CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015605
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vacuolar protein sorting-associated protein 13C 
Protein Synonyms/Alias
  
Gene Name
 VPS13C 
Gene Synonyms/Alias
 KIAA1421 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
316PYAESELKTPKLDCNubiquitination[1]
578QALKVEAKLEHWYITubiquitination[2, 3]
695LDLRINLKPSYLVVPubiquitination[4]
797LAKAMVEKDIRMARFubiquitination[4]
821HVRISDQKMKDVLYLubiquitination[4]
823RISDQKMKDVLYLMNubiquitination[4]
1062EVQISTEKQQKNSTLubiquitination[4, 5]
1230ERAATSVKDLAQRSFubiquitination[4, 5]
1298RMDVQLTKLTLYRTVubiquitination[4, 5]
1338LAASWYHKVPVVEIKubiquitination[4]
1380EGTEDLDKVKPRVQEubiquitination[4, 5]
1382TEDLDKVKPRVQETGubiquitination[4]
1512LLKMLLTKADSDGPEubiquitination[4]
1585ESRSIAVKAVSSNISubiquitination[4]
1594VSSNISQKDVFDLKIubiquitination[4]
1636ASISVKPKQTDVFARubiquitination[4]
1660DLQSIHKKAVSILGDubiquitination[5]
1745ERAASSMKDLAQKSFubiquitination[4]
1750SMKDLAQKSFRLLMDubiquitination[4]
1815NIELTQLKLSRTILQubiquitination[4, 5]
1862PGMEIKGKLKPMQVAubiquitination[4]
1864MEIKGKLKPMQVALSubiquitination[4]
2077QSPENVAKETQILPRubiquitination[4, 5]
2155EASVRDLKVLACPFLubiquitination[4, 5, 6]
2168FLREKRGKNITTVLQubiquitination[4]
2233DGSKDTSKEMENLWGubiquitination[1, 2, 3, 5, 6]
2304PLLLAESKFSGNIKNubiquitination[2, 3]
2356WNLRLDVKKNPVQDKubiquitination[4]
2357NLRLDVKKNPVQDKSubiquitination[3, 4, 7]
2419STFDYSLKDRAPFTVubiquitination[1, 4, 5]
2427DRAPFTVKNAVGVPIubiquitination[4, 5]
2435NAVGVPIKVKPNCNLubiquitination[4, 5]
2437VGVPIKVKPNCNLRVubiquitination[4]
2612STTYISWKEELHRSRubiquitination[4, 5]
2721VLVKYQGKNWNGHFRubiquitination[4]
2792RSEDIHVKHPADFRDubiquitination[4, 5]
2930VGCEGSSKPFFYNRQubiquitination[4, 5]
3144LLEQSYQKHQISRDHubiquitination[5]
3166NFEVNFDKDPMEMRLubiquitination[4]
3487RITGSVGKGLAAITMubiquitination[2, 3, 4, 5, 6, 8]
3496LAAITMDKEYQQKRRubiquitination[4, 5]
3501MDKEYQQKRREELSRubiquitination[4, 5, 8]
3538GVTGIITKPVEGAKKacetylation[9]
3538GVTGIITKPVEGAKKubiquitination[4, 5]
3544TKPVEGAKKEGAAGFubiquitination[4, 5]
3545KPVEGAKKEGAAGFFubiquitination[4, 5]
3553EGAAGFFKGIGKGLVubiquitination[4, 5]
3557GFFKGIGKGLVGAVAubiquitination[2, 3, 4, 5]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [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]
 [9] 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
Functional Description
  
Sequence Annotation
 MOD_RES 614 614 Phosphothreonine.
 MOD_RES 619 619 Phosphoserine.
 MOD_RES 624 624 Phosphothreonine.
 MOD_RES 737 737 Phosphoserine.
 MOD_RES 1437 1437 Phosphothreonine (By similarity).
 MOD_RES 1979 1979 Phosphoserine (By similarity).
 MOD_RES 3538 3538 N6-acetyllysine.
 CROSSLNK 2357 2357 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3753 AA 
Protein Sequence
MVLESVVADL LNRFLGDYVE NLNKSQLKLG IWGGNVALDN LQIKENALSE LDVPFKVKAG 60
QIDKLTLKIP WKNLYGEAVV ATLEGLYLLV VPGASIKYDA VKEEKSLQDV KQKELSRIEE 120
ALQKAAEKGT HSGEFIYGLE NFVYKDIKPG RKRKKHKKHF KKPFKGLDRS KDKPKEAKKD 180
TFVEKLATQV IKNVQVKITD IHIKYEDDVT DPKRPLSFGV TLGELSLLTA NEHWTPCILN 240
EADKIIYKLI RLDSLSAYWN VNCSMSYQRS REQILDQLKN EILTSGNIPP NYQYIFQPIS 300
ASAKLYMNPY AESELKTPKL DCNIEIQNIA IELTKPQYLS MIDLLESVDY MVRNAPYRKY 360
KPYLPLHTNG RRWWKYAIDS VLEVHIRRYT QMWSWSNIKK HRQLLKSYKI AYKNKLTQSK 420
VSEEIQKEIQ DLEKTLDVFN IILARQQAQV EVIRSGQKLR KKSADTGEKR GGWFSGLWGK 480
KESKKKDEES LIPETIDDLM TPEEKDKLFT AIGYSESTHN LTLPKQYVAH IMTLKLVSTS 540
VTIRENKNIP EILKIQIIGL GTQVSQRPGA QALKVEAKLE HWYITGLRQQ DIVPSLVASI 600
GDTTSSLLKI KFETNPEDSP ADQTLIVQSQ PVEVIYDAKT VNAVVEFFQS NKGLDLEQIT 660
SATLMKLEEI KERTATGLTH IIETRKVLDL RINLKPSYLV VPQTGFHHEK SDLLILDFGT 720
FQLNSKDQGL QKTTNSSLEE IMDKAYDKFD VEIKNVQLLF ARAEETWKKC RFQHPSTMHI 780
LQPMDIHVEL AKAMVEKDIR MARFKVSGGL PLMHVRISDQ KMKDVLYLMN SIPLPQKSSA 840
QSPERQVSSI PIISGGTKGL LGTSLLLDTV ESESDDEYFD AEDGEPQTCK SMKGSELKKA 900
AEVPNEELIN LLLKFEIKEV ILEFTKQQKE EDTILVFNVT QLGTEATMRT FDLTVVSYLK 960
KISLDYHEIE GSKRKPLHLI SSSDKPGLDL LKVEYIKADK NGPSFQTAFG KTEQTVKVAF 1020
SSLNLLLQTQ ALVASINYLT TIIPSDDQSI SVAKEVQIST EKQQKNSTLP KAIVSSRDSD 1080
IIDFRLFAKL NAFCVIVCNE KNNIAEIKIQ GLDSSLSLQS RKQSLFARLE NIIVTDVDPK 1140
TVHKKAVSIM GNEVFRFNLD LYPDATEGDL YTDMSKVDGV LSLNVGCIQI VYLHKFLMSL 1200
LNFLNNFQTA KESLSAATAQ AAERAATSVK DLAQRSFRVS INIDLKAPVI VIPQSSISTN 1260
AVVVDLGLIR VHNQFSLVSD EDYLNPPVID RMDVQLTKLT LYRTVIQPGI YHPDIQLLHP 1320
INLEFLVNRN LAASWYHKVP VVEIKGHLDS MNVSLNQEDL NLLFRILTEN LCEGTEDLDK 1380
VKPRVQETGE IKEPLEISIS QDVHDSKNTL TTGVEEIRSV DIINMLLNFE IKEVVVTLMK 1440
KSEKKGRPLH ELNVLQLGME AKVKTYDMTA KAYLKKISMQ CFDFTDSKGE PLHIINSSNV 1500
TDEPLLKMLL TKADSDGPEF KTIHDSTKQR LKVSFASLDL VLHLEALLSF MDFLSSAAPF 1560
SEPSSSEKES ELKPLVGESR SIAVKAVSSN ISQKDVFDLK ITAELNAFNV FVCDQKCNIA 1620
DIKIHGMDAS ISVKPKQTDV FARLKDIIVM NVDLQSIHKK AVSILGDEVF RFQLTLYPDA 1680
TEGEAYADMS KVDGKLSFKV GCIQIVYVHK FFMSLLNFLN NFQTAKEALS TATVQAAERA 1740
ASSMKDLAQK SFRLLMDINL KAPVIIIPQS SVSPNAVIAD LGLIRVENKF SLVPMEHYSL 1800
PPVIDKMNIE LTQLKLSRTI LQASLPQNDI EILKPVNMLL SIQRNLAAAW YVQIPGMEIK 1860
GKLKPMQVAL SEDDLTVLMK ILLENLGEAS SQPSPTQSVQ ETVRVRKVDV SSVPDHLKEQ 1920
EDWTDSKLSM NQIVSLQFDF HFESLSIILY NNDINQESGV AFHNDSFQLG ELRLHLMASS 1980
GKMFKDGSMN VSVKLKTCTL DDLREGIERA TSRMIDRKND QDNNSSMIDI SYKQDKNGSQ 2040
IDAVLDKLYV CASVEFLMTV ADFFIKAVPQ SPENVAKETQ ILPRQTATGK VKIEKDDSVR 2100
PNMTLKAMIT DPEVVFVASL TKADAPALTA SFQCNLSLST SKLEQMMEAS VRDLKVLACP 2160
FLREKRGKNI TTVLQPCSLF MEKCTWASGK QNINIMVKEF IIKISPIILN TVLTIMAALS 2220
PKTKEDGSKD TSKEMENLWG IKSINDYNTW FLGVDTATEI TESFKGIEHS LIEENCGVVV 2280
ESIQVTLECG LGHRTVPLLL AESKFSGNIK NWTSLMAAVA DVTLQVHYYN EIHAVWEPLI 2340
ERVEGKRQWN LRLDVKKNPV QDKSLLPGDD FIPEPQMAIH ISSGNTMNIT ISKSCLNVFN 2400
NLAKGFSEGT ASTFDYSLKD RAPFTVKNAV GVPIKVKPNC NLRVMGFPEK SDIFDVDAGQ 2460
NLELEYASMV PSSQGNLSIL SRQESSFFTL TIVPHGYTEV ANIPVARPGR RLYNVRNPNA 2520
SHSDSVLVQI DATEGNKVIT LRSPLQIKNH FSIAFIIYKF VKNVKLLERI GIARPEEEFH 2580
VPLDSYRCQL FIQPAGILEH QYKESTTYIS WKEELHRSRE VRCMLQCPSV EVSFLPLIVN 2640
TVALPDELSY ICTHGEDWDV AYIIHLYPSL TLRNLLPYSL RYLLEGTAET HELAEGSTAD 2700
VLHSRISGEI MELVLVKYQG KNWNGHFRIR DTLPEFFPVC FSSDSTEVTT VDLSVHVRRI 2760
GSRMVLSVFS PYWLINKTTR VLQYRSEDIH VKHPADFRDI ILFSFKKKNI FTKNKVQLKI 2820
STSAWSSSFS LDTVGSYGCV KCPANNMEYL VGVSIKMSSF NLSRIVTLTP FCTIANKSSL 2880
ELEVGEIASD GSMPTNKWNY IASSECLPFW PESLSGKLCV RVVGCEGSSK PFFYNRQDNG 2940
TLLSLEDLNG GILVDVNTAE HSTVITFSDY HEGSAPALIM NHTPWDILTY KQSGSPEEMV 3000
LLPRQARLFA WADPTGTRKL TWTYAANVGE HDLLKDGCGQ FPYDANIQIH WVSFLDGRQR 3060
VLLFTDDVAL VSKALQAEEM EQADYEITLS LHSLGLSLVN NESKQEVSYI GITSSGVVWE 3120
VKPKQKWKPF SQKQIILLEQ SYQKHQISRD HGWIKLDNNF EVNFDKDPME MRLPIRSPIK 3180
RDFLSGIQIE FKQSSHQRSL RARLYWLQVD NQLPGAMFPV VFHPVAPPKS IALDSEPKPF 3240
IDVSVITRFN EYSKVLQFKY FMVLIQEMAL KIDQGFLGAI IALFTPTTDP EAERRRTKLI 3300
QQDIDALNAE LMETSMTDMS ILSFFEHFHI SPVKLHLSLS LGSGGEESDK EKQEMFAVHS 3360
VNLLLKSIGA TLTDVDDLIF KLAYYEIRYQ FYKRDQLIWS VVRHYSEQFL KQMYVLVLGL 3420
DVLGNPFGLI RGLSEGVEAL FYEPFQGAVQ GPEEFAEGLV IGVRSLFGHT VGGAAGVVSR 3480
ITGSVGKGLA AITMDKEYQQ KRREELSRQP RDFGDSLARG GKGFLRGVVG GVTGIITKPV 3540
EGAKKEGAAG FFKGIGKGLV GAVARPTGGI VDMASSTFQG IQRAAESTEE VSSLRPPRLI 3600
HEDGIIRPYD RQESEGSDLL ENHIKKLEGE TYRYHCAIPG SKKTILMVTN RRVLCIKEVE 3660
ILGLMCVDWQ CPFEDFVFPP SVSENVLKIS VKEQGLFHKK DSANQGCVRK VYLKDTATAE 3720
RACNAIEDAQ STRQQQKLMK QSSVRLLRPQ LPS 3753 
Gene Ontology
  
Interpro
 IPR015412; Autophagy-rel_C.
 IPR026847; VPS13.
 IPR026854; VPS13A_N.
 IPR009543; VPSAP_dom. 
Pfam
 PF09333; ATG_C
 PF12624; Chorein_N
 PF06650; DUF1162 
SMART
  
PROSITE
  
PRINTS