CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012491
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Early endosome antigen 1 
Protein Synonyms/Alias
 Endosome-associated protein p162; Zinc finger FYVE domain-containing protein 2 
Gene Name
 EEA1 
Gene Synonyms/Alias
 ZFYVE2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58GSADELFKHYEAVHDubiquitination[1, 2, 3]
100QDLQASLKEEKWYSEubiquitination[4, 5]
164MKDLFEQKAAQLATEubiquitination[5]
178EIADIKSKYDEERSLmethylation[6]
392ETKYQHLKAEFKQLQacetylation[7]
848LQKVKMEKEALMTELmethylation[8]
1138EIKCRQEKEITKLNEacetylation[9]
1165ITNLKDAKQLLIQQKacetylation[7]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Post-translational modifications in the rat lumbar spinal cord in experimental autoimmune encephalomyelitis.
 Grant JE, Hu J, Liu T, Jain MR, Elkabes S, Li H.
 J Proteome Res. 2007 Jul;6(7):2786-91. [PMID: 17567059]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [9] 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] 
Functional Description
 Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking. 
Sequence Annotation
 ZN_FING 41 64 C2H2-type.
 ZN_FING 1352 1410 FYVE-type.
 MOD_RES 70 70 Phosphoserine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Endosome; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1411 AA 
Protein Sequence
MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY 60
EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ 120
QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD 180
EERSLREAAE QKVTRLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM 240
TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL 300
TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL 360
HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH 420
SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ 480
HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS 540
LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD 600
QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA 660
QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKYLS 720
LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI 780
VSSTRLDLQK KSEALESIKQ KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE 840
LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ 900
LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN 960
INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN 1020
YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL 1080
KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI 1140
TKLNEELKSH KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV 1200
KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS 1260
QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL 1320
DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI 1380
FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G 1411 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
 GO:0055037; C:recycling endosome; IEA:Compara.
 GO:0005969; C:serine-pyruvate aminotransferase complex; IEA:Compara.
 GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
 GO:0005516; F:calmodulin binding; NAS:UniProtKB.
 GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; TAS:UniProtKB.
 GO:0045022; P:early endosome to late endosome transport; NAS:UniProtKB.
 GO:0016189; P:synaptic vesicle to endosome fusion; TAS:UniProtKB.
 GO:0006906; P:vesicle fusion; IMP:UniProtKB. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01363; FYVE 
SMART
 SM00064; FYVE
 SM00355; ZnF_C2H2 
PROSITE
 PS50178; ZF_FYVE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS