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Q61194 (P3C2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Short name=PI3K-C2-alpha
Short name=PtdIns-3-kinase C2 subunit alpha
EC=2.7.1.154
Alternative name(s):
Cpk-m
Phosphoinositide 3-kinase-C2-alpha
p170
Gene names
Name:Pik3c2a
Synonyms:Cpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.6 Ref.7

Catalytic activity

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

Cofactor

Calcium or magnesium. Manganese cannot be used By similarity.

Enzyme regulation

Activated by clathrin By similarity. Only slightly inhibited by wortmannin and LY294002. Activated by insulin. Ref.3 Ref.4

Subunit structure

Interacts with ERBB2 and EGFR. Interacts with clathrin trimers By similarity. Ref.8

Subcellular location

Cell membrane. Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus. Cytoplasm By similarity. Note: Has a preference for membranes containing PtdIns(4,5)P2 or PtdIns(3,4)P2.

Tissue specificity

Detected in podocytes. Ref.7

Post-translational modification

Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation By similarity. Phosphorylated upon insulin stimulation; which may lead to enzyme activation. Ref.4

Disruption phenotype

Chronic renal failure and kidney lesions. Affects podocyte morphology and function. Ref.7

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 domain.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K-RBD domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Contains 1 PX (phox homology) domain.

Sequence caution

The sequence AAB07682.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processEndocytosis
Exocytosis
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

exocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from direct assay Ref.3. Source: GOC

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phosphatidylinositol 3-kinase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from direct assay Ref.3. Source: MGI

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 binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61194-1)

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: Q61194-2)

The sequence of this isoform differs from the canonical sequence as follows:
     276-303: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 16861685Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
PRO_0000088796

Regions

Domain422 – 51089PI3K-RBD
Domain682 – 841160C2 PI3K-type
Domain861 – 1037177PIK helical
Domain1133 – 1395263PI3K/PI4K
Domain1420 – 1536117PX
Domain1557 – 1660104C2
Region2 – 142141Interaction with clathrin; sufficient to induce clathrin assemby By similarity
Region1488 – 14936Interaction with PtdIns(4,5)P2-containing membranes By similarity
Motif1606 – 161712Nuclear localization signal By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue601Phosphoserine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue3281Phosphoserine By similarity
Modified residue3391Phosphoserine By similarity

Natural variations

Alternative sequence276 – 30328Missing in isoform 2.
VSP_015254

Experimental info

Sequence conflict1401G → V in AK049609. Ref.2
Sequence conflict6681A → G in AAC52604. Ref.1
Sequence conflict9541E → G in AAC52604. Ref.1
Sequence conflict1206 – 12083FKD → LR Ref.3
Sequence conflict1211 – 12122LA → TS Ref.3
Sequence conflict12181Y → N in AAB07682. Ref.3
Sequence conflict1325 – 13262KQ → T in AAB07682. Ref.3

Secondary structure

...................... 1686
Helix Strand Turn

Details...

Sequences

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

Last modified August 30, 2005. Version 2.
Checksum: E390BA7D730F4F87

FASTA1,686190,758
        10         20         30         40         50         60 
MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD SPRGFELSSS 

        70         80         90        100        110        120 
TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL EKILLDDNFE TRKPPALPVT 

       130        140        150        160        170        180 
PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS TYTLPSTYPS AYSKQATFQN GFSPRMPTFP 

       190        200        210        220        230        240 
STESVYLRLP GQSPYFSYPL TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG 

       250        260        270        280        290        300 
KARTDLEIAN SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL 

       310        320        330        340        350        360 
LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA QGQVSQKDPN 

       370        380        390        400        410        420 
GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD HCTNPGYLLS PVTVQRNMCG 

       430        440        450        460        470        480 
ENASVKVSIE IEGLQLPVTF TCDVSSTVEI IIMQALCWVH DDLNQVDVGS YILKVCGQEE 

       490        500        510        520        530        540 
VLQNNHCLGS HEHIQNCRKW DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK 

       550        560        570        580        590        600 
PYKEVMTRHP VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA 

       610        620        630        640        650        660 
VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT AIYDLLRLHA 

       670        680        690        700        710        720 
NSSRCSTACP RGSRNIKEAW TATEQLQFTV YAAHGISSNW VSNYEKYYLI CSLSHNGKDL 

       730        740        750        760        770        780 
FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK 

       790        800        810        820        830        840 
QRKGPEALGK VSLTLFDFKR FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF 

       850        860        870        880        890        900 
PSPAFDIIYT SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY 

       910        920        930        940        950        960 
YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF ADQEVRSLAV 

       970        980        990       1000       1010       1020 
SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA LGNIQIAHSL YWLLKDALHD 

      1030       1040       1050       1060       1070       1080 
THFGSRYEHV LGALLSVGGK GLREELSKQM KLVQLLGGVA EKVRQASGST RQVVLQKSME 

      1090       1100       1110       1120       1130       1140 
RVQSFFLRNK CRLPLKPSLV AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG 

      1150       1160       1170       1180       1190       1200 
EDLRQDMLAL QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY 

      1210       1220       1230       1240       1250       1260 
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS 

      1270       1280       1290       1300       1310       1320 
TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY 

      1330       1340       1350       1360       1370       1380 
NLIRKQTNLF LNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG 

      1390       1400       1410       1420       1430       1440 
SIATKFNFFI HNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK 

      1450       1460       1470       1480       1490       1500 
HYIYVVRILR EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 

      1510       1520       1530       1540       1550       1560 
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV PFSPTLGQIG 

      1570       1580       1590       1600       1610       1620 
GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDTHKTSKR KTKISRKTRN 

      1630       1640       1650       1660       1670       1680 
PTFNEMLVYS GYSKETLRQR ELQLSVLSAE SLRENFFLGG ITLPLKDFNL SKETVKWYQL 


TAATYL 

« Hide

Isoform 2 [UniParc].

Checksum: 4D18EBC1DDC2A57D
Show »

FASTA1,658187,526

References

« Hide 'large scale' references
[1]"Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain."
Molz L., Chen Y.-W., Hirano M., Williams L.T.
J. Biol. Chem. 271:13892-13899(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356 (ISOFORM 1).
Tissue: Embryonic spinal cord.
[3]"Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain."
Virbasius J.V., Guilherme A., Czech M.P.
J. Biol. Chem. 271:13304-13307(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-1686 (ISOFORM 1), FUNCTION, ENZYME REGULATION.
Tissue: Adipocyte.
[4]"Insulin activates the alpha isoform of class II phosphoinositide 3-kinase."
Brown R.A., Domin J., Arcaro A., Waterfield M.D., Shepherd P.R.
J. Biol. Chem. 274:14529-14532(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[6]"Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion."
Leibiger B., Moede T., Uhles S., Barker C.J., Creveaux M., Domin J., Berggren P.-O., Leibiger I.B.
FASEB J. 24:1824-1837(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ISULIN SECRETION.
[7]"Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function."
Harris D.P., Vogel P., Wims M., Moberg K., Humphries J., Jhaver K.G., DaCosta C.M., Shadoan M.K., Xu N., Hansen G.M., Balakrishnan S., Domin J., Powell D.R., Oravecz T.
Mol. Cell. Biol. 31:63-80(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN KIDNEY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[8]"Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha."
Liu L., Song X., He D., Komma C., Kita A., Virbasius J.V., Huang G., Bellamy H.D., Miki K., Czech M.P., Zhou G.W.
J. Biol. Chem. 281:4254-4260(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1561-1686, INTERACTION WITH PHOSPHATIDYLINOSITIDE-CONTAINING MEMBRANES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52193 mRNA. Translation: AAC52604.1.
AK049609 mRNA. No translation available.
U55772 mRNA. Translation: AAB07682.1. Different initiation.
PIRT42642.
RefSeqNP_035213.2. NM_011083.2.
UniGeneMm.3810.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B3RX-ray2.30A/B1561-1686[»]
ProteinModelPortalQ61194.
SMRQ61194. Positions 733-1391, 1421-1532, 1561-1682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202158. 3 interactions.
IntActQ61194. 1 interaction.

PTM databases

PhosphoSiteQ61194.

Proteomic databases

PaxDbQ61194.
PRIDEQ61194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18704.
KEGGmmu:18704.

Organism-specific databases

CTD5286.
MGIMGI:1203729. Pik3c2a.

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000006920.
HOVERGENHBG082099.
KOK00923.
PhylomeDBQ61194.

Enzyme and pathway databases

BRENDA2.7.1.154. 3474.

Gene expression databases

GenevestigatorQ61194.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProIPR016024. 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.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00168. 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.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50004. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIK3C2A. mouse.
EvolutionaryTraceQ61194.
NextBio294759.
PROQ61194.
SOURCESearch...

Entry information

Entry nameP3C2A_MOUSE
AccessionPrimary (citable) accession number: Q61194
Secondary accession number(s): Q61182
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 123 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

MGD cross-references

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