CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010755
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vigilin 
Protein Synonyms/Alias
 High density lipoprotein-binding protein; HDL-binding protein 
Gene Name
 HDLBP 
Gene Synonyms/Alias
 HBP; VGL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88HVPLEERKYKDMNQFubiquitination[1]
90PLEERKYKDMNQFGEubiquitination[1]
138GKLDAVMKARKDIVAubiquitination[1]
202QIKITGTKEGIEKARubiquitination[1]
231VERLEVEKAFHPFIAubiquitination[1, 2, 3]
274EIVFTGEKEQLAQAVubiquitination[1]
314HKYVIGPKGNSLQEIubiquitination[1]
349ILRGEPEKLGQALTEubiquitination[1]
494PQGVQQAKRELLELAubiquitination[1, 4]
1031AANLDRAKAGLLERVubiquitination[1]
1039AGLLERVKELQAEQEubiquitination[1]
1240WTASSSEKAPDMSSSubiquitination[5]
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] 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] 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] 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] 
Functional Description
 Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol. 
Sequence Annotation
 DOMAIN 158 229 KH 1.
 DOMAIN 230 302 KH 2.
 DOMAIN 303 371 KH 3.
 DOMAIN 372 442 KH 4.
 DOMAIN 443 514 KH 5.
 DOMAIN 515 588 KH 6.
 DOMAIN 589 660 KH 7.
 DOMAIN 661 734 KH 8.
 DOMAIN 735 807 KH 9.
 DOMAIN 808 880 KH 10.
 DOMAIN 881 979 KH 11.
 DOMAIN 980 1059 KH 12.
 DOMAIN 1060 1134 KH 13.
 DOMAIN 1135 1209 KH 14.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 295 295 Phosphothreonine (Potential).
 MOD_RES 296 296 Phosphothreonine (Potential).
 MOD_RES 437 437 Phosphotyrosine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cholesterol metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; HDL; Lipid metabolism; Lipid transport; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Steroid metabolism; Sterol metabolism; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1268 AA 
Protein Sequence
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP 60
SGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA 120
KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVAIPKE HHRFVIGKNG EKLQDLELKT 180
ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP 240
YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV 300
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK 360
ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA 420
QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL 480
IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV 540
IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG 600
GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI 660
PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA 720
EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR VIFPAAEDKD QDLITIIGKE 780
DAVREAQKEL EALIQNLDNV VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS 840
GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT 900
RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI IIISGRKEKC 960
EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD EFEVNIHVPA PELQSDIIAI 1020
TGLAANLDRA KAGLLERVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL 1080
EHDVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA 1140
RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD 1200
VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF PSFGAQVAPK 1260
TLPWGPKR 1268 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0008289; F:lipid binding; TAS:ProtInc.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
 GO:0006869; P:lipid transport; IEA:UniProtKB-KW. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS