CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001324
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Signal recognition particle subunit SRP72 
Protein Synonyms/Alias
 SRP72; Signal recognition particle 72 kDa protein 
Gene Name
 SRP72 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42NKILQINKDDVTALHacetylation[1]
51DVTALHCKVVCLIQNacetylation[2]
73NVINTHTKVLANNSLubiquitination[3, 4, 5]
84NNSLSFEKAYCEYRLubiquitination[1, 3, 5, 6]
99NRIENALKTIESANQubiquitination[7]
110SANQQTDKLKELYGQubiquitination[6]
112NQQTDKLKELYGQVLubiquitination[3, 4, 5]
201QAMKILQKAEDLCRRubiquitination[6]
287FDSKKKVKLTNAEGVubiquitination[1, 6]
297NAEGVEFKLSKKQLQubiquitination[1, 6]
301VEFKLSKKQLQAIEFubiquitination[1, 6]
325NQAEQCRKISASLQSubiquitination[6]
352AAQLCREKQHTKAIEubiquitination[6]
356CREKQHTKAIELLQEubiquitination[6]
376PENAAEIKLTMAQLKubiquitination[7]
383KLTMAQLKISQGNISubiquitination[3, 4, 5, 6, 7, 8, 9, 10]
391ISQGNISKACLILRSubiquitination[4, 6, 7, 9, 10, 11, 12]
463FKLKYGRKKEAISDLubiquitination[6]
464KLKYGRKKEAISDLQubiquitination[6]
475SDLQQLWKQNPKDIHubiquitination[3, 4, 5, 6, 7]
498YSLVDPEKAKALSKHubiquitination[6, 7]
500LVDPEKAKALSKHLPubiquitination[6]
504EKAKALSKHLPSSDSubiquitination[3, 5]
544VTGDSQPKEQGQGDLubiquitination[1, 6, 7]
569LPKNYDPKVTPDPERubiquitination[1, 6, 7]
594RGRKKGKKKDQIGKGubiquitination[13]
595GRKKGKKKDQIGKGTubiquitination[13]
600KKKDQIGKGTQGATAubiquitination[1, 7, 12, 13]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] 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]
 [11] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [12] 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]
 [13] 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] 
Functional Description
 Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. 
Sequence Annotation
 REPEAT 11 44 TPR 1.
 REPEAT 109 142 TPR 2.
 REPEAT 226 259 TPR 3.
 REPEAT 406 439 TPR 4.
 REPEAT 447 480 TPR 5.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 571 571 Phosphothreonine.
 MOD_RES 618 618 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Signal recognition particle; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 671 AA 
Protein Sequence
MASGGSGGVS VPALWSEVNR YGQNGDFTRA LKTVNKILQI NKDDVTALHC KVVCLIQNGS 60
FKEALNVINT HTKVLANNSL SFEKAYCEYR LNRIENALKT IESANQQTDK LKELYGQVLY 120
RLERYDECLA VYRDLVRNSQ DDYDEERKTN LSAVVAAQSN WEKVVPENLG LQEGTHELCY 180
NTACALIGQG QLNQAMKILQ KAEDLCRRSL SEDTDGTEED PQAELAIIHG QMAYILQLQG 240
RTEEALQLYN QIIKLKPTDV GLLAVIANNI ITINKDQNVF DSKKKVKLTN AEGVEFKLSK 300
KQLQAIEFNK ALLAMYTNQA EQCRKISASL QSQSPEHLLP VLIQAAQLCR EKQHTKAIEL 360
LQEFSDQHPE NAAEIKLTMA QLKISQGNIS KACLILRSIE ELKHKPGMVS ALVTMYSHEE 420
DIDSAIEVFT QAIQWYQNHQ PKSPAHLSLI REAANFKLKY GRKKEAISDL QQLWKQNPKD 480
IHTLAQLISA YSLVDPEKAK ALSKHLPSSD SMSLKVDVEA LENSAGATYI RKKGGKVTGD 540
SQPKEQGQGD LKKKKKKKKG KLPKNYDPKV TPDPERWLPM RERSYYRGRK KGKKKDQIGK 600
GTQGATAGAS SELDASKTVS SPPTSPRPGS AATVSASTSN IIPPRHQKPA GAPATKKKQQ 660
QKKKKGGKGG W 671 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
 GO:0008312; F:7S RNA binding; IEA:InterPro.
 GO:0005047; F:signal recognition particle binding; IPI:UniProtKB.
 GO:0042493; P:response to drug; IDA:UniProtKB.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006412; P:translation; TAS:Reactome. 
Interpro
 IPR013699; Signal_recog_part_SRP72_RNA-bd.
 IPR026270; SRP72.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF08492; SRP72
 PF00515; TPR_1
 PF13174; TPR_6 
SMART
  
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS