CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005998
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor HIVEP2 
Protein Synonyms/Alias
 Human immunodeficiency virus type I enhancer-binding protein 2; HIV-EP2; MHC-binding protein 2; MBP-2 
Gene Name
 HIVEP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
178EQAEEAHKKEHKPKKubiquitination[1]
332VPILIIPKSGIPLPNubiquitination[1, 2]
358PNPSLNTKADDSHTVubiquitination[1, 2]
366ADDSHTVKQKLALRLubiquitination[1]
368DSHTVKQKLALRLSEubiquitination[3]
428YEEIIFGKYCRLSPRubiquitination[4, 5]
453ERAAMGRKGIMEPLPubiquitination[1]
469VNTRLDVKMFEDPVSubiquitination[1]
482VSQLIPSKGDVDPSQubiquitination[1]
517SSIRNEGKLYPANFQubiquitination[1, 2]
655WEDSETPKQNYRDISubiquitination[1]
1455LELFMETKQQKRVKEubiquitination[3]
1745FGSKLERKLVGNILKubiquitination[3]
1752KLVGNILKERGKGDIubiquitination[3]
1783KIFEGGYKSNEDYVYubiquitination[3]
2092MRHLSPRKEAALRREubiquitination[5, 6]
2273ASGESFSKDPYVLSKubiquitination[2]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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
Functional Description
 This protein specifically binds to the DNA sequence 5'- GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon- beta genes. It may act in T-cell activation. 
Sequence Annotation
 REPEAT 2053 2056 1.
 REPEAT 2059 2062 2.
 REPEAT 2071 2074 3.
 REPEAT 2083 2086 4.
 REPEAT 2089 2092 5.
 REPEAT 2106 2109 6.
 REPEAT 2112 2115 7.
 REPEAT 2118 2121 8.
 REPEAT 2130 2133 9.
 REPEAT 2145 2148 10.
 ZN_FING 189 211 C2H2-type 1.
 ZN_FING 217 239 C2H2-type 2.
 ZN_FING 1799 1821 C2H2-type 3.
 ZN_FING 1827 1851 C2H2-type 4.
 REGION 2053 2148 10 X 4 AA tandem repeats of S-P-[RGMKC]-
 MOTIF 937 943 Nuclear localization signal (Potential).
 CROSSLNK 2092 2092 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2446 AA 
Protein Sequence
MDTGDTALGQ KATSRSGETD KASGRWRQEQ SAVIKMSTFG SHEGQRQPQI EPEQIGNTAS 60
AQLFGSGKLA SPSEVVQQVA EKQYPPHRPS PYSCQHSLSF PQHSLPQGVM HSTKPHQSLE 120
GPPWLFPGPL PSVASEDLFP FPIHGHSGGY PRKKISSLNP AYSQYSQKSI EQAEEAHKKE 180
HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA 240
HAIKAGLVPF TESAVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKMSPGPP 300
IPLDIASRGG YHGSLEESLG GPMKVPILII PKSGIPLPNE SSQYIGPDML PNPSLNTKAD 360
DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS 420
YEEIIFGKYC RLSPRNALSV TTTSQERAAM GRKGIMEPLP HVNTRLDVKM FEDPVSQLIP 480
SKGDVDPSQT SMLKSTKFNS ESRQPQIIPS SIRNEGKLYP ANFQGSNPVL LEAPVDSSPL 540
IRSNSVPTSS ATNLTIPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS 600
VQEGHVEVEH HGRMLKGISS SSLKEKKLSP GDRVGYDYDV CRKPYKKWED SETPKQNYRD 660
ISCLSSLKHG GEYFMDPVVP LQGVPSMFGT TCENRKRRKE KSVGDEEDTP MICSSIVSTP 720
VGIMASDYDP KLQMQEGVRS GFAMAGHENL SHGHTERFDP CRPQLQPGSP SLVSEESPSA 780
IDSDKMSDLG GRKPPGNVIS VIQHTNSLSR PNSFERSESA ELVACTQDKA PSPSETCDSE 840
ISEAPVSPEW APPGDGAESG GKPSPSQQVQ QQSYHTQPRL VRQHNIQVPE IRVTEEPDKP 900
EKEKEAQSKE PEKPVEEFQW PQRSETLSQL PAEKLPPKKK RLRLADMEHS SGESSFESTG 960
TGLSRSPSQE SNLSHSSSFS MSFEREETSK LSALPKQDEF GKHSEFLTVP AGSYSLSVPG 1020
HHHQKEMRRC SSEQMPCPHP AEVPEVRSKS FDYGNLSHAP VSGAAASTVS PSRERKKCFL 1080
VRQASFSGSP EISQGEVGMD QSVKQEQLEH LHAGLRSGWH HGPPAVLPPL QQEDPGKQVA 1140
GPCPPLSSGP LHLAQPQIMH MDSQESLRNP LIQPTSYMTS KHLPEQPHLF PHQETIPFSP 1200
IQNALFQFQY PTVCMVHLPA QQPPWWQAHF PHPFAQHPQK SYGKPSFQTE IHSSYPLEHV 1260
AEHTGKKPAE YAHTKEQTYP CYSGASGLHP KNLLPKFPSD QSSKSTETPS EQVLQEDFAS 1320
ANAGSLQSLP GTVVPVRIQT HVPSYGSVMY TSISQILGQN SPAIVICKVD ENMTQRTLVT 1380
NAAMQGIGFN IAQVLGQHAG LEKYPIWKAP QTLPLGLESS IPLCLPSTSD SVATLGGSKR 1440
MLSPASSLEL FMETKQQKRV KEEKMYGQIV EELSAVELTN SDIKKDLSRP QKPQLVRQGC 1500
ASEPKDGLQS GSSSFSSLSP SSSQDYPSVS PSSREPFLPS KEMLSGSRAP LPGQKSSGPS 1560
ESKESSDELD IDETASDMSM SPQSSSLPAG DGQLEEEGKG HKRPVGMLVR MASAPSGNVA 1620
DSTLLLTDMA DFQQILQFPS LRTTTTVSWC FLNYTKPNYV QQATFKSSVY ASWCISSCNP 1680
NPSGLNTKTT LALLRSKQKI TAEIYTLAAM HRPGTGKLTS SSAWKQFTQM KPDASFLFGS 1740
KLERKLVGNI LKERGKGDIH GDKDIGSKQT EPIRIKIFEG GYKSNEDYVY VRGRGRGKYI 1800
CEECGIRCKK PSMLKKHIRT HTDVRPYVCK LCNFAFKTKG NLTKHMKSKA HMKKCLELGV 1860
SMTSVDDTET EEAENLEDLH KAAEKHSMSS ISTDHQFSDA EESDGEDGDD NDDDDEDEDD 1920
FDDQGDLTPK TRSRSTSPQP PRFSSLPVNV GAVPHGVPSD SSLGHSSLIS YLVTLPSIRV 1980
TQLMTPSDSC EDTQMTEYQR LFQSKSTDSE PDKDRLDIPS CMDEECMLPS EPSSSPRDFS 2040
PSSHHSSPGY DSSPCRDNSP KRYLIPKGDL SPRRHLSPRR DLSPMRHLSP RKEAALRREM 2100
SQRDVSPRRH LSPRRPVSPG KDITARRDLS PRRERRYMTT IRAPSPRRAL YHNPPLSMGQ 2160
YLQAEPIVLG PPNLRRGLPQ VPYFSLYGDQ EGAYEHPGSS LFPEGPNDYV FSHLPLHSQQ 2220
QVRAPIPMVP VGGIQMVHSM PPALSSLHPS PTLPLPMEGF EEKKGASGES FSKDPYVLSK 2280
QHEKRGPHAL QSSGPPSTPS SPRLLMKQST SEDSLNATER EQEENIQTCT KAIASLRIAT 2340
EEAALLGPDQ PARVQEPHQN PLGSAHVSIR HFSRPEPGQP CTSATHPDLH DGEKDNFGTS 2400
QTPLAHSTFY SKSCVDDKQL DFHSSKELSS STEESKDPSS EKSQLH 2446 
Gene Ontology
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0003677; F:DNA binding; TAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
  
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS