CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023660
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-phosphatidylinositol 3-phosphate 5-kinase 
Protein Synonyms/Alias
 Phosphatidylinositol 3-phosphate 5-kinase; FYVE finger-containing phosphoinositide kinase; PIKfyve; Phosphatidylinositol 3-phosphate 5-kinase type III; PIPkin-III; Type III PIP kinase 
Gene Name
 PIKFYVE 
Gene Synonyms/Alias
 KIAA0981; PIP5K3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
356LLDSVQLKDLWKKICubiquitination[1]
736LQEREFLKNYVQRIVubiquitination[1]
754PTLVLVEKTVSRIAQubiquitination[1]
938ELRIVFEKGEQENKNubiquitination[1]
1165RGGRIQPKNSDPFAHubiquitination[1]
1206SDAVWSTKVDCLNPIubiquitination[1]
1414VSLLQDLKDFFQKVSubiquitination[1]
1435DERLASLKTDTFSKTubiquitination[1]
1493VFESLIAKKQSLCEVubiquitination[1]
1494FESLIAKKQSLCEVLubiquitination[1]
1516QDLFQQEKGRKRPSVubiquitination[1, 2]
1801VDGGDTQKKQLINPHubiquitination[3]
1832YYAGEFHKMREVILDubiquitination[1]
1861PWQARGGKSGAAFYAubiquitination[1]
1953MAQVFDLKGSLRNRNubiquitination[1]
1962SLRNRNVKTDTGKESubiquitination[1]
2062GILGGQGKMPTVVSPubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes. 
Sequence Annotation
 DOMAIN 365 440 DEP.
 DOMAIN 1758 2084 PIPK.
 ZN_FING 158 218 FYVE-type.
 REGION 1842 2098 Catalytic.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 307 307 Phosphoserine (By similarity).
 MOD_RES 318 318 Phosphoserine; by PKB/AKT1 or PKB/AKT2.
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 1544 1544 Phosphoserine.
 MOD_RES 1549 1549 Phosphoserine.
 MOD_RES 1754 1754 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Corneal dystrophy; Disease mutation; Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2098 AA 
Protein Sequence
MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERA 60
EGGQGEQQPL SGSWTSPQLP SRTQSVRSPT PYKKQLNEEL QRRSSALDTR RKAEPTFGGH 120
DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC 180
RLCGQIFCSR CCNQEIPGKF MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDSA 240
CSVSVLDPSE PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNTPLSTRLV SVQEDAGKSP 300
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRTYVRTE TTEDERKILL DSVQLKDLWK 360
KICHHSSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI ATRAQAIAIG QAMVDGRWLD 420
CVSHHDQLFR DEYALYRPLQ STEFSETPSP DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI 480
AEEGDDNLAN SASPSKRTSV SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH 540
PADQKEYLIS DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENG 600
EKQAMERLLS ANHNHMMALL QQLLHSDSLS SSWRDIIVSL VCQVVQTVRP DVKNQDDDMD 660
IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMSSCIK NPKILLLKCS IEYLYREETK 720
FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV LVEKTVSRIA QDMLLEHGIT LVINVKSQVL 780
ERISRMTQGD LVMSMDQLLT KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK 840
LRGGSDYELA RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQNPSFH SLIEGRGHEG 900
AVQEQYGGGS IPWDPDIPPE SLPCDDSSLL ELRIVFEKGE QENKNLPQAV ASVKHQEHST 960
TACPAGLPCA FFAPVPESLL PLPVDDQQDA LGSEQPETLQ QTVVLQDPKS QIRAFRDPLQ 1020
DDTGLYVTEE VTSSEDKRKT YSLAFKQELK DVILCISPVI TFREPFLLTE KGMRCSTRDY 1080
FAEQVYWSPL LNKEFKEMEN RRKKQLLRDL SGLQGMNGSI QAKSIQVLPS HELVSTRIAE 1140
HLGDSQSLGR MLADYRARGG RIQPKNSDPF AHSKDASSTS SGQSGSKNEG DEERGLILSD 1200
AVWSTKVDCL NPINHQRLCV LFSSSSAQSS NAPSACVSPW IVTMEFYGKN DLTLGIFLER 1260
YCFRPSYQCP SMFCDTPMVH HIRRFVHGQG CVQIILKELD SPVPGYQHTI LTYSWCRICK 1320
QVTPVVALSN ESWSMSFAKY LELRFYGHQY TRRANAEPCG HSIHHDYHQY FSYNQMVASF 1380
SYSPIRLLEV CVPLPKIFIK RQAPLKVSLL QDLKDFFQKV SQVYVAIDER LASLKTDTFS 1440
KTREEKMEDI FAQKEMEEGE FKNWIEKMQA RLMSSSVDTP QQLQSVFESL IAKKQSLCEV 1500
LQAWNNRLQD LFQQEKGRKR PSVPPSPGRL RQGEESKISA MDASPRNISP GLQNGEKEDR 1560
FLTTLSSQSS TSSTHLQLPT PPEVMSEQSV GGPPELDTAS SSEDVFDGHL LGSTDSQVKE 1620
KSTMKAIFAN LLPGNSYNPI PFPFDPDKHY LMYEHERVPI AVCEKEPSSI IAFALSCKEY 1680
RNALEELSKA TQWNSAEEGL PTNSTSDSRP KSSSPIRLPE MSGGQTNRTT ETEPQPTKKA 1740
SGMLSFFRGT AGKSPDLSSQ KRETLRGADS AYYQVGQTGK EGTENQGVEP QDEVDGGDTQ 1800
KKQLINPHVE LQFSDANAKF YCRLYYAGEF HKMREVILDS SEEDFIRSLS HSSPWQARGG 1860
KSGAAFYATE DDRFILKQMP RLEVQSFLDF APHYFNYITN AVQQKRPTAL AKILGVYRIG 1920
YKNSQNNTEK KLDLLVMENL FYGRKMAQVF DLKGSLRNRN VKTDTGKESC DVVLLDENLL 1980
KMVRDNPLYI RSHSKAVLRT SIHSDSHFLS SHLIIDYSLL VGRDDTSNEL VVGIIDYIRT 2040
FTWDKKLEMV VKSTGILGGQ GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC 2098 
Gene Ontology
 GO:0031410; C:cytoplasmic vesicle; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0031901; C:early endosome membrane; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0031902; C:late endosome membrane; TAS:Reactome.
 GO:0045121; C:membrane raft; IDA:HGNC.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:EC.
 GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; TAS:HGNC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; TAS:Reactome.
 GO:0044267; P:cellular protein metabolic process; IEA:InterPro.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0032288; P:myelin assembly; IEA:Compara.
 GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
 GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR002423; Cpn60/TCP-1.
 IPR000591; DEP_dom.
 IPR027409; GroEL-like_apical_dom.
 IPR027483; PInositol-4-P-5-kinase_C.
 IPR002498; PInositol-4-P-5-kinase_core.
 IPR027484; PInositol-4-P-5-kinase_N.
 IPR016034; PInositol-4P-5-kinase_core_sub.
 IPR027410; TCP-1-like_intermed.
 IPR011991; WHTH_DNA-bd_dom.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00118; Cpn60_TCP1
 PF00610; DEP
 PF01363; FYVE
 PF01504; PIP5K 
SMART
 SM00049; DEP
 SM00064; FYVE
 SM00330; PIPKc 
PROSITE
 PS50186; DEP
 PS51455; PIPK
 PS50178; ZF_FYVE 
PRINTS