STF1_HUMAN - dbPTM
STF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STF1_HUMAN
UniProt AC Q13285
Protein Name Steroidogenic factor 1
Gene Name NR5A1
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization Nucleus .
Protein Description Transcriptional activator. Essential for sexual differentiation and formation of the primary steroidogenic tissues. [PubMed: 27378692 Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1]
Protein Sequence MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT
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
34AcetylationLLTCESCKGFFKRTV
EEEHHHCCCHHHHHH
68.9511479297
38AcetylationESCKGFFKRTVQNNK
HHCCCHHHHHHCCCC
44.9211479297
72AcetylationCPFCRFQKCLTVGMR
CCCHHHHHHHHHHHH
28.6211479297
100"N6,N6-dimethyllysine"NKFGPMYKRDRALKQ
CCCCHHHHHHHHHHH
41.38-
100MethylationNKFGPMYKRDRALKQ
CCCCHHHHHHHHHHH
41.38-
1062-HydroxyisobutyrylationYKRDRALKQQKKAQI
HHHHHHHHHHHHHHH
50.09-
119SumoylationQIRANGFKLETGPPM
HHHHCCEECCCCCCC
46.97-
119UbiquitinationQIRANGFKLETGPPM
HHHHCCEECCCCCCC
46.971999590
119SumoylationQIRANGFKLETGPPM
HHHHCCEECCCCCCC
46.9715192080
194SumoylationAFPGRAIKSEYPEPY
CCCCCCCCCCCCCCC
35.93-
194SumoylationAFPGRAIKSEYPEPY
CCCCCCCCCCCCCCC
35.9315192080
203PhosphorylationEYPEPYASPPQPGLP
CCCCCCCCCCCCCCC
31.1311038323
430PhosphorylationLVEVRALSMQAKEYL
HHHHHHHHHHHHHHH
14.0915523052

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
203SPhosphorylationKinaseCDK7P50613
Uniprot
203SPhosphorylationKinaseMAPK1P28482
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
203SPhosphorylation

19015234
203SPhosphorylation

19015234
203SSumoylation

19015234

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 STF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRIP1_HUMANNRIP1physical
12782406
NRIP1_HUMANNRIP1physical
11459805
ZN653_HUMANZNF653physical
12920234
GATA4_HUMANGATA4physical
10446911
NR0B1_HUMANNR0B1physical
11713202
NCOA1_HUMANNCOA1physical
9328345
TREF1_HUMANTRERF1physical
12101186
CTNB1_HUMANCTNNB1physical
12554773
SOX9_HUMANSOX9physical
9774680
PITX1_HUMANPITX1physical
10369682
CXXC1_HUMANCXXC1physical
20211142
CBP_HUMANCREBBPphysical
10628748
BARD1_HUMANBARD1physical
21087664
ARIP4_HUMANRAD54L2physical
19692572
NR0B1_HUMANNR0B1physical
14963109
NCK2_HUMANNCK2physical
25416956
TPC2A_HUMANTRAPPC2physical
20498720
TPC2B_HUMANTRAPPC2physical
20498720

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
61296546,XY sex reversal 3 (SRXY3)
184757Adrenocortical insufficiency, without ovarian defect (ACIWOD)
612964Premature ovarian failure 7 (POF7)
613957Spermatogenic failure 8 (SPGF8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"SUMOylation inhibits SF-1 activity by reducing CDK7-mediated serine203 phosphorylation.";
Yang W.-H., Heaton J.H., Brevig H., Mukherjee S., Iniguez-Lluhi J.A.,Hammer G.D.;
Mol. Cell. Biol. 29:613-625(2009).
Cited for: SUMOYLATION, AND PHOSPHORYLATION AT SER-203.
"Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7.";
Lewis A.E., Rusten M., Hoivik E.A., Vikse E.L., Hansson M.L.,Wallberg A.E., Bakke M.;
Mol. Endocrinol. 22:91-104(2008).
Cited for: PHOSPHORYLATION AT SER-203, AND INTERACTION WITH CDK7.
"Phosphorylation of the nuclear receptor SF-1 modulates cofactorrecruitment: integration of hormone signaling in reproduction andstress.";
Hammer G.D., Krylova I., Zhang Y., Darimont B.D., Simpson K.,Weigel N.L., Ingraham H.A.;
Mol. Cell 3:521-526(1999).
Cited for: PHOSPHORYLATION AT SER-203.
Sumoylation
ReferencePubMed
"Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergycontrol motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9.";
Komatsu T., Mizusaki H., Mukai T., Ogawa H., Baba D., Shirakawa M.,Hatakeyama S., Nakayama K.I., Yamamoto H., Kikuchi A., Morohashi K.;
Mol. Endocrinol. 18:2451-2462(2004).
Cited for: SUMOYLATION AT LYS-119 AND LYS-194, AND MUTAGENESIS OF LYS-119 ANDLYS-194.

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