATYVLGI GDRHSDNIMI 

       910        920        930        940        950        960 
RESGQLFHID FGHFLGNFKT KFGINRERVP FILTYDFVHV IQQGKTNNSE KFERFRGYCE 

       970        980        990       1000       1010       1020 
RAYTILRRHG LLFLHLFALM RAAGLPELSC SKDIQYLKDS LALGKTEEEA LKHFRVKFNE 

      1030       1040 
ALRESWKTKV NWLAHNVSKD NRQ 

« Hide

Isoform 2 [UniParc].

Checksum: F61391FD8427F323
Show »

FASTA21224,355

References

« Hide 'large scale' references
[1]"p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes."
Chantry D., Vojtek A., Kashishian A., Holtzman D.A., Wood C., Gray P.W., Cooper J.A., Hoekstra M.F.
J. Biol. Chem. 272:19236-19241(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Spleen.
[2]"Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice."
Okkenhaug K., Bilancio A., Farjot G., Priddle H., Sancho S., Peskett E., Pearce W., Meek S.E., Salpekar A., Waterfield M.D., Smith A.J., Vanhaesebroeck B.
Science 297:1031-1034(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
Strain: 129P2.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A crucial role for the p110delta subunit of phosphatidylinositol 3-kinase in B cell development and activation."
Clayton E., Bardi G., Bell S.E., Chantry D., Downes C.P., Gray A., Humphries L.A., Rawlings D., Reynolds H., Vigorito E., Turner M.
J. Exp. Med. 196:753-763(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN B-CELLS, DISRUPTION PHENOTYPE.
[6]"Role of Eras in promoting tumor-like properties in mouse embryonic stem cells."
Takahashi K., Mitsui K., Yamanaka S.
Nature 423:541-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERAS.
[7]"Essential role for the p110delta phosphoinositide 3-kinase in the allergic response."
Ali K., Bilancio A., Thomas M., Pearce W., Gilfillan A.M., Tkaczyk C., Kuehn N., Gray A., Giddings J., Peskett E., Fox R., Bruce I., Walker C., Sawyer C., Okkenhaug K., Finan P., Vanhaesebroeck B.
Nature 431:1007-1011(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAST CELLS, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
[8]"T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase."
Webb L.M.C., Vigorito E., Wymann M.P., Hirsch E., Turner M.
J. Immunol. 175:2783-2787(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T-CELL DEVELOPMENT.
[9]"T cell receptor-induced phosphoinositide-3-kinase p110delta activity is required for T cell localization to antigenic tissue in mice."
Jarmin S.J., David R., Ma L., Chai J.-G., Dewchand H., Takesono A., Ridley A.J., Okkenhaug K., Marelli-Berg F.M.
J. Clin. Invest. 118:1154-1164(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T-CELL MIGRATION, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
[10]"The p110 delta of PI3K plays a critical role in NK cell terminal maturation and cytokine/chemokine generation."
Guo H., Samarakoon A., Vanhaesebroeck B., Malarkannan S.
J. Exp. Med. 205:2419-2435(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NATURAL KILLER CELLS, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-910.
[11]"p110gamma and p110delta isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease."
Saudemont A., Garcon F., Yadi H., Roche-Molina M., Kim N., Segonds-Pichon A., Martin-Fontecha A., Okkenhaug K., Colucci F.
Proc. Natl. Acad. Sci. U.S.A. 106:5795-5800(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NATURAL KILLER CELL MIGRATION, ENZYME REGULATION.
[12]"p37delta is a new isoform of PI3K p110delta that increases cell proliferation and is overexpressed in tumors."
Fransson S., Uv A., Eriksson H., Andersson M.K., Wettergren Y., Bergo M., Ejeskar K.
Oncogene 31:3277-3286(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Peripheral blood leukocyte.
[13]"The p110 delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors."
Berndt A., Miller S., Williams O., Le D.D., Houseman B.T., Pacold J.I., Gorrec F., Hon W.-C., Liu Y., Rommel C., Gaillard P., Ruckle T., Schwarz M.K., Shokat K.M., Shaw J.P., Williams R.L.
Nat. Chem. Biol. 6:117-124(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 106-1043 IN A COMPLEX WITH IC87114; PIK-39; SW13; SW14; SW30; DL06; DL07; ZSTK474; AS5; GDC-0941; INK654; INK666 AND AS15.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86587 mRNA. Translation: AAC25676.1.
AF532989 Genomic DNA. Translation: AAN05615.1.
AL607078 Genomic DNA. Translation: CAM23914.1.
CU207384 Genomic DNA. Translation: CAQ51667.1.
CH466594 Genomic DNA. Translation: EDL14872.1.
PIRT43502.
RefSeqNP_001157524.1. NM_001164052.1.
XP_006536078.1. XM_006536015.1.
XP_006538715.1. XM_006538652.1.
UniGeneMm.229108.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WXFX-ray1.90A106-1043[»]
2WXGX-ray2.00A106-1043[»]
2WXHX-ray1.90A106-1043[»]
2WXIX-ray2.80A106-1043[»]
2WXJX-ray2.60A106-1043[»]
2WXKX-ray2.90A106-1043[»]
2WXLX-ray1.99A106-1043[»]
2WXMX-ray2.80A106-1043[»]
2WXNX-ray2.60A106-1043[»]
2WXOX-ray2.49A106-1043[»]
2WXPX-ray2.30A106-1043[»]
2WXQX-ray2.70A106-1043[»]
2WXRX-ray2.50A106-1043[»]
2X38X-ray2.20A106-1043[»]
4AJWX-ray2.80A/B110-1043[»]
ProteinModelPortalO35904.
SMRO35904. Positions 20-102, 109-1026.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202161. 2 interactions.
DIPDIP-39841N.
IntActO35904. 6 interactions.

Chemistry

ChEMBLCHEMBL2216745.

PTM databases

PhosphoSiteO35904.

Proteomic databases

PaxDbO35904.
PRIDEO35904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105689; ENSMUSP00000101314; ENSMUSG00000039936. [O35904-1]
GeneID18707.
KEGGmmu:18707.
UCSCuc008vwq.1. mouse. [O35904-1]

Organism-specific databases

CTD5293.
MGIMGI:1098211. Pik3cd.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00620000087742.
HOGENOMHOG000252911.
HOVERGENHBG052721.
KOK00922.

Enzyme and pathway databases

BRENDA2.7.1.153. 3474.
UniPathwayUPA00220.

Gene expression databases

ArrayExpressO35904.
BgeeO35904.
GenevestigatorO35904.

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.
[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.
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

ChiTaRSPIK3CD. mouse.
EvolutionaryTraceO35904.
NextBio294773.
PROO35904.
SOURCESearch...

Entry information

Entry namePK3CD_MOUSE
AccessionPrimary (citable) accession number: O35904
Secondary accession number(s): Q8CJ28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot