CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020252
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spermatogenesis-associated protein 5-like protein 1 
Protein Synonyms/Alias
  
Gene Name
 SPATA5L1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15FPEGPLLKLLPLDARubiquitination[1]
48ARLGSAVKISLPDGGubiquitination[1, 2]
247AGPPGVGKTQLVRAVubiquitination[1, 3, 4, 5]
372VIGTPTLKQRKEILQubiquitination[1, 6]
375TPTLKQRKEILQVITubiquitination[1]
425HALLHSEKNQDNPVIubiquitination[7]
442IDFLEAFKNIQPSSFubiquitination[3]
459VIGLMDIKPVDWEEIubiquitination[1, 6]
473IGGLEDVKLKLKQSIubiquitination[1]
475GLEDVKLKLKQSIEWubiquitination[1]
477EDVKLKLKQSIEWPLubiquitination[1, 6]
485QSIEWPLKFPWEFVRubiquitination[1, 3]
499RMGLTQPKGVLLYGPubiquitination[1, 4, 7]
511YGPPGCAKTTLVRALubiquitination[1, 2, 7]
577LGARSASKTGCDVQEubiquitination[1]
600ELDGVGLKTIERRGSubiquitination[1, 3, 6]
608TIERRGSKSSQQEFQubiquitination[1]
656YIPPPDHKGRLSILKubiquitination[1]
663KGRLSILKVCTKTMPubiquitination[1]
715GLDATTVKQEHFLKSubiquitination[1]
721VKQEHFLKSLKTVKPubiquitination[1]
724EHFLKSLKTVKPSLSacetylation[8]
724EHFLKSLKTVKPSLSubiquitination[1]
727LKSLKTVKPSLSCKDubiquitination[1]
733VKPSLSCKDLALYENubiquitination[1]
744LYENLFKKEGFSNVEubiquitination[1, 6]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
  
Sequence Annotation
 NP_BIND 241 248 ATP 1 (Potential).
 NP_BIND 505 512 ATP 2 (Potential).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 753 AA 
Protein Sequence
MAPDSDPFPE GPLLKLLPLD ARDRGTQRCR LGPAALHALG ARLGSAVKIS LPDGGSCLCT 60
AWPRRDGADG FVQLDPLCAS PGAAVGASRS RRSLSLNRLL LVPCPPLRRV AVWPVLRERA 120
GAPGARNTAA VLEAAQELLR NRPISLGHVV VAPPGAPGLV AALHIVGGTP SPDPAGLVTP 180
RTRVSLGGEP PSEAQPQPEV PLGGLSEAAD SLRELLRLPL RYPRALTALG LAVPRGVLLA 240
GPPGVGKTQL VRAVAREAGA ELLAVSAPAL QGSRPGETEE NVRRVFQRAR ELASRGPSLL 300
FLDEMDALCP QRGSRAPESR VVAQVLTLLD GASGDREVVV VGATNRPDAL DPALRRPGRF 360
DREVVIGTPT LKQRKEILQV ITSKMPISSH VDLGLLAEMT VGYVGADLTA LCREAAMHAL 420
LHSEKNQDNP VIDEIDFLEA FKNIQPSSFR SVIGLMDIKP VDWEEIGGLE DVKLKLKQSI 480
EWPLKFPWEF VRMGLTQPKG VLLYGPPGCA KTTLVRALAT SCHCSFVSVS GADLFSPFVG 540
DSEKVLSQIF RQARASTPAI LFLDEIDSIL GARSASKTGC DVQERVLSVL LNELDGVGLK 600
TIERRGSKSS QQEFQEVFNR SVMIIAATNR PDVLDTALLR PGRLDKIIYI PPPDHKGRLS 660
ILKVCTKTMP IGPDVSLENL AAETCFFSGA DLRNLCTEAA LLALQENGLD ATTVKQEHFL 720
KSLKTVKPSL SCKDLALYEN LFKKEGFSNV EGI 753 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA 
SMART
 SM00382; AAA 
PROSITE
 PS00674; AAA 
PRINTS