CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022578
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ankyrin repeat and FYVE domain-containing protein 1 
Protein Synonyms/Alias
 Ankyrin repeats hooked to a zinc finger motif 
Gene Name
 ANKFY1 
Gene Synonyms/Alias
 ANKHZN; KIAA1255 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MAEEEVAKLEKHLMLubiquitination[1]
11EEVAKLEKHLMLLRQubiquitination[1]
43LLAAQANKESSSESFubiquitination[1]
279ATTLVSHKADVDMVDubiquitination[1]
489AHVNHRNKWGETPLHubiquitination[1]
585IIPDFSLKDSRDQTVubiquitination[1]
636AIQRQDSKSALFLLEubiquitination[1, 2]
851AMTFKNNKSAEAILKubiquitination[1, 3]
858KSAEAILKRESGAAEubiquitination[1, 3, 4, 5, 6]
870AAEQVDNKGRNFLHVubiquitination[1]
931NLLLAGAKVNELTKHubiquitination[1]
1088FNYQVATKQLLFRLLubiquitination[1]
1146TKEIPIIKFDLNKPVubiquitination[1]
1151IIKFDLNKPVRVCNIubiquitination[1, 3, 4]
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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] 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]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
  
Sequence Annotation
 DOMAIN 68 130 BTB.
 REPEAT 217 247 ANK 1.
 REPEAT 255 284 ANK 2.
 REPEAT 288 317 ANK 3.
 REPEAT 322 362 ANK 4.
 REPEAT 366 396 ANK 5.
 REPEAT 490 519 ANK 6.
 REPEAT 542 572 ANK 7.
 REPEAT 588 617 ANK 8.
 REPEAT 621 650 ANK 9.
 REPEAT 654 683 ANK 10.
 REPEAT 687 716 ANK 11.
 REPEAT 724 753 ANK 12.
 REPEAT 769 798 ANK 13.
 REPEAT 802 832 ANK 14.
 REPEAT 836 865 ANK 15.
 REPEAT 870 899 ANK 16.
 REPEAT 905 934 ANK 17.
 REPEAT 938 967 ANK 18.
 REPEAT 971 1001 ANK 19.
 REPEAT 1005 1037 ANK 20.
 REPEAT 1043 1072 ANK 21.
 ZN_FING 1104 1164 FYVE-type.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; ANK repeat; Complete proteome; Cytoplasm; Direct protein sequencing; Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1169 AA 
Protein Sequence
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD 60
LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW 120
IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS 180
TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE 240
MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG 300
DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP 360
NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV 420
NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN 480
GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS 540
VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG 600
MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ 660
LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG 720
PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW 780
GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP 840
FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR 900
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE 960
NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN 1020
AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI 1080
FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK 1140
EIPIIKFDLN KPVRVCNICF DVLTLGGVS 1169 
Gene Ontology
 GO:0010008; C:endosome membrane; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12796; Ank_2
 PF00651; BTB
 PF01363; FYVE 
SMART
 SM00248; ANK
 SM00225; BTB
 SM00064; FYVE 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50097; BTB
 PS50178; ZF_FYVE 
PRINTS
 PR01415; ANKYRIN.