Tag | Content |
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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 |
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459 | EVLKLLQKEPTKDLQ | ubiquitination | [1] | 651 | DSSPGPHKHSFLDLK | ubiquitination | [1] | 698 | HRTPEETKLPEDQSC | ubiquitination | [1] | 731 | SEAQWRYKVVTSNQG | ubiquitination | [1] | 1036 | LMQTGLAKSETLEER | ubiquitination | [1] | 1095 | ALALPESKSTPLSCL | ubiquitination | [1] | 1127 | IQSQLLQKTLGRQTP | ubiquitination | [1] | 1321 | SRGTKVSKPGLSWKE | ubiquitination | [1] | 1586 | LERSEHDKALQLLQR | ubiquitination | [1] | 1717 | LLSRYAGKALDLPYP | ubiquitination | [1] | 2442 | LNCLEAFKRIPPQEL | ubiquitination | [1] |
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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. |
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