ANDR_HUMAN - dbPTM
ANDR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANDR_HUMAN
UniProt AC P10275
Protein Name Androgen receptor
Gene Name AR
Organism Homo sapiens (Human).
Sequence Length 920
Subcellular Localization Nucleus . Cytoplasm . Detected at the promoter of target genes (PubMed:25091737). Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence o
Protein 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.; Isoform 3 and isoform 4 lack the C-terminal ligand-binding domain and may therefore constitutively activate the transcription of a specific set of genes independently of steroid hormones..
Protein Sequence MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
11PhosphorylationQLGLGRVYPRPPSKT
EECCCCCCCCCCCCC
7.6825002506
16PhosphorylationRVYPRPPSKTYRGAF
CCCCCCCCCCHHHHH
40.0712015328
18PhosphorylationYPRPPSKTYRGAFQN
CCCCCCCCHHHHHHH
23.8425002506
19PhosphorylationPRPPSKTYRGAFQNL
CCCCCCCHHHHHHHH
15.7025002506
29PhosphorylationAFQNLFQSVREVIQN
HHHHHHHHHHHHHHC
18.7927499020
81PhosphorylationQQQQQQQETSPRQQQ
HHHHHHHHCCHHHHH
19.8212015328
83PhosphorylationQQQQQETSPRQQQQQ
HHHHHHCCHHHHHHH
46.8612015328
94PhosphorylationQQQQQGEDGSPQAHR
HHHHHCCCCCCCHHH
26.5920363803
96PhosphorylationQQQGEDGSPQAHRRG
HHHCCCCCCCHHHCC
52.0430278072
119PhosphorylationEEQQPSQPQSALECH
CCCCCCCCCHHHHHC
41.3112015328
121PhosphorylationQQPSQPQSALECHPE
CCCCCCCHHHHHCCC
9.7512015328
142PhosphorylationPGAAVAASKGLPQQL
CCHHHHHHCCCCCCC
39.8426546556
206PhosphorylationQEAVSEGSSSGRARE
HHHHHHCCCCHHHHC
33.7111404460
208PhosphorylationAVSEGSSSGRAREAS
HHHHCCCCHHHHCCC
32.2111404460
213PhosphorylationSSSGRAREASGAPTS
CCCHHHHCCCCCCCC
30.6322155408
215PhosphorylationSGRAREASGAPTSSK
CHHHHCCCCCCCCCC
11.1611404460
217PhosphorylationRAREASGAPTSSKDN
HHHCCCCCCCCCCCC
45.13-
219PhosphorylationREASGAPTSSKDNYL
HCCCCCCCCCCCCCC
46.65-
223PhosphorylationGAPTSSKDNYLGGTS
CCCCCCCCCCCCCCC
19.5019060867
225PhosphorylationPTSSKDNYLGGTSTI
CCCCCCCCCCCCCCC
27.2919060867
231PhosphorylationNYLGGTSTISDNAKE
CCCCCCCCCCHHHHH
25.54-
233PhosphorylationLGGTSTISDNAKELC
CCCCCCCCHHHHHHH
46.23-
242PhosphorylationNAKELCKAVSVSMGL
HHHHHHHHHHHHCCC
17.21-
244PhosphorylationKELCKAVSVSMGLGV
HHHHHHHHHHCCCCH
10.30-
246PhosphorylationLCKAVSVSMGLGVEA
HHHHHHHHCCCCHHH
16.27-
256PhosphorylationLGVEALEHLSPGEQL
CCHHHHHHCCCCCCC
32.5412015328
258PhosphorylationVEALEHLSPGEQLRG
HHHHHHCCCCCCCCC
31.7212015328
267PhosphorylationGEQLRGDCMYAPLLG
CCCCCCCCCCHHHCC
16.0520623637
269PhosphorylationQLRGDCMYAPLLGVP
CCCCCCCCHHHCCCC
15.6120623637
280PhosphorylationLGVPPAVRPTPCAPL
CCCCCCCCCCCCCCH
22.0420713353
282PhosphorylationVPPAVRPTPCAPLAE
CCCCCCCCCCCCHHH
7.2020713353
291PhosphorylationCAPLAECKGSLLDDS
CCCHHHCCCCCCCCC
15.9720713353
293PhosphorylationPLAECKGSLLDDSAG
CHHHCCCCCCCCCCC
8.0220713353
298PhosphorylationKGSLLDDSAGKSTED
CCCCCCCCCCCCCCC
28.5327251275
300PhosphorylationSLLDDSAGKSTEDTA
CCCCCCCCCCCCCCH
35.7912015328
301PhosphorylationLLDDSAGKSTEDTAE
CCCCCCCCCCCCCHH
41.1719369195
302PhosphorylationLDDSAGKSTEDTAEY
CCCCCCCCCCCCHHC
61.5312015328
303PhosphorylationDDSAGKSTEDTAEYS
CCCCCCCCCCCHHCC
51.8319369195
307PhosphorylationGKSTEDTAEYSPFKG
CCCCCCCHHCCCCCC
21.1219369195
308PhosphorylationKSTEDTAEYSPFKGG
CCCCCCHHCCCCCCC
18.5012015328
309PhosphorylationSTEDTAEYSPFKGGY
CCCCCHHCCCCCCCC
33.7819369195
310PhosphorylationTEDTAEYSPFKGGYT
CCCCHHCCCCCCCCC
10.6412015328
328PhosphorylationEGESLGCSGSAAAGS
CCCCCCCCCCCCCCC
9.8427251275
330PhosphorylationESLGCSGSAAAGSSG
CCCCCCCCCCCCCCC
17.6627251275
335PhosphorylationSGSAAAGSSGTLELP
CCCCCCCCCCCEECC
35.7027251275
336PhosphorylationGSAAAGSSGTLELPS
CCCCCCCCCCEECCC
21.0022210691
338PhosphorylationAAAGSSGTLELPSTL
CCCCCCCCEECCCHH
59.4827251275
346PhosphorylationLELPSTLSLYKSGAL
EECCCHHHHHHCCCC
10.3417045208
348PhosphorylationLPSTLSLYKSGALDE
CCCHHHHHHCCCCCH
18.7517045208
357PhosphorylationSGALDEAAAYQSRDY
CCCCCHHHHHCCCCC
11.4217045208
359PhosphorylationALDEAAAYQSRDYYN
CCCHHHHHCCCCCCC
17.9117045208
362PhosphorylationEAAAYQSRDYYNFPL
HHHHHCCCCCCCCCH
10.1317045208
363PhosphorylationAAAYQSRDYYNFPLA
HHHHCCCCCCCCCHH
18.0217494760
364PhosphorylationAAYQSRDYYNFPLAL
HHHCCCCCCCCCHHH
26.3227642862
365PhosphorylationAYQSRDYYNFPLALA
HHCCCCCCCCCHHHC
2.7917494760
386SumoylationPPPHPHARIKLENPL
CCCCCCCCCCCCCCC
44.16-
386SumoylationPPPHPHARIKLENPL
CCCCCCCCCCCCCCC
44.16-
388SumoylationPHPHARIKLENPLDY
CCCCCCCCCCCCCCH
52.37-
388SumoylationPHPHARIKLENPLDY
CCCCCCCCCCCCCCH
52.3711121022
393PhosphorylationRIKLENPLDYGSAWA
CCCCCCCCCHHHHHH
22.2117045208
395PhosphorylationKLENPLDYGSAWAAA
CCCCCCCHHHHHHHH
17.8917045208
405PhosphorylationAWAAAAAQCRYGDLA
HHHHHHHHCHHCCHH
26.79-
407PhosphorylationAAAAAQCRYGDLASL
HHHHHHCHHCCHHHH
12.24-
422PhosphorylationHGAGAAGPGSGSPSA
CCCCCCCCCCCCCCH
38.9512015328
424PhosphorylationAGAAGPGSGSPSAAA
CCCCCCCCCCCCHHH
19.8512015328
426PhosphorylationAAGPGSGSPSAAASS
CCCCCCCCCCHHHCC
32.0312015328
503PhosphorylationDFTAPDVWYPGGMVS
CCCCCCCCCCCCCCC
7.5819369195
504PhosphorylationFTAPDVWYPGGMVSR
CCCCCCCCCCCCCCC
19.7019369195
515PhosphorylationMVSRVPYPSPTCVKS
CCCCCCCCCCCCCCC
27.3118511414
516PhosphorylationVSRVPYPSPTCVKSE
CCCCCCCCCCCCCCC
25.8822985185
518PhosphorylationRVPYPSPTCVKSEMG
CCCCCCCCCCCCCCC
4.0528348404
520SumoylationPYPSPTCVKSEMGPW
CCCCCCCCCCCCCCC
42.73-
520SumoylationPYPSPTCVKSEMGPW
CCCCCCCCCCCCCCC
42.73-
521SumoylationYPSPTCVKSEMGPWM
CCCCCCCCCCCCCCC
16.65-
521SumoylationYPSPTCVKSEMGPWM
CCCCCCCCCCCCCCC
16.6511121022
534PhosphorylationWMDSYSGPYGDMRLE
CCCCCCCCCCCCCHH
29.3220383201
535PhosphorylationMDSYSGPYGDMRLET
CCCCCCCCCCCCHHH
25.9320383201
551PhosphorylationRDHVLPIDYYFPPQK
HHCCCCCCEECCCCC
14.0217045208
552PhosphorylationDHVLPIDYYFPPQKT
HCCCCCCEECCCCCE
13.0817045208
578PhosphorylationHYGALTCGSCKVFFK
CCCEECCCCCCEEEH
16.9518511414
579PhosphorylationYGALTCGSCKVFFKR
CCEECCCCCCEEEHH
2.3618511414
606AcetylationRNDCTIDKFRRKNCP
CCCCCHHHHHHHCCC
8.95118298201
619AcetylationCPSCRLRKCYEAGMT
CCCCCHHHHHHHCCH
2.76118298199
630AcetylationAGMTLGARKLKKLGN
HCCHHHHHHHHHHCC
65.21-
630MethylationAGMTLGARKLKKLGN
HCCHHHHHHHHHHCC
65.21-
631AcetylationGMTLGARKLKKLGNL
CCHHHHHHHHHHCCC
5.0111971970
631MethylationGMTLGARKLKKLGNL
CCHHHHHHHHHHCCC
5.0121273441
632AcetylationMTLGARKLKKLGNLK
CHHHHHHHHHHCCCC
49.33-
632MethylationMTLGARKLKKLGNLK
CHHHHHHHHHHCCCC
49.33-
633AcetylationTLGARKLKKLGNLKL
HHHHHHHHHHCCCCC
72.5511994312
633MethylationTLGARKLKKLGNLKL
HHHHHHHHHHCCCCC
72.5520959290
634AcetylationLGARKLKKLGNLKLQ
HHHHHHHHHCCCCCC
5.4111971970
647PhosphorylationLQEEGEASSTTSPTE
CCCCCCCCCCCCCCH
42.6328450419
648PhosphorylationQEEGEASSTTSPTEE
CCCCCCCCCCCCCHH
28.8824719451
649PhosphorylationEEGEASSTTSPTEET
CCCCCCCCCCCCHHH
34.3624719451
650PhosphorylationEGEASSTTSPTEETT
CCCCCCCCCCCHHHH
29.8825849741
651PhosphorylationGEASSTTSPTEETTQ
CCCCCCCCCCHHHHC
41.5625849741
653PhosphorylationASSTTSPTEETTQKL
CCCCCCCCHHHHCEE
57.6525072903
656PhosphorylationTTSPTEETTQKLTVS
CCCCCHHHHCEEEHH
27.3025072903
657PhosphorylationTSPTEETTQKLTVSH
CCCCHHHHCEEEHHH
46.2925072903
761MethylationSFTNVNSRMLYFAPD
HCCCCCCCEEECCCH
3.41-
791PhosphorylationQCVRMRHLSQEFGWL
HHHHHHHHHHHHCCC
22.8711404460
792PhosphorylationCVRMRHLSQEFGWLQ
HHHHHHHHHHHCCCC
57.2911404460
826UbiquitinationVDGLKNQKFFDELRM
CCCCCCCHHHHHHHH
7.22-
837AcetylationELRMNYIKELDRIIA
HHHHHHHHHHHHHHC
46.477367661
845UbiquitinationELDRIIACKRKNPTS
HHHHHHCCCCCCCCC
58.3419345326
846UbiquitinationLDRIIACKRKNPTSC
HHHHHCCCCCCCCCH
43.82PubMed
847UbiquitinationDRIIACKRKNPTSCS
HHHHCCCCCCCCCHH
53.4219345326
848UbiquitinationRIIACKRKNPTSCSR
HHHCCCCCCCCCHHH
49.46PubMed
850PhosphorylationIACKRKNPTSCSRRF
HCCCCCCCCCHHHHH
52.3222584579
851PhosphorylationACKRKNPTSCSRRFY
CCCCCCCCCHHHHHH
16.0222584579
857PhosphorylationPTSCSRRFYQLTKLL
CCCHHHHHHHHHHHH
10.78-
858PhosphorylationTSCSRRFYQLTKLLD
CCHHHHHHHHHHHHH
39.69-
915PhosphorylationLSGKVKPIYFHTQ--
HCCCCEEEEEECC--
9.6117045208
916PhosphorylationSGKVKPIYFHTQ---
CCCCEEEEEECC---
5.3510221692

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
81SPhosphorylationKinaseCDK9P50750
GPS
83SPhosphorylationKinaseCDK1P06493
PSP
83SPhosphorylationKinaseCDK5Q00535
PSP
83SPhosphorylationKinaseCDK9P50750
Uniprot
96SPhosphorylationKinaseCDK2P24941
PSP
213SPhosphorylationKinasePKB_GROUP-PhosphoELM
213SPhosphorylationKinaseAKT-FAMILY-GPS
215SPhosphorylationKinaseAKT1P31749
PSP
215SPhosphorylationKinasePIM1P11309
PSP
223YPhosphorylationKinaseCSKP41240
GPS
225YPhosphorylationKinaseFERP16591
PSP
225YPhosphorylationKinaseCSKP41240
Uniprot
267YPhosphorylationKinaseCSKP41240
GPS
269YPhosphorylationKinaseACKQ07912
PSP
269YPhosphorylationKinaseCSKP41240
Uniprot
282TPhosphorylationKinaseAURKAO14965
GPS
293SPhosphorylationKinaseAURKAO14965
GPS
307YPhosphorylationKinaseCSKP41240
GPS
309YPhosphorylationKinaseCSKP41240
Uniprot
310SPhosphorylationKinaseCDK1P06493
PSP
310SPhosphorylationKinaseCDK11BP21127
PSP
310SPhosphorylationKinaseCDK5Q00535
PSP
346YPhosphorylationKinaseCSKP41240
GPS
348YPhosphorylationKinaseCSKP41240
Uniprot
357YPhosphorylationKinaseCSKP41240
GPS
359YPhosphorylationKinaseCSKP41240
Uniprot
362YPhosphorylationKinaseCSKP41240
GPS
363YPhosphorylationKinaseCSKP41240
GPS
364YPhosphorylationKinaseCSKP41240
Uniprot
365YPhosphorylationKinaseCSKP41240
Uniprot
365YPhosphorylationKinaseACKQ07912
PSP
393YPhosphorylationKinaseCSKP41240
GPS
395YPhosphorylationKinaseCSKP41240
Uniprot
516SPhosphorylationKinaseMAPK3P27361
GPS
516SPhosphorylationKinaseMAPK1P28482
GPS
516SPhosphorylationKinaseCDK7P50613
PSP
516SPhosphorylationKinaseCDK1P06493
PSP
534YPhosphorylationKinaseCSKP41240
GPS
535YPhosphorylationKinaseCSKP41240
Uniprot
535YPhosphorylationKinaseSRCP12931
PSP
551YPhosphorylationKinaseCSKP41240
GPS
552YPhosphorylationKinaseCSKP41240
Uniprot
579SPhosphorylationKinasePRKCAP17252
GPS
579SPhosphorylationKinasePAK6Q9NQU5
PSP
650SPhosphorylationKinaseSTK4Q13043
GPS
651SPhosphorylationKinaseMST1P26927
Uniprot
651SPhosphorylationKinaseMAPK14Q16539
GPS
651SPhosphorylationKinaseMAPK8P45983
GPS
651SPhosphorylationKinaseMAPK3P27361
GPS
791SPhosphorylationKinaseAKT-FAMILY-GPS
791SPhosphorylationKinasePKB_GROUP-PhosphoELM
792SPhosphorylationKinaseAKT1P31749
PSP
851TPhosphorylationKinasePIM1P11309
PSP
915YPhosphorylationKinaseCSKP41240
GPS
916YPhosphorylationKinaseCSKP41240
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:12559985
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRNF6Q9Y252
PMID:14559117
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:18703514
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:24508459:25274033
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:23518348

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
6Kubiquitylation

1424203
83SPhosphorylation

20980437
388KSumoylation

11121022
521KSumoylation

11121022

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ANDR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RACK1_HUMANGNB2L1physical
12958311
FLNA_HUMANFLNAphysical
12682292
RAN_HUMANRANphysical
10400640
NR2C2_HUMANNR2C2physical
10611280
NCOA3_HUMANNCOA3physical
10965917
RNF4_HUMANRNF4physical
9710597
RNF4_HUMANRNF4physical
10617653
NCOA4_HUMANNCOA4physical
9892017
NCOA4_HUMANNCOA4physical
8643607
PAK6_HUMANPAK6physical
11278661
ZN363_HUMANRCHY1physical
12200228
PIAS2_HUMANPIAS2physical
11117529
PIAS2_HUMANPIAS2physical
9920921
HNF4A_HUMANHNF4Aphysical
12944908
IL6RB_HUMANIL6STphysical
15129430
SMAD3_HUMANSMAD3physical
11707452
CCNH_HUMANCCNHphysical
10734072
CDK7_HUMANCDK7physical
10734072
ANDR_HUMANARphysical
15525515
STAT3_HUMANSTAT3physical
11322786
STAT3_HUMANSTAT3physical
11751884
ANDR_HUMANARphysical
15062556
JUN_HUMANJUNphysical
9211894
XRCC5_HUMANXRCC5physical
15640154
XRCC6_HUMANXRCC6physical
15640154
CTNB1_HUMANCTNNB1physical
15256534
CTNB1_HUMANCTNNB1physical
14593076
NCOA1_HUMANNCOA1physical
15256534
NCOR1_HUMANNCOR1physical
15256534
NCOR1_HUMANNCOR1physical
14593076
NCOR1_HUMANNCOR1physical
12089345
SMAD3_HUMANSMAD3physical
11280774
NCOR2_HUMANNCOR2physical
12441355
NCOR2_HUMANNCOR2physical
14593076
NCOR2_HUMANNCOR2physical
11923464
NCOA2_HUMANNCOA2physical
14593076
FOXO1_HUMANFOXO1physical
12482965
ANDR_HUMANARphysical
15256534
ANDR_HUMANARphysical
11504717
MAGAB_HUMANMAGEA11physical
15684378
CTNB1_HUMANCTNNB1physical
12799378
P53_HUMANTP53genetic
11504717
TGFI1_HUMANTGFB1I1physical
11856738
NCOA6_HUMANNCOA6physical
14645241
CBP_HUMANCREBBPphysical
9822653
EGFR_HUMANEGFRphysical
15305378
EGFR_HUMANEGFRphysical
15288768
GRIP1_HUMANGRIP1physical
10607837
PELP1_HUMANPELP1physical
15466214
SRC_HUMANSRCphysical
15027889
SART3_HUMANSART3physical
15031286
ZMIZ1_HUMANZMIZ1physical
14609956
HDAC3_HUMANHDAC3physical
12943985
HDAC4_HUMANHDAC4physical
12943985
GELS_HUMANGSNphysical
12941811
PSPC1_HUMANPSPC1physical
12810069
NONO_HUMANNONOphysical
12810069
NCOA2_HUMANNCOA2physical
12810069
CBP_HUMANCREBBPphysical
12810069
ANDR_HUMANARphysical
12682292
EFCB6_HUMANEFCAB6physical
12612053
HDAC1_HUMANHDAC1physical
11994312
CDK9_HUMANCDK9physical
11266437
NSD1_HUMANNSD1physical
11509567
CBP_HUMANCREBBPgenetic
9482849
TS101_HUMANTSG101physical
10508170
COX5B_HUMANCOX5Bphysical
11719263
RAF1_HUMANRAF1physical
8349631
SVIL_HUMANSVILphysical
11792840
FHL2_HUMANFHL2physical
10654935
PAK6_HUMANPAK6physical
11773441
PIAS4_HUMANPIAS4physical
11439351
NCOA4_HUMANNCOA4physical
11818501
NR0B1_HUMANNR0B1physical
11875111
TMF1_HUMANTMF1physical
10428808
SRY_HUMANSRYphysical
11585838
CTNB1_HUMANCTNNB1physical
11916967
UBC9_HUMANUBE2Iphysical
10383460
UBC9_HUMANUBE2Igenetic
10383460
SMAD3_HUMANSMAD3physical
12226080
SMAD4_HUMANSMAD4physical
12226080
CALR_HUMANCALRphysical
8107809
NCOA4_HUMANNCOA4physical
11779876
RNF14_HUMANRNF14physical
11779876
TGFI1_HUMANTGFB1I1physical
11779876
SPDEF_HUMANSPDEFphysical
10625666
NCOA3_HUMANNCOA3physical
11747336
RNF4_HUMANRNF4physical
11719514
PATZ1_HUMANPATZ1physical
11719514
ETV5_HUMANETV5physical
8798622
BAG1_HUMANBAG1physical
9565586
PIAS1_HUMANPIAS1physical
11117529
PIAS3_HUMANPIAS3physical
11117529
HMGB1_HUMANHMGB1physical
9671457
HMGB2_HUMANHMGB2physical
9671457
PRP6_HUMANPRPF6physical
12039962
RNF14_HUMANRNF14physical
10085091
T2FA_HUMANGTF2F1physical
9238003
T2FB_HUMANGTF2F2physical
9238003
TBP_HUMANTBPphysical
9238003
TF2H1_HUMANGTF2H1physical
10734072
MED1_HUMANMED1physical
12218053
HS90A_HUMANHSP90AA1physical
1525041
PMEPA_HUMANPMEPA1physical
18703514
RAD9A_HUMANRAD9Aphysical
14966297
SMCA4_HUMANSMARCA4physical
14966121
SMRC1_HUMANSMARCC1physical
14966121
NCOA2_HUMANNCOA2physical
14966121
NCOA3_HUMANNCOA3physical
14966121
RNF14_HUMANRNF14physical
12612084
NCOA4_HUMANNCOA4physical
12612084
NCOA2_HUMANNCOA2physical
12612084
NCOA2_HUMANNCOA2physical
15684378
TRI68_HUMANTRIM68physical
18451177
HSPB2_HUMANHSPB2physical
17974989
MDM2_HUMANMDM2physical
17974989
HS90A_HUMANHSP90AA1physical
17974989
NSD2_HUMANWHSC1physical
19481544
ZN363_HUMANRCHY1physical
17721809
MDN1_HUMANMDN1physical
19762545
NAL10_HUMANNLRP10physical
19762545
SMCA2_HUMANSMARCA2physical
19762545
SMCA4_HUMANSMARCA4physical
19762545
ZBT16_HUMANZBTB16physical
19762545
MED24_HUMANMED24physical
19762545
DEN5A_HUMANDENND5Aphysical
19762545
ZBTB1_HUMANZBTB1physical
19762545
MD12L_HUMANMED12Lphysical
19762545
SMRD1_HUMANSMARCD1physical
19762545
SPOP_HUMANSPOPphysical
19762545
MLH3_HUMANMLH3physical
19762545
KIFA3_HUMANKIFAP3physical
19762545
HDAC1_HUMANHDAC1physical
15640443
MDM2_HUMANMDM2physical
15640443
SIR1_HUMANSIRT1physical
16923962
NCOR1_HUMANNCOR1physical
16914745
ZN363_HUMANRCHY1physical
16914734
ZN318_HUMANZNF318physical
16469430
SMCE1_HUMANSMARCE1physical
18559499
EP300_HUMANEP300physical
18487222
SMCA2_HUMANSMARCA2physical
18487222
SMCA4_HUMANSMARCA4physical
18487222
CTNB1_HUMANCTNNB1physical
12944908
HDAC1_HUMANHDAC1physical
15835920
TGIF1_HUMANTGIF1physical
11682623
KAT5_HUMANKAT5physical
10364196
NCOR2_HUMANNCOR2physical
15062576
SRC_HUMANSRCphysical
15062576
SFPQ_HUMANSFPQphysical
17452459
NONO_HUMANNONOphysical
17452459
G45IP_HUMANGADD45GIP1physical
17885209
HDAC4_HUMANHDAC4physical
21242980
UBP26_HUMANUSP26physical
20501646
RNF6_HUMANRNF6physical
19345326
NELFD_HUMANNELFCDphysical
20069563
HS90A_HUMANHSP90AA1physical
19706771
CHIP_HUMANSTUB1physical
19706771
GELS_HUMANGSNphysical
15604093
RNF14_HUMANRNF14physical
15604093
REPS2_HUMANREPS2physical
15604093
NCOA4_HUMANNCOA4physical
15604093
KIF1A_HUMANKIF1Aphysical
15604093
ERCC3_HUMANERCC3physical
21157430
ERCC2_HUMANERCC2physical
21157430
TF2H2_HUMANGTF2H2physical
21157430
CDK7_HUMANCDK7physical
21157430
MDM2_HUMANMDM2physical
21157430
CHIP_HUMANSTUB1physical
21157430
HS90A_HUMANHSP90AA1physical
21157430
TIF1A_HUMANTRIM24physical
19909775
ZBT7A_HUMANZBTB7Aphysical
20812024
NCOR1_HUMANNCOR1physical
15598662
E2F1_HUMANE2F1physical
22508987
E2F4_HUMANE2F4physical
22508987
NCOR2_HUMANNCOR2physical
22508987
PRS6A_HUMANPSMC3physical
19325002
CHIP_HUMANSTUB1physical
15107424
LATS2_HUMANLATS2physical
15131260
CSN2_HUMANCOPS2physical
17356171
NCOR2_HUMANNCOR2physical
17356171
UBP10_HUMANUSP10physical
16368182
TAF1_HUMANTAF1physical
20181722
ACK1_HUMANTNK2physical
17494760
DDB2_HUMANDDB2physical
22846800
PAX6_HUMANPAX6physical
19790232
RNF14_HUMANRNF14physical
17110431
ARI5A_HUMANARID5Aphysical
15941852
NCOA1_HUMANNCOA1physical
12163482
PAX6_HUMANPAX6physical
21935435
TCF20_HUMANTCF20physical
21935435
DCAF6_HUMANDCAF6physical
15784617
CHIP_HUMANSTUB1physical
20661446
FKBP5_HUMANFKBP5physical
20661446
FKBP4_HUMANFKBP4physical
20661446
PPP5_HUMANPPP5Cphysical
20661446
DNJC7_HUMANDNAJC7physical
20661446
PPID_HUMANPPIDphysical
20661446
MAGAB_HUMANMAGEA11physical
19828458
TAB2_HUMANTAB2physical
16469706
NCOR1_HUMANNCOR1physical
16469706
HDAC3_HUMANHDAC3physical
16469706
TBL1R_HUMANTBL1XR1physical
16469706
SIN3A_HUMANSIN3Aphysical
16469706
SIN3B_HUMANSIN3Bphysical
16469706
PARK7_HUMANPARK7physical
17510388
HS90A_HUMANHSP90AA1physical
19805354
STAT3_HUMANSTAT3physical
12804609
MDM2_HUMANMDM2physical
23132866
AKT1_HUMANAKT1physical
18332867
MDM2_HUMANMDM2physical
18332867
SIAH2_HUMANSIAH2physical
23518348
NCOR1_HUMANNCOR1physical
23518348
ACTB_HUMANACTBphysical
17353003
HS90A_HUMANHSP90AA1physical
17353003
NCOA1_HUMANNCOA1physical
17353003
JHD2C_HUMANJMJD1Cphysical
17353003
SMAD1_HUMANSMAD1physical
17183365
VHL_HUMANVHLphysical
23961993
NCOA4_HUMANNCOA4physical
10347167
TEBP_HUMANPTGES3physical
22899854
RBL1_HUMANRBL1physical
23853093
UBP12_HUMANUSP12physical
24056413
SPOP_HUMANSPOPphysical
24508459
VHL_HUMANVHLphysical
24422631
RNF14_HUMANRNF14physical
24422631
ANDR_HUMANARphysical
23172223
MAGAB_HUMANMAGEA11physical
23172223
EP300_HUMANEP300physical
23172223
NCOA1_HUMANNCOA1physical
23975195
MAGAB_HUMANMAGEA11physical
24722188
UBP12_HUMANUSP12physical
25216524
SPOP_HUMANSPOPphysical
25274033
DAPK3_HUMANDAPK3physical
23146908
TS101_HUMANTSG101physical
23146908
AATF_HUMANAATFphysical
23146908
KAT2B_HUMANKAT2Bphysical
10779504
TF65_HUMANRELAgenetic
9482849
TRI18_HUMANMID1physical
24913494
TF7L2_HUMANTCF7L2physical
12799378
ELF3_HUMANELF3physical
23435425
UBP7_HUMANUSP7physical
26175158
HS90A_HUMANHSP90AA1physical
26342197
PP1A_HUMANPPP1CAphysical
26636645
AHR_HUMANAHRphysical
25908644
ANDR_HUMANARphysical
25908644
WDR20_HUMANWDR20physical
26462181
WDR48_HUMANWDR48physical
26462181
UBP12_HUMANUSP12physical
26462181
PRP8_HUMANPRPF8physical
26371515
UBP26_HUMANUSP26physical
27089915
HS90A_HUMANHSP90AA1physical
20048054
FKBP5_HUMANFKBP5physical
20048054
TEBP_HUMANPTGES3physical
20048054
PP2AA_HUMANPPP2CAphysical
20048054
EP300_HUMANEP300physical
27903893
HS90A_HUMANHSP90AA1physical
27903893
CACL1_HUMANCACUL1physical
27085459
KDM1A_HUMANKDM1Aphysical
27085459
UBP14_HUMANUSP14physical
28151478
SMRC2_HUMANSMARCC2physical
28611094
TLE3_HUMANTLE3physical
28611094
TCF20_HUMANTCF20physical
28611094
GSE1_HUMANGSE1physical
28611094
ARI1A_HUMANARID1Aphysical
28611094
JHD2C_HUMANJMJD1Cphysical
28611094
ARI1B_HUMANARID1Bphysical
28611094
SMRC1_HUMANSMARCC1physical
28611094
KDM1A_HUMANKDM1Aphysical
28611094
BCOR_HUMANBCORphysical
28611094
SMCE1_HUMANSMARCE1physical
28611094
SMCA4_HUMANSMARCA4physical
28611094
SNF5_HUMANSMARCB1physical
28611094
NCOR2_HUMANNCOR2physical
28611094
KMT2D_HUMANKMT2Dphysical
28611094
SMCA2_HUMANSMARCA2physical
28611094
CHD7_HUMANCHD7physical
28611094
RCOR1_HUMANRCOR1physical
28611094
DPF1_HUMANDPF1physical
28611094
RAI1_HUMANRAI1physical
28611094
AP2A_HUMANTFAP2Aphysical
28611094
2ABA_HUMANPPP2R2Aphysical
28611094
REQU_HUMANDPF2physical
28611094
ARI3B_HUMANARID3Bphysical
28611094
CNBP_HUMANCNBPphysical
28611094
NCOR1_HUMANNCOR1physical
28611094
ARI5B_HUMANARID5Bphysical
28611094
NFL_HUMANNEFLphysical
28611094
RS21_HUMANRPS21physical
28611094
SPS2L_HUMANSPATS2Lphysical
28611094
SMRD1_HUMANSMARCD1physical
28611094
RCC2_HUMANRCC2physical
28611094
DD19A_HUMANDDX19Aphysical
28611094
SYK_HUMANKARSphysical
28611094
SIAH2_HUMANSIAH2physical
28549433
NCOR1_HUMANNCOR1physical
28549433
EP300_HUMANEP300physical
28549433
MDM2_HUMANMDM2physical
28708672
SUV92_HUMANSUV39H2physical
28042025
AKT1_HUMANAKT1physical
28708672
DCAF6_HUMANDCAF6physical
28212551
DDB2_HUMANDDB2physical
28212551
BRD2_HUMANBRD2physical
28805820
BRD3_HUMANBRD3physical
28805820
BRD4_HUMANBRD4physical
28805820
CHIP_HUMANSTUB1physical
27835608
KDM6A_HUMANKDM6Aphysical
22722839
ASXL1_HUMANASXL1physical
22722839
KMT2A_HUMANKMT2Aphysical
22722839
KMT2D_HUMANKMT2Dphysical
22722839
ASH2L_HUMANASH2Lphysical
22722839
FOXA1_HUMANFOXA1physical
22722839
ERG_HUMANERGphysical
22722839

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300068Androgen insensitivity syndrome (AIS)
313200Spinal and bulbar muscular atrophy X-linked 1 (SMAX1)
Note=Defects in AR may play a role in metastatic prostate cancer. The mutated receptor stimulates prostate growth and metastases development despite of androgen ablation. This treatment can reduce primary and metastatic lesions probably by inducing apoptosis of tumor cells when they express the wild-type receptor.
312300
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01128Bicalutamide
DB04839Cyproterone acetate
DB01406Danazol
DB01395Drospirenone
DB00858Drostanolone
DB08899Enzalutamide
DB00687Fludrocortisone
DB01185Fluoxymesterone
DB00499Flutamide
DB01026Ketoconazole
DB00367Levonorgestrel
DB06710Methyltestosterone
DB08804Nandrolone decanoate
DB00984Nandrolone phenpropionate
DB00665Nilutamide
DB00621Oxandrolone
DB00421Spironolactone
DB00624Testosterone
DB01420Testosterone Propionate
Regulatory Network of ANDR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"MST1 is a multifunctional caspase-independent inhibitor of androgenicsignaling.";
Cinar B., Collak F.K., Lopez D., Akgul S., Mukhopadhyay N.K.,Kilicarslan M., Gioeli D.G., Freeman M.R.;
Cancer Res. 71:4303-4313(2011).
Cited for: PHOSPHORYLATION AT SER-650, AND INTERACTION WITH STK4/MST1.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; THR-301 ANDTYR-307, AND MASS SPECTROMETRY.
"CDK9 regulates AR promoter selectivity and cell growth through serine81 phosphorylation.";
Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B.,Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C.,Conaway M., Carey M.F., Gioeli D.;
Mol. Endocrinol. 24:2267-2280(2010).
Cited for: FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-81 BY CDK9, MUTAGENESISOF SER-81, AND INTERACTION WITH CDK9.
"Effect of Ack1 tyrosine kinase inhibitor on ligand-independentandrogen receptor activity.";
Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H.,Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.;
Prostate 70:1274-1285(2010).
Cited for: PHOSPHORYLATION AT TYR-267, AND ENZYME REGULATION.
"Activated Cdc42-associated kinase Ack1 promotes prostate cancerprogression via androgen receptor tyrosine phosphorylation.";
Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E.,Mohler J.L., Earp H.S., Whang Y.E.;
Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007).
Cited for: INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-267 AND TYR-363 BY TNK2,AND MUTAGENESIS OF TYR-267 AND TYR-363.
"Regulation of androgen receptor activity by tyrosinephosphorylation.";
Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,Veenstra T.D., Chen H., Qiu Y.;
Cancer Cell 10:309-319(2006).
Cited for: PHOSPHORYLATION AT TYR-223; TYR-267; TYR-307; TYR-346; TYR-357;TYR-362; TYR-363; TYR-393; TYR-534; TYR-551 AND TYR-915, MUTAGENESISOF TYR-223; TYR-267; TYR-307; TYR-346; TYR-357; TYR-362; TYR-363;TYR-393; TYR-534; TYR-551 AND TYR-915, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1).";
Poukka H., Karvonen U., Jaenne O.A., Palvimo J.J.;
Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000).
Cited for: SUMOYLATION AT LYS-386 AND LYS-520.
Ubiquitylation
ReferencePubMed
"Regulation of androgen receptor transcriptional activity andspecificity by RNF6-induced ubiquitination.";
Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z.,Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,Veenstra T.D., Qiu Y.;
Cancer Cell 15:270-282(2009).
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION ATLYS-845 AND LYS-847 BY RNF6, MUTAGENESIS OF LYS-845 AND LYS-847,INTERACTION WITH RNF14 AND RNF6, AND SUBCELLULAR LOCATION.

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