CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004379
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 40 
Protein Synonyms/Alias
 Cirhin interaction protein; CIRIP; Gate keeper of apoptosis-activating protein; GAAP; Human immunodeficiency virus type I enhancer-binding protein 1; HIV-EP1; Major histocompatibility complex-binding protein 1; MBP-1; Positive regulatory domain II-binding factor 1; PRDII-BF1 
Gene Name
 HIVEP1 
Gene Synonyms/Alias
 ZNF40 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
594LSSAQKQKDLQVTNVubiquitination[1]
625TNENSHQKGDMNPLEubiquitination[1]
634DMNPLEGKQDSHVGTubiquitination[1]
661YSQEQQGKLLSPRSLubiquitination[1, 2, 3, 4, 5]
742MRPPLATKTLEERISubiquitination[1]
750TLEERISKLISDNEAubiquitination[1]
797DSFQFDLKPVGRRTSubiquitination[1, 4]
1259HDQEKSEKFSWPQRSubiquitination[4]
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] 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]
 [4] 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]
 [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] 
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 HIV-1. 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, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis. 
Sequence Annotation
 ZN_FING 406 428 C2H2-type 1.
 ZN_FING 434 456 C2H2-type 2.
 ZN_FING 959 986 C2H2-type 3.
 ZN_FING 2088 2110 C2H2-type 4.
 ZN_FING 2116 2140 C2H2-type 5.
 MOD_RES 429 429 Phosphothreonine.
 MOD_RES 492 492 Phosphoserine.
 MOD_RES 495 495 Phosphoserine.
 MOD_RES 1036 1036 Phosphoserine.
 MOD_RES 1735 1735 Phosphoserine.
 MOD_RES 1749 1749 Phosphoserine.
 MOD_RES 1753 1753 Phosphoserine.  
Keyword
 3D-structure; Activator; Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2718 AA 
Protein Sequence
MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEILQAGVKG TSESLKGVKR KKIVAENHLK 60
KIPKSPLRNP LQAKHKQNTE ESSFAVLHSA SESHKKQNYI PVKNGKQFTK QNGETPGIIA 120
EASKSEESVS PKKPLFLQQP SELRRWRSEG ADPAKFSDLD EQCDSSSLSS KTRTDNSECI 180
SSHCGTTSPS YTNTAFDVLL KAMEPELSTL SQKGSPCAIK TEKLRPNKTA RSPPKLKNSS 240
MDAPNQTSQE LVAESQSSCT SYTVHMSAAQ KNEQGAMQSA SHLYHQHEHF VPKSNQHNQQ 300
LPGCSGFTGS LTNLQNQENA KLEQVYNIAV TSSVGLTSPS SRSQVTPQNQ QMDSASPLSI 360
SPANSTQSPP MPIYNSTHVA SVVNQSVEQM CNLLLKDQKP KKQGKYICEY CNRACAKPSV 420
LLKHIRSHTG ERPYPCVTCG FSFKTKSNLY KHKKSHAHTI KLGLVLQPDA GGLFLSHESP 480
KALSIHSDVE DSGESEEEGA TDERQHDLGA MELQPVHIIK RMSNAETLLK SSFTPSSPEN 540
VIGDFLLQDR SAESQAVTEL PKVVVHHVTV SPLRTDSPKA MDPKPELSSA QKQKDLQVTN 600
VQPLSANMSQ GGVSRLETNE NSHQKGDMNP LEGKQDSHVG TVHAQLQRQQ ATDYSQEQQG 660
KLLSPRSLGS TDSGYFSRSE SADQTVSPPT PFARRLPSTE QDSGRSNGPS AALVTTSTPS 720
ALPTGEKALL LPGQMRPPLA TKTLEERISK LISDNEALVD DKQLDSVKPR RTSLSRRGSI 780
DSPKSYIFKD SFQFDLKPVG RRTSSSSDIP KSPFTPTEKS KQVFLLSVPS LDCLPITRSN 840
SMPTTGYSAV PANIIPPPHP LRGSQSFDDK IGTFYDDVFV SGPNAPVPQS GHPRTLVRQA 900
AIEDSSANES HVLGTGQSLD ESHQGCHAAG EAMSVRSKAL AQGPHIEKKK SHQGRGTMFE 960
CETCRNRYRK LENFENHKKF YCSELHGPKT KVAMREPEHS PVPGGLQPQI LHYRVAGSSG 1020
IWEQTPQIRK RRKMKSVGDD EELQQNESGT SPKSSEGLQF QNALGCNPSL PKHNVTIRSD 1080
QQHKNIQLQN SHIHLVARGP EQTMDPKLST IMEQQISSAA QDKIELQRHG TGISVIQHTN 1140
SLSRPNSFDK PEPFERASPV SFQELNRTGK SGSLKVIGIS QEESHPSRDG SHPHQLALSD 1200
ALRGELQESS RKSPSERHVL GQPSRLVRQH NIQVPEILVT EEPDRDLEAQ CHDQEKSEKF 1260
SWPQRSETLS KLPTEKLPPK KKRLRLAEIE HSSTESSFDS TLSRSLSRES SLSHTSSFSA 1320
SLDIEDVSKT EASPKIDFLN KAEFLMIPAG LNTLNVPGCH REMRRTASEQ INCTQTSMEV 1380
SDLRSKSFDC GSITPPQTTP LTELQPPSSP SRVGVTGHVP LLERRRGPLV RQISLNIAPD 1440
SHLSPVHPTS FQNTALPSVN AVPYQGPQLT STSLAEFSAN TLHSQTQVKD LQAETSNSSS 1500
TNVFPVQQLC DINLLNQIHA PPSHQSTQLS LQVSTQGSKP DKNSVLSGSS KSEDCFAPKY 1560
QLHCQVFTSG PSCSSNPVHS LPNQVISDPV GTDHCVTSAT LPTKLIDSMS NSHPLLPPEL 1620
RPLGSQVQKV PSSFMLPIRL QSSVPAYCFA TLTSLPQILV TQDLPNQPIC QTNHSVVPIS 1680
EEQNSVPTLQ KGHQNALPNP EKEFLCENVF SEMSQNSSLS ESLPITQKIS VGRLSPQQES 1740
SASSKRMLSP ANSLDIAMEK HQKRAKDENG AVCATDVRPL EALSSRVNEA SKQKKPILVR 1800
QVCTTEPLDG VMLEKDVFSQ PEISNEAVNL TNVLPADNSS TGCSKFVVIE PISELQEFEN 1860
IKSSTSLTLT VRSSPAPSEN THISPLKCTD NNQERKSPGV KNQGDKVNIQ EQSQQPVTSL 1920
SLFNIKDTQQ LAFPSLKTTT NFTWCYLLRQ KSLHLPQKDQ KTSAYTDWTV SASNPNPLGL 1980
PTKVALALLN SKQNTGKSLY CQAITTHSKS DLLVYSSKWK SSLSKRALGN QKSTVVEFSN 2040
KDASEINSEQ DKENSLIKSE PRRIKIFDGG YKSNEEYVYV RGRGRGKYIC EECGIRCKKP 2100
SMLKKHIRTH TDVRPYHCTY CNFSFKTKGN LTKHMKSKAH SKKCVDLGVS VGLIDEQDTE 2160
ESDEKQRFSY ERSGYDLEES DGPDEDDNEN EDDDEDSQAE SVLSATPSVT ASPQHLPSRS 2220
SLQDPVSTDE DVRITDCFSG VHTDPMDVLP RALLTRMTVL STAQSDYNRK TLSPGKARQR 2280
AARDENDTIP SVDTSRSPCH QMSVDYPESE EILRSSMAGK AVAITQSPSS VRLPPAAAEH 2340
SPQTAAGMPS VASPHPDPQE QKQQITLQPT PGLPSPHTHL FSHLPLHSQQ QSRTPYNMVP 2400
VGGIHVVPAG LTYSTFVPLQ AGPVQLTIPA VSVVHRTLGT HRNTVTEVSG TTNPAGVAEL 2460
SSVVPCIPIG QIRVPGLQNL STPGLQSLPS LSMETVNIVG LANTNMAPQV HPPGLALNAV 2520
GLQVLTANPS SQSSPAPQAH IPGLQILNIA LPTLIPSVSQ VAVDAQGAPE MPASQSKACE 2580
TQPKQTSVAS ANQVSRTESP QGLPTVQREN AKKVLNPPAP AGDHARLDGL SKMDTEKAAS 2640
ANHVKPKPEL TSIQGQPAST SQPLLKAHSE VFTKPSGQQT LSPDRQVPRP TALPRRQPTV 2700
HFSDVSSDDD EDRLVIAT 2718 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 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