CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013384
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Angiomotin 
Protein Synonyms/Alias
  
Gene Name
 AMOT 
Gene Synonyms/Alias
 KIAA1071 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94SENLIMEKQLSPRMQubiquitination[1, 2, 3, 4, 5]
113LPTYEEAKVQSQYFRubiquitination[1, 2, 4, 5, 6]
167DEGLRDLKQGHVRSLubiquitination[2]
209PQPNDLYKNPTSSSEubiquitination[4]
219TSSSEFYKAQGPLPNubiquitination[1, 2, 3, 4, 5]
464EKVARLQKVETEIQRubiquitination[6]
545SQLFAKNKESQREKEacetylation[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] 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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
 Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. 
Sequence Annotation
 MOTIF 1081 1084 PDZ-binding.
 MOD_RES 712 712 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Cell junction; Coiled coil; Complete proteome; Phosphoprotein; Reference proteome; Tight junction; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1084 AA 
Protein Sequence
MRNSEEQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNGPPFPS GSGNPGPQSD 60
VLSPQDHHQQ LVAHAARQEP QGQEIQSENL IMEKQLSPRM QNNEELPTYE EAKVQSQYFR 120
GQQHASVGAA FYVTGVTNQK MRTEGRPSVQ RLNPGKMHQD EGLRDLKQGH VRSLSERLMQ 180
MSLATSGVKA HPPVTSAPLS PPQPNDLYKN PTSSSEFYKA QGPLPNQHSL KGMEHRGPPP 240
EYPFKGMPPQ SVVCKPQEPG HFYSEHRLNQ PGRTEGQLMR YQHPPEYGAA RPAQDISLPL 300
SARNSQPHSP TSSLTSGGSL PLLQSPPSTR LSPARHPLVP NQGDHSAHLP RPQQHFLPNQ 360
AHQGDHYRLS QPGLSQQQQQ QQQQHHHHHH HQQQQQQQPQ QQPGEAYSAM PRAQPSSASY 420
QPVPADPFAI VSRAQQMVEI LSDENRNLRQ ELEGCYEKVA RLQKVETEIQ RVSEAYENLV 480
KSSSKREALE KAMRNKLEGE IRRMHDFNRD LRERLETANK QLAEKEYEGS EDTRKTISQL 540
FAKNKESQRE KEKLEAELAT ARSTNEDQRR HIEIRDQALS NAQAKVVKLE EELKKKQVYV 600
DKVEKMQQAL VQLQAACEKR EQLEHRLRTR LERELESLRI QQRQGNCQPT NVSEYNAAAL 660
MELLREKEER ILALEADMTK WEQKYLEENV MRHFALDAAA TVAAQRDTTV ISHSPNTSYD 720
TALEARIQKE EEEILMANKR CLDMEGRIKT LHAQIIEKDA MIKVLQQRSR KEPSKTEQLS 780
CMRPAKSLMS ISNAGSGLLS HSSTLTGSPI MEEKRDDKSW KGSLGILLGG DYRAEYVPST 840
PSPVPPSTPL LSAHSKTGSR DCSTQTERGT ESNKTAAVAP ISVPAPVAAA ATAAAITATA 900
ATITTTMVAA APVAVAAAAA PAAAAAPSPA TAAATAAAVS PAAAGQIPAA ASVASAAAVA 960
PSAAAAAAVQ VAPAAPAPVP APALVPVPAP AAAQASAPAQ TQAPTSAPAV APTPAPTPTP 1020
AVAQAEVPAS PATGPGPHRL SIPSLTCNPD KTDGPVFHSN TLERKTPIQI LGQEPDAEMV 1080
EYLI 1084 
Gene Ontology
 GO:0005884; C:actin filament; IDA:UniProtKB.
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030139; C:endocytic vesicle; IDA:MGI.
 GO:0009897; C:external side of plasma membrane; IDA:MGI.
 GO:0016021; C:integral to membrane; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:MGI.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0005923; C:tight junction; IDA:UniProtKB.
 GO:0043532; F:angiostatin binding; IDA:UniProtKB.
 GO:0004872; F:receptor activity; IDA:MGI.
 GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
 GO:0043534; P:blood vessel endothelial cell migration; IEA:Compara.
 GO:0042074; P:cell migration involved in gastrulation; IEA:Compara.
 GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
 GO:0034613; P:cellular protein localization; IDA:MGI.
 GO:0006935; P:chemotaxis; IEA:Compara.
 GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IEA:Compara.
 GO:0001702; P:gastrulation with mouth forming second; IEA:Compara.
 GO:0035329; P:hippo signaling cascade; IGI:MGI.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
 GO:0034260; P:negative regulation of GTPase activity; IEA:Compara.
 GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
 GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
 GO:0045793; P:positive regulation of cell size; TAS:UniProtKB.
 GO:0040019; P:positive regulation of embryonic development; IEA:Compara.
 GO:0051496; P:positive regulation of stress fiber assembly; TAS:UniProtKB.
 GO:0030334; P:regulation of cell migration; IDA:MGI.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:Compara.
 GO:0001570; P:vasculogenesis; IEA:Compara. 
Interpro
 IPR009114; Angiomotin.
 IPR024646; Angiomotin_C. 
Pfam
 PF12240; Angiomotin_C 
SMART
  
PROSITE
  
PRINTS
 PR01807; ANGIOMOTIN.