CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013577
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger FYVE domain-containing protein 26 
Protein Synonyms/Alias
  
Gene Name
 Zfyve26 
Gene Synonyms/Alias
 Kiaa0321 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
459EVLKLLQKEPTKDLQubiquitination[1]
651DSSPGPHKHSFLDLKubiquitination[1]
698HRTPEETKLPEDQSCubiquitination[1]
731SEAQWRYKVVTSNQGubiquitination[1]
1036LMQTGLAKSETLEERubiquitination[1]
1095ALALPESKSTPLSCLubiquitination[1]
1127IQSQLLQKTLGRQTPubiquitination[1]
1321SRGTKVSKPGLSWKEubiquitination[1]
1586LERSEHDKALQLLQRubiquitination[1]
1717LLSRYAGKALDLPYPubiquitination[1]
2442LNCLEAFKRIPPQELubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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 (By similarity). 
Sequence Annotation
 ZN_FING 1802 1862 FYVE-type.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Lipid-binding; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2529 AA 
Protein Sequence
MSYPFGKEET ATEEELFEFF CECLRRGDWE LAQACVPQLH RGQGEIPQKV EDILQALVQC 60
PILLRCGPDI NPQRLAWLWL LVLEKWLAPE KKLLSTAIRR KLEFLFLSED LQGDIPETIL 120
KELFETLAQG PAGSIPDRRT PQLSPEAVSV LWNLLKQAPR PAQALLELLL EDHHSASLCP 180
SPLQKSLLDL IREALQTLRD PASQPPGVAD AVCGALQALC CKAELPESEW RVLCEELLET 240
CRTEDSPLQE ERLLGCLLHK AGRNLLSLYG HTYAEKVAER PPKATLSGKD HPDPERAMLA 300
LFSTPDPAHA WKMAFFYCLS NNKHFLEQIL VTALTLLKEE DFPSLGYLLD REFRPLSHLL 360
VLLGWTHCQS LESAKRLLQT LYRTQDQGHD ELLRDACEGL WAHLEVLEWC VQQSSNLIPK 420
RELLCHLHGG DSHSVLYSLH HLTNLPALNE EEVLKLLQKE PTKDLQGEHE THDASVPEHL 480
SQCQSLTLYQ GFCAMKYAVY ALCVNSHQHS QCQDCRDSAS EDLALVEPGS DSLPSPGASH 540
LFPTYLARCR QYLHSIPASL CLEILENIFS LLLITSADLH PEPHLPEDYA EDEDIEGKGP 600
LGLRSPSESP QHIAATERRS ERASMGPRNP AHTVPGCPKA EPKDSSPGPH KHSFLDLKHF 660
TSGVNGFLAD EFAMGAFLSL LQEQLTEISS HRTPEETKLP EDQSCSAARD GLQSRLHRFS 720
KVLSEAQWRY KVVTSNQGSE EQPSRRYRPI ATRHSSLRRG RRTRRTRADG RERGSNPSLE 780
GTSSELSTST SEGSLSAVSG QVESDSRFQT QPQSSIIPMM FSTPESLLAS CILRGNFAEA 840
HQVVLMFNLK SSPIAGELMF VERYQEVIQE LARVEHKIEN QNSDGGNNTI RRTGSGRSTL 900
QAIGSAAAAG MVFYSISDVT EKLLSPSEDP IPTLQEDFWI NATPMETTTP LREVLEDLSP 960
PAMAAFDLAC CQCQLWKTCK QLLETAERRL SSSLESRGRR LDQVVLNPDG MRGFPFVLQQ 1020
ISKILSYPLM QTGLAKSETL EERGGGAPRS SISELLQMCW PSLTEDCVAS HTSLSQQLEQ 1080
ALQSLREALA LPESKSTPLS CLVEQAAQKA PEAEAHPVHI QSQLLQKTLG RQTPAGHRQT 1140
DYVGAFFSYC SSLAAVLLRS LSSDPDHVEV RVGNPFVLLQ QSSSQLVSHL LLERQVPPDR 1200
LAALLAQEHL NLSVPQVIVS CCCEPLTLCL SRQSQQASSL LTHLGMLARE HASHLLDGLP 1260
LSTLGSPRPS ENPSAERKSH SSPKDSLPAF TASALAFLKS RSKILAMVAC LRTSRGTKVS 1320
KPGLSWKELR GRREAPLTAE KVAQECEHLL EQFPVFEAAL LANWEPLQQA SEPKQSLAAS 1380
LCGQANLSTV LLGLHSSLAL DILTEAFEGA LVARDWPRAL QLIDVYGQDL DDLSIVQDSV 1440
LTCAAVCDKE GWQYLFPVKD ASLRSQLALR FVDKWPLESC LEILAYCVSD MAVQEELKSE 1500
LQRKLMELRV YQKILGLQDP PVWCDWQTLR SCCAEDPSAV MDMMLDSQEY ELCEEWGRLY 1560
PIPREHLVSL HHKHLLHLLE RSEHDKALQL LQRIPDPTMC LEVTERSLDQ HPSLATSHFL 1620
ANYLTSHFYG ELTTDRHREI QALYMGSKVL LTLPEQHRAS YARLSSSPLL MLEQLLMNMK 1680
VDWATTAVQT LHQLLAGQDI GFTLDEVDSL LSRYAGKALD LPYPLREKRS DSMIHLQEPV 1740
HQASDSETLS RSSSAEFSAA AAPGSALVRS PSPKERAFPQ TQPPVEFVPP ETPPARDQWV 1800
PDETESVCMV CCREHFTMFN RRHHCRRCGR LVCGSCSTKK MVVEGFRENP TRVCDQCYSY 1860
YNKDTPEESP CQSEVPDSAK NESPPYSAVV RVPKATEVEW ILSLSEEENE LVRSEFYYEQ 1920
APSASLCIAI LNLHRDSIAC GHQLIEHCCR LSRGLTNPEV DAGLLIDIMK QLLFSAKMMF 1980
VKAGQSQDLA LCDSYISKVD VLHLLVAAAY RHVPSLDQIL QPAAVTRLRN QLLEAEYYQL 2040
GVEVSTKTGL DSTGAWHAWG MACLKAGNLT VAREKFTRCL KPPLDLNQLS HGSRLVQDVV 2100
EYLESTVRPL VSLQDDDYFA TLRELEATLR TQSLLLEAIP EGKIMNNTYY QECLFYLHNY 2160
STNLAIISFY MRHNCLREAL LHLLNKESPP EVFIEGIFQP SYKSGKLHTL ENLLESIDPT 2220
LESWGAHLIA ACQHLQKNSY YHILYELQQF MKDQVRAAMT CIRFFSHKAK SYTELGEKLS 2280
WLLKAKDHLK IYLQETSRSS GRKKATFFRK KMTAADVSRH MNTLQLQMEV TRFLHRCESA 2340
GTSQVTTLPL PTLFGNNHMK MEVACKVMLG GKNVEDGFGI AFRVLQDFQL DAAATYCRAA 2400
RQLVEREKYG EIRQLLKCVS ESGMAAKSDG DTILLNCLEA FKRIPPQELE GLIQAIHSDD 2460
NKVRAYLTCC KLRSAYLIAV KQEHSQAAAL VQQVQQAAKS SGDSVVQDIC AQWLLTSHSR 2520
GAHGSGSRK 2529 
Gene Ontology
 GO:0005813; C:centrosome; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0030496; C:midbody; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
 GO:0000910; P:cytokinesis; ISS:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; ISS: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