CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003781
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Androgen receptor 
Protein Synonyms/Alias
 Dihydrotestosterone receptor; Nuclear receptor subfamily 3 group C member 4 
Gene Name
 AR 
Gene Synonyms/Alias
 DHTR; NR3C4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
386PHPHARIKLENPLDYsumoylation[1, 2, 3, 4]
520YPSPTCVKSEMGPWMsumoylation[1, 2, 3, 4]
630GMTLGARKLKKLGNLacetylation[5, 6, 7]
630GMTLGARKLKKLGNLmethylation[8]
632TLGARKLKKLGNLKLacetylation[5, 6, 7]
632TLGARKLKKLGNLKLmethylation[9]
633LGARKLKKLGNLKLQacetylation[5, 6, 7]
845LDRIIACKRKNPTSCubiquitination[10]
847RIIACKRKNPTSCSRubiquitination[10]
Reference
 [1] Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1).
 Poukka H, Karvonen U, Janne OA, Palvimo JJ.
 Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14145-50. [PMID: 11121022]
 [2] PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription.
 Nishida T, Yasuda H.
 J Biol Chem. 2002 Nov 1;277(44):41311-7. [PMID: 12177000]
 [3] Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements.
 Callewaert L, Verrijdt G, Haelens A, Claessens F.
 Mol Endocrinol. 2004 Jun;18(6):1438-49. [PMID: 15031320]
 [4] Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation.
 Mukherjee S, Thomas M, Dadgar N, Lieberman AP, Iñiguez-Lluhí JA.
 J Biol Chem. 2009 Aug 7;284(32):21296-306. [PMID: 19497852]
 [5] p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation.
 Fu M, Wang C, Reutens AT, Wang J, Angeletti RH, Siconolfi-Baez L, Ogryzko V, Avantaggiati ML, Pestell RG.
 J Biol Chem. 2000 Jul 7;275(27):20853-60. [PMID: 10779504]
 [6] Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function.
 Fu M, Wang C, Wang J, Zhang X, Sakamaki T, Yeung YG, Chang C, Hopp T, Fuqua SA, Jaffray E, Hay RT, Palvimo JJ, Jänne OA, Pestell RG.
 Mol Cell Biol. 2002 May;22(10):3373-88. [PMID: 11971970]
 [7] Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor.
 Gaughan L, Logan IR, Cook S, Neal DE, Robson CN.
 J Biol Chem. 2002 Jul 19;277(29):25904-13. [PMID: 11994312]
 [8] Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase.
 Ko S, Ahn J, Song CS, Kim S, Knapczyk-Stwora K, Chatterjee B.
 Mol Endocrinol. 2011 Mar;25(3):433-44. [PMID: 21273441]
 [9] Regulation of the androgen receptor by SET9-mediated methylation.
 Gaughan L, Stockley J, Wang N, McCracken SR, Treumann A, Armstrong K, Shaheen F, Watt K, McEwan IJ, Wang C, Pestell RG, Robson CN.
 Nucleic Acids Res. 2011 Mar;39(4):1266-79. [PMID: 20959290]
 [10] 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
 Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. 
Sequence Annotation
 DNA_BIND 559 631 Nuclear receptor.
 ZN_FING 559 579 NR C4-type.
 ZN_FING 595 619 NR C4-type.
 REGION 1 558 Modulating.
 REGION 551 919 Interaction with LPXN.
 REGION 571 661 Interaction with HIPK3 (By similarity).
 REGION 624 919 Interaction with KAT7.
 REGION 690 919 Ligand-binding.
 BINDING 705 705 Androgen.
 BINDING 752 752 Androgen.
 BINDING 877 877 Androgen.
 MOD_RES 81 81 Phosphoserine; by CDK9.
 MOD_RES 94 94 Phosphoserine.
 MOD_RES 223 223 Phosphotyrosine; by CSK.
 MOD_RES 267 267 Phosphotyrosine; by CSK and TNK2.
 MOD_RES 307 307 Phosphotyrosine; by CSK.
 MOD_RES 346 346 Phosphotyrosine; by CSK.
 MOD_RES 357 357 Phosphotyrosine; by CSK.
 MOD_RES 362 362 Phosphotyrosine; by CSK.
 MOD_RES 363 363 Phosphotyrosine; by CSK and TNK2.
 MOD_RES 393 393 Phosphotyrosine; by CSK.
 MOD_RES 534 534 Phosphotyrosine; by CSK.
 MOD_RES 551 551 Phosphotyrosine; by CSK.
 MOD_RES 650 650 Phosphoserine; by STK4/MST1.
 MOD_RES 915 915 Phosphotyrosine; by CSK.
 CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 520 520 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 845 845 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 847 847 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Activator; Alternative splicing; Complete proteome; Cytoplasm; Disease mutation; DNA-binding; Isopeptide bond; Lipid-binding; Lipoprotein; Metal-binding; Neurodegeneration; Nucleus; Palmitate; Phosphoprotein; Polymorphism; Pseudohermaphroditism; Receptor; Reference proteome; Steroid-binding; Transcription; Transcription regulation; Triplet repeat expansion; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 919 AA 
Protein Sequence
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ 60
QQQQQQQQQQ QQQQQQQQET SPRQQQQQQG EDGSPQAHRR GPTGYLVLDE EQQPSQPQSA 120
LECHPERGCV PEPGAAVAAS KGLPQQLPAP PDEDDSAAPS TLSLLGPTFP GLSSCSADLK 180
DILSEASTMQ LLQQQQQEAV SEGSSSGRAR EASGAPTSSK DNYLGGTSTI SDNAKELCKA 240
VSVSMGLGVE ALEHLSPGEQ LRGDCMYAPL LGVPPAVRPT PCAPLAECKG SLLDDSAGKS 300
TEDTAEYSPF KGGYTKGLEG ESLGCSGSAA AGSSGTLELP STLSLYKSGA LDEAAAYQSR 360
DYYNFPLALA GPPPPPPPPH PHARIKLENP LDYGSAWAAA AAQCRYGDLA SLHGAGAAGP 420
GSGSPSAAAS SSWHTLFTAE EGQLYGPCGG GGGGGGGGGG GGGGGGGGGG GGEAGAVAPY 480
GYTRPPQGLA GQESDFTAPD VWYPGGMVSR VPYPSPTCVK SEMGPWMDSY SGPYGDMRLE 540
TARDHVLPID YYFPPQKTCL ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND 600
CTIDKFRRKN CPSCRLRKCY EAGMTLGARK LKKLGNLKLQ EEGEASSTTS PTEETTQKLT 660
VSHIEGYECQ PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK 720
ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM 780
YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR 840
IIACKRKNPT SCSRRFYQLT KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS 900
VQVPKILSGK VKPIYFHTQ 919 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0005497; F:androgen binding; NAS:UniProtKB.
 GO:0004882; F:androgen receptor activity; IDA:UniProtKB.
 GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0016049; P:cell growth; NAS:UniProtKB.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0007267; P:cell-cell signaling; TAS:ProtInc.
 GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IEA:Compara.
 GO:0048808; P:male genitalia morphogenesis; IEA:Compara.
 GO:0008584; P:male gonad development; IEA:Compara.
 GO:0019102; P:male somatic sex determination; IEA:Compara.
 GO:0060749; P:mammary gland alveolus development; IEA:Compara.
 GO:0060571; P:morphogenesis of an epithelial fold; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
 GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Compara.
 GO:0045720; P:negative regulation of integrin biosynthetic process; IDA:BHF-UCL.
 GO:0048645; P:organ formation; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
 GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Compara.
 GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
 GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Compara.
 GO:0043410; P:positive regulation of MAPK cascade; IEA:Compara.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
 GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:BHF-UCL.
 GO:0030850; P:prostate gland development; NAS:UniProtKB.
 GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Compara.
 GO:0060736; P:prostate gland growth; IEA:Compara.
 GO:0051259; P:protein oligomerization; IDA:MGI.
 GO:0050790; P:regulation of catalytic activity; IEA:Compara.
 GO:0048638; P:regulation of developmental growth; IEA:Compara.
 GO:0090003; P:regulation of establishment of protein localization to plasma membrane; IDA:BHF-UCL.
 GO:0060685; P:regulation of prostatic bud formation; IEA:Compara.
 GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Compara.
 GO:0032868; P:response to insulin stimulus; IEA:Compara.
 GO:0007548; P:sex differentiation; NAS:UniProtKB.
 GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006810; P:transport; TAS:ProtInc. 
Interpro
 IPR001103; Andrgn_rcpt.
 IPR008946; Nucl_hormone_rcpt_ligand-bd.
 IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
 IPR001628; Znf_hrmn_rcpt.
 IPR013088; Znf_NHR/GATA. 
Pfam
 PF02166; Androgen_recep
 PF00104; Hormone_recep
 PF00105; zf-C4 
SMART
 SM00430; HOLI
 SM00399; ZnF_C4 
PROSITE
 PS00031; NUCLEAR_REC_DBD_1
 PS51030; NUCLEAR_REC_DBD_2 
PRINTS
 PR00521; ANDROGENR.
 PR00047; STROIDFINGER.