CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002052
UniProt Accession
Genbank Protein ID
 K02013 
Genbank Nucleotide ID
  
Protein Name
 Gag-Pol polyprotein 
Protein Synonyms/Alias
 Pr160Gag-Pol; Matrix protein p17; MA; Capsid protein p24; CA; Spacer peptide p2; Nucleocapsid protein p7; NC; Transframe peptide; TF; p6-pol; p6*; Protease; PR; Retropepsin; Reverse transcriptase/ribonuclease H; Exoribonuclease H; p66 RT; p51 RT; p15; Integrase; IN 
Gene Name
 gag-pol 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Human immunodeficiency virus type 1 group M subtype B (isolat 
NCBI Taxa ID
 11686 
Lysine Modification
Position
Peptide
Type
References
1423IKVVPRRKAKIIRDYacetylation[1, 2]
1425VVPRRKAKIIRDYGKacetylation[1, 2]
1432KIIRDYGKQMAGDDCacetylation[2]
Reference
 [1] Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF.
 Brès V, Tagami H, Péloponèse JM, Loret E, Jeang KT, Nakatani Y, Emiliani S, Benkirane M, Kiernan RE.
 EMBO J. 2002 Dec 16;21(24):6811-9. [PMID: 12486002]
 [2] Acetylation of HIV-1 integrase by p300 regulates viral integration.
 Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M.
 EMBO J. 2005 Sep 7;24(17):3070-81. [PMID: 16096645] 
Functional Description
 Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity). 
Sequence Annotation
 DOMAIN 520 589 Peptidase A2.
 DOMAIN 643 833 Reverse transcriptase.
 DOMAIN 1033 1156 RNase H.
 DOMAIN 1213 1363 Integrase catalytic.
 ZN_FING 390 407 CCHC-type 1.
 ZN_FING 411 428 CCHC-type 2.
 ZN_FING 1162 1203 Integrase-type.
 DNA_BIND 1382 1429 Integrase-type.
 REGION 826 834 RT 'primer grip' (By similarity).
 MOTIF 16 22 Nuclear export signal (By similarity).
 MOTIF 26 32 Nuclear localization signal (By
 MOTIF 997 1013 Tryptophan repeat motif (By similarity).
 ACT_SITE 525 525 For protease activity; shared with
 METAL 709 709 Magnesium; catalytic; for reverse
 METAL 784 784 Magnesium; catalytic; for reverse
 METAL 785 785 Magnesium; catalytic; for reverse
 METAL 1042 1042 Magnesium; catalytic; for RNase H
 METAL 1077 1077 Magnesium; catalytic; for RNase H
 METAL 1097 1097 Magnesium; catalytic; for RNase H
 METAL 1148 1148 Magnesium; catalytic; for RNase H
 METAL 1223 1223 Magnesium; catalytic; for integrase
 METAL 1275 1275 Magnesium; catalytic; for integrase
 MOD_RES 132 132 Phosphotyrosine; by host (By similarity).
 LIPID 2 2 N-myristoyl glycine; by host (By  
Keyword
 3D-structure; Activation of host caspases by virus; AIDS; Aspartyl protease; Capsid maturation; Capsid protein; Complete proteome; DNA integration; DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease; Host cell membrane; Host cytoplasm; Host gene expression shutoff by virus; Host membrane; Host nucleus; Host translation shutoff by virus; Host-virus interaction; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; Modulation of host cell apoptosis by virus; Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease; Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase; Transferase; Viral genome integration; Viral nucleoprotein; Viral penetration into host nucleus; Virion; Virus entry into host cell; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1447 AA 
Protein Sequence
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI 60
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA 120
DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT 180
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT 240
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF 300
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA 360
RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH IARNCRAPRK KGCWKCGKEG 420
HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTI SSEQTRANSP TRRELQVWGR 480
DNNSLSEAGA DRQGTVSFNF PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG 540
RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP 600
ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF 660
AIKKKDSTKW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD 720
EDFRKYTAFT IPSINNETPG IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY 780
QYMDDLYVGS DLEIGQHRTK IEELRQHLLR WGLTTPDKKH QKEPPFLWMG YELHPDKWTV 840
QPIVLPEKDS WTVNDIQKLV GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL 900
ELAENREILK EPVHGVYYDP SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYARTRGAH 960
TNDVKQLTEA VQKITTESIV IWGKTPKFKL PIQKETWETW WTEYWQATWI PEWEFVNTPP 1020
LVKLWYQLEK EPIVGAETFY VDGAASRETK LGKAGYVTNR GRQKVVTLTD TTNQKTELQA 1080
IHLALQDSGL EVNIVTDSQY ALGIIQAQPD KSESELVNQI IEQLIKKEKV YLAWVPAHKG 1140
IGGNEQVDKL VSAGIRKVLF LDGIDKAQDE HEKYHSNWRA MASDFNLPPV VAKEIVASCD 1200
KCQLKGEAMH GQVDCSPGIW QLDCTHLEGK VILVAVHVAS GYIEAEVIPA ETGQETAYFL 1260
LKLAGRWPVK TIHTDNGSNF TSTTVKAACW WAGIKQEFGI PYNPQSQGVV ESMNKELKKI 1320
IGQVRDQAEH LKTAVQMAVF IHNFKRKGGI GGYSAGERIV DIIATDIQTK ELQKQITKIQ 1380
NFRVYYRDSR DPLWKGPAKL LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV 1440
ASRQDED 1447 
Gene Ontology
 GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
 GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
 GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
 GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0004533; F:exoribonuclease H activity; IEA:EC.
 GO:0004523; F:ribonuclease H activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
 GO:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0006278; P:RNA-dependent DNA replication; IEA:InterPro.
 GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
 GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
 GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW. 
Interpro
 IPR000721; Gag_p24.
 IPR001037; Integrase_C_retrovir.
 IPR001584; Integrase_cat-core.
 IPR017856; Integrase_Zn-bd_dom-like_N.
 IPR003308; Integrase_Zn-bd_dom_N.
 IPR000071; Lentvrl_matrix_N.
 IPR012344; Matrix_N_HIV/RSV.
 IPR018061; Pept_A2A_retrovirus_sg.
 IPR001995; Peptidase_A2_cat.
 IPR021109; Peptidase_aspartic.
 IPR001969; Peptidase_aspartic_AS.
 IPR008916; Retrov_capsid_C.
 IPR008919; Retrov_capsid_N.
 IPR010999; Retrovr_matrix_N.
 IPR012337; RNaseH-like_dom.
 IPR002156; RNaseH_domain.
 IPR000477; RVT.
 IPR010659; RVT_connect.
 IPR010661; RVT_thumb.
 IPR001878; Znf_CCHC. 
Pfam
 PF00540; Gag_p17
 PF00607; Gag_p24
 PF00552; IN_DBD_C
 PF02022; Integrase_Zn
 PF00075; RNase_H
 PF00665; rve
 PF00077; RVP
 PF00078; RVT_1
 PF06815; RVT_connect
 PF06817; RVT_thumb
 PF00098; zf-CCHC 
SMART
 SM00343; ZnF_C2HC 
PROSITE
 PS50175; ASP_PROT_RETROV
 PS00141; ASP_PROTEASE
 PS50994; INTEGRASE
 PS51027; INTEGRASE_DBD
 PS50879; RNASE_H
 PS50878; RT_POL
 PS50158; ZF_CCHC
 PS50876; ZF_INTEGRASE 
PRINTS
 PR00234; HIV1MATRIX.