CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009281
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Signal recognition particle 54 kDa protein 
Protein Synonyms/Alias
 SRP54 
Gene Name
 SRP54 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50DVNIKLVKQLRENVKubiquitination[1, 2, 3]
71EMASGLNKRKMIQHAubiquitination[2]
81MIQHAVFKELVKLVDacetylation[4]
92KLVDPGVKAWTPTKGubiquitination[2, 5]
267LSAVAATKSPIIFIGubiquitination[6]
311IDKVNELKLDDNEALubiquitination[3, 6, 7]
321DNEALIEKLKHGQFTubiquitination[1, 3, 5, 6]
323EALIEKLKHGQFTLRubiquitination[2, 5]
398DGAKVFSKQPGRIQRubiquitination[2]
426ELLTQYTKFAQMVKKubiquitination[1, 2, 3, 6]
438VKKMGGIKGLFKGGDubiquitination[2]
442GGIKGLFKGGDMSKNubiquitination[2]
448FKGGDMSKNVSQSQMubiquitination[2, 5, 6]
457VSQSQMAKLNQQMAKubiquitination[1, 2, 3, 5, 6, 8]
464KLNQQMAKMMDPRVLubiquitination[1, 2, 3, 5, 6]
496QGAAGNMKGMMGFNNubiquitination[5]
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] 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]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] 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]
 [6] 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]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [8] 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
 Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). 
Sequence Annotation
 NP_BIND 108 115 GTP (By similarity).
 NP_BIND 190 194 GTP (By similarity).
 NP_BIND 248 251 GTP (By similarity).
 REGION 1 295 G-domain.
 REGION 296 504 M-domain.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding; Signal recognition particle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 504 AA 
Protein Sequence
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCTALL EADVNIKLVK QLRENVKSAI 60
DLEEMASGLN KRKMIQHAVF KELVKLVDPG VKAWTPTKGK QNVIMFVGLQ GSGKTTTCSK 120
LAYYYQRKGW KTCLICADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVI IASEGVEKFK 180
NENFEIIIVD TSGRHKQEDS LFEEMLQVAN AIQPDNIVYV MDASIGQACE AQAKAFKDKV 240
DVASVIVTKL DGHAKGGGAL SAVAATKSPI IFIGTGEHID DFEPFKTQPF ISKLLGMGDI 300
EGLIDKVNEL KLDDNEALIE KLKHGQFTLR DMYEQFQNIM KMGPFSQILG MIPGFGTDFM 360
SKGNEQESMA RLKKLMTIMD SMNDQELDST DGAKVFSKQP GRIQRVARGS GVSTRDVQEL 420
LTQYTKFAQM VKKMGGIKGL FKGGDMSKNV SQSQMAKLNQ QMAKMMDPRV LHHMGGMAGL 480
QSMMRQFQQG AAGNMKGMMG FNNM 504 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
 GO:0008312; F:7S RNA binding; IDA:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0030942; F:endoplasmic reticulum signal peptide binding; IDA:UniProtKB.
 GO:0019003; F:GDP binding; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IDA:UniProtKB.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
 GO:0006184; P:GTP catabolic process; IDA:GOC.
 GO:0042493; P:response to drug; IDA:UniProtKB.
 GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; ISS:UniProtKB.
 GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; ISS:UniProtKB.
 GO:0006412; P:translation; TAS:Reactome. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR027417; P-loop_NTPase.
 IPR013822; Signal_recog_particl_SRP54_hlx.
 IPR004125; Signal_recog_particle_SRP54_M.
 IPR022941; SRP54.
 IPR006325; SRP54_euk.
 IPR000897; SRP54_GTPase_dom. 
Pfam
 PF00448; SRP54
 PF02881; SRP54_N
 PF02978; SRP_SPB 
SMART
 SM00382; AAA
 SM00962; SRP54
 SM00963; SRP54_N 
PROSITE
 PS00300; SRP54 
PRINTS