CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031141
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 cDNA FLJ61339, highly similar to Alanyl-tRNA synthetase (EC 6.1.1.7) 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
854KRVLEKTKQFIDSNPubiquitination[1]
900LALNEALKLFKMHSPubiquitination[1, 2]
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] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Aminoacyl-tRNA synthetase; Ligase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 992 AA 
Protein Sequence
MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS 60
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 120
LLTQEFGIPI ERLYVTYFGG DEAAGLEADL ECKQIWQNLG TYLYSFVRLD DTKILPGNMK 180
DNFWEMGDTG PCGPCSEIHY DRIGGRDAAH LVNQDDPNVL EIWNLVFIQY NREADGILKP 240
LPKKSIDTGM GLERLVSVLQ NKMSNYDTDL FVPYFEAIQK GTGARPYTGK VGAEDADGID 300
MAYRVLADHA RTITVALADG GRPDNTGRGY VLRRILRRAV RCAHEKLNAS RGFFATLVDV 360
VVQSLGDAFP ELKKDPDMVK DIINEEEVQF LKTLSRGRRI LDRKIQSLGD SKTIPGDTAW 420
LLYDTYGFPV DLTGLIAEEK GLVVDMDGFE EERKLAQLKS QGKGAGGEDL IMLDIYAIEE 480
LRARGLEVTD DSPKYNYHLD SSGSYVFENT VATVMALRRE KMFVEEVSTG QECGVVLDKT 540
CFYAEQGGQI YDEGYLVKVD DSSEDKTEFT VKNAQVRGGY VLHIGTIYGD LKVGDQVWLF 600
IDEPRRRPIM SNHTATHILN FALRSVLGEA DQKGSLVAPD RLRFDFTAKG AMSTQQIKKA 660
EEIANEMIEA AKAVYTQDCP LAAAKAIQGL RAVFDETYPD PVRVVSIGVP VSELLDDPSG 720
PAGSLTSVEF CGGTHLRNSS HAGAFVIVTE EAIAKGIRRI VAVTGAEAQK TLRKAESLKK 780
CLSVMEAKVK AQTAPNKDVQ REIADLGEAL ATAVIPQWQK DELRETLKSL KKVMDDLDRA 840
SKADVQKRVL EKTKQFIDSN PNQPLVILEM ESGASAKATQ GPGSPPLGLI SSLALNEALK 900
LFKMHSPQTS AMLFTVDNEA GKITCLCQVP QNAANRGLKA SEWVQQVSGL MDGKGGGKDV 960
SAQATGKNVG CLQEALQLAT SFAQLRLGDV KN 992 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR002318; Ala-tRNA-lgiase_IIc.
 IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
 IPR018165; Ala-tRNA-synth_IIc_core.
 IPR018164; Ala-tRNA-synth_IIc_N.
 IPR023033; Ala_tRNA_ligase_euk/bac.
 IPR003156; Pesterase_DHHA1.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF02272; DHHA1
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.