CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014739
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger FYVE domain-containing protein 26 
Protein Synonyms/Alias
 FYVE domain-containing centrosomal protein; FYVE-CENT; Spastizin 
Gene Name
 ZFYVE26 
Gene Synonyms/Alias
 KIAA0321 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MNHPFGKEEAASQKubiquitination[1]
266LLSCLLHKASRGLLSubiquitination[1]
295PRATASGKVSPDHLDubiquitination[1, 2]
707SSRSPPEKPKQESQSubiquitination[1]
709RSPPEKPKQESQSCSubiquitination[1]
886ELAQVEHKIENQNSDubiquitination[2]
1045LMSASQTKSESVEEKubiquitination[2]
1052KSESVEEKGGGPPRCubiquitination[1, 2]
1309SSALAFLKSRSKLLAubiquitination[1]
1313AFLKSRSKLLATVACubiquitination[1]
1469WQYLFPVKDASLRSRubiquitination[2]
1583HLISLHQKHLLHLLEubiquitination[1]
1596LERRDHDKALQLLRRubiquitination[1]
1727LLSRYAEKALDFPYPubiquitination[1, 2]
1963EHCCRLSKGLTNPEVubiquitination[2]
2416AARQLVEKEKYSEIQacetylation[3]
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] 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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair. 
Sequence Annotation
 ZN_FING 1812 1872 FYVE-type.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Hereditary spastic paraplegia; Lipid-binding; Metal-binding; Neurodegeneration; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2539 AA 
Protein Sequence
MNHPFGKEEA ASQKQLFGFF CECLRRGEWE LAQACVPQLQ EGQGDIPKRV EDILQALVVC 60
PNLLRCGQDI NPQRVAWVWL LVLEKWLARE KKLLPVVFRR KLEFLLLSED LQGDIPENIL 120
EELYETLTQG AVGHVPDGNP RRESWTPRLS SEAVSVLWDL LRQSPQPAQA LLELLLEEDD 180
GTGLCHWPLQ NALVDLIRKA LRALQGPDSV PPGVVDAIYG ALRTLRCPAE PLGVELHLLC 240
EELLEACRTE GSPLREERLL SCLLHKASRG LLSLYGHTYA EKVTEKPPRA TASGKVSPDH 300
LDPERAMLAL FSNPNPAEAW KVAYFYCLSN NKHFLEQILV TALTLLKEED FPNLGCLLDR 360
EFRPLSCLLV LLGWTHCQSL ESAKRLLQTL HRTQGPGCDE LLRDACDGLW AHLEVLEWCI 420
QQSSNPIPKR DLLYHLHGGD SHSVLYTLHH LTNLPALREE DVLKLLQKVP AKDPQQEPDA 480
VDAPVPEHLS QCQNLTLYQG FCAMKYAIYA LCVNSHQHSQ CQDCKDSLSE DLASATEPAN 540
DSLSSPGAAN LFSTYLARCQ QYLCSIPDSL CLELLENIFS LLLITSADLH PEPHLPEDYA 600
EDDDIEGKSP SGLRSPSESP QHIAHPERKS ERGSLGVPKT LAYTMPSHVK AEPKDSYPGP 660
HRHSFLDLKH FTSGISGFLA DEFAIGAFLR LLQEQLDEIS SRSPPEKPKQ ESQSCSGSRD 720
GLQSRLHRLS KVVSEAQWRH KVVTSNHRSE EQPSRRYQPA TRHPSLRRGR RTRRSQADGR 780
DRGSNPSLES TSSELSTSTS EGSLSAMSGR NELHSRLHPH PQSSLIPMMF SPPESLLASC 840
ILRGNFAEAH QVLFTFNLKS SPSSGELMFM ERYQEVIQEL AQVEHKIENQ NSDAGSSTIR 900
RTGSGRSTLQ AIGSAAAAGM VFYSISDVTD KLLNTSGDPI PMLQEDFWIS TALVEPTAPL 960
REVLEDLSPP AMAAFDLACS QCQLWKTCKQ LLETAERRLN SSLERRGRRI DHVLLNADGI 1020
RGFPVVLQQI SKSLNYLLMS ASQTKSESVE EKGGGPPRCS ITELLQMCWP SLSEDCVASH 1080
TTLSQQLDQV LQSLREALEL PEPRTPPLSS LVEQAAQKAP EAEAHPVQIQ TQLLQKNLGK 1140
QTPSGSRQMD YLGTFFSYCS TLAAVLLQSL SSEPDHVEVK VGNPFVLLQQ SSSQLVSHLL 1200
FERQVPPERL AALLAQENLS LSVPQVIVSC CCEPLALCSS RQSQQTSSLL TRLGTLAQLH 1260
ASHCLDDLPL STPSSPRTTE NPTLERKPYS SPRDSSLPAL TSSALAFLKS RSKLLATVAC 1320
LGASPRLKVS KPSLSWKELR GRREVPLAAE QVARECERLL EQFPLFEAFL LAAWEPLRGS 1380
LQQGQSLAVN LCGWASLSTV LLGLHSPIAL DVLSEAFEES LVARDWSRAL QLTEVYGRDV 1440
DDLSSIKDAV LSCAVACDKE GWQYLFPVKD ASLRSRLALQ FVDRWPLESC LEILAYCISD 1500
TAVQEGLKCE LQRKLAELQV YQKILGLQSP PVWCDWQTLR SCCVEDPSTV MNMILEAQEY 1560
ELCEEWGCLY PIPREHLISL HQKHLLHLLE RRDHDKALQL LRRIPDPTMC LEVTEQSLDQ 1620
HTSLATSHFL ANYLTTHFYG QLTAVRHREI QALYVGSKIL LTLPEQHRAS YSHLSSNPLF 1680
MLEQLLMNMK VDWATVAVQT LQQLLVGQEI GFTMDEVDSL LSRYAEKALD FPYPQREKRS 1740
DSVIHLQEIV HQAADPETLP RSPSAEFSPA APPGISSIHS PSLRERSFPP TQPSQEFVPP 1800
ATPPARHQWV PDETESICMV CCREHFTMFN RRHHCRRCGR LVCSSCSTKK MVVEGCRENP 1860
ARVCDQCYSY CNKDVPEEPS EKPEALDSSK SESPPYSFVV RVPKADEVEW ILDLKEEENE 1920
LVRSEFYYEQ APSASLCIAI LNLHRDSIAC GHQLIEHCCR LSKGLTNPEV DAGLLTDIMK 1980
QLLFSAKMMF VKAGQSQDLA LCDSYISKVD VLNILVAAAY RHVPSLDQIL QPAAVTRLRN 2040
QLLEAEYYQL GVEVSTKTGL DTTGAWHAWG MACLKAGNLT AAREKFSRCL KPPFDLNQLN 2100
HGSRLVQDVV EYLESTVRPF VSLQDDDYFA TLRELEATLR TQSLSLAVIP EGKIMNNTYY 2160
QECLFYLHNY STNLAIISFY VRHSCLREAL LHLLNKESPP EVFIEGIFQP SYKSGKLHTL 2220
ENLLESIDPT LESWGKYLIA ACQHLQKKNY YHILYELQQF MKDQVRAAMT CIRFFSHKAK 2280
SYTELGEKLS WLLKAKDHLK IYLQETSRSS GRKKTTFFRK KMTAADVSRH MNTLQLQMEV 2340
TRFLHRCESA GTSQITTLPL PTLFGNNHMK MDVACKVMLG GKNVEDGFGI AFRVLQDFQL 2400
DAAMTYCRAA RQLVEKEKYS EIQQLLKCVS ESGMAAKSDG DTILLNCLEA FKRIPPQELE 2460
GLIQAIHNDD NKVRAYLICC KLRSAYLIAV KQEHSRATAL VQQVQQAAKS SGDAVVQDIC 2520
AQWLLTSHPR GAHGPGSRK 2539 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB. 
Interpro
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01363; FYVE 
SMART
 SM00064; FYVE 
PROSITE
 PS50178; ZF_FYVE 
PRINTS