SRBP1_HUMAN - dbPTM
SRBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRBP1_HUMAN
UniProt AC P36956
Protein Name Sterol regulatory element-binding protein 1
Gene Name SREBF1
Organism Homo sapiens (Human).
Sequence Length 1147
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane
Multi-pass membrane protein . Moves from the endoplasmic reticulum to the Gol
Protein Description Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway (By similarity). Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3')..
Protein Sequence MDEPPFSEAALEQALGEPCDLDAALLTDIEDMLQLINNQDSDFPGLFDPPYAGSGAGGTDPASPDTSSPGSLSPPPATLSSSLEAFLSGPQAAPSPLSPPQPAPTPLKMYPSMPAFSPGPGIKEESVPLSILQTPTPQPLPGALLPQSFPAPAPPQFSSTPVLGYPSPPGGFSTGSPPGNTQQPLPGLPLASPPGVPPVSLHTQVQSVVPQQLLTVTAAPTAAPVTTTVTSQIQQVPVLLQPHFIKADSLLLTAMKTDGATVKAAGLSPLVSGTTVQTGPLPTLVSGGTILATVPLVVDAEKLPINRLAAGSKAPASAQSRGEKRTAHNAIEKRYRSSINDKIIELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLSLRTAVHKSKSLKDLVSACGSGGNTDVLMEGVKTEVEDTLTPPPSDAGSPFQSSPLSLGSRGSGSGGSGSDSEPDSPVFEDSKAKPEQRPSLHSRGMLDRSRLALCTLVFLCLSCNPLASLLGARGLPSPSDTTSVYHSPGRNVLGTESRDGPGWAQWLLPPVVWLLNGLLVLVSLVLLFVYGEPVTRPHSGPAVYFWRHRKQADLDLARGDFAQAAQQLWLALRALGRPLPTSHLDLACSLLWNLIRHLLQRLWVGRWLAGRAGGLQQDCALRVDASASARDAALVYHKLHQLHTMGKHTGGHLTATNLALSALNLAECAGDAVSVATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPPAMQWLCHPVGHRFFVDGDWSVLSTPWESLYSLAGNPVDPLAQVTQLFREHLLERALNCVTQPNPSPGSADGDKEFSDALGYLQLLNSCSDAAGAPAYSFSISSSMATTTGVDPVAKWWASLTAVVIHWLRRDEEAAERLCPLVEHLPRVLQESERPLPRAALHSFKAARALLGCAKAESGPASLTICEKASGYLQDSLATTPASSSIDKAVQLFLCDLLLVVRTSLWRQQQPPAPAPAAQGTSSRPQASALELRGFQRDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPTRTHQLLDRSLRRRAGPGGKGGAVAELEPRPTRREHAEALLLASCYLPPGFLSAPGQRVGMLAEAARTLEKLGDRRLLHDCQQMLMRLGGGTTVTSS
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
59PhosphorylationAGSGAGGTDPASPDT
CCCCCCCCCCCCCCC
37.58-
63PhosphorylationAGGTDPASPDTSSPG
CCCCCCCCCCCCCCC
28.7922384276
98PhosphorylationQAAPSPLSPPQPAPT
CCCCCCCCCCCCCCC
37.61-
105PhosphorylationSPPQPAPTPLKMYPS
CCCCCCCCCCCCCCC
43.27-
110PhosphorylationAPTPLKMYPSMPAFS
CCCCCCCCCCCCCCC
7.2027080861
112PhosphorylationTPLKMYPSMPAFSPG
CCCCCCCCCCCCCCC
21.6529978859
117PhosphorylationYPSMPAFSPGPGIKE
CCCCCCCCCCCCCCC
30.9325159151
123SumoylationFSPGPGIKEESVPLS
CCCCCCCCCCCCCEE
62.43-
123SumoylationFSPGPGIKEESVPLS
CCCCCCCCCCCCCEE
62.43-
232 (in isoform 3)Ubiquitination-28.3021906983
249PhosphorylationPHFIKADSLLLTAMK
CCEEECCHHHHHHHC
26.2728555341
256UbiquitinationSLLLTAMKTDGATVK
HHHHHHHCCCCCEEE
40.7921906983
256 (in isoform 1)Ubiquitination-40.7921906983
256 (in isoform 2)Ubiquitination-40.7921906983
275PhosphorylationSPLVSGTTVQTGPLP
CCCCCCCEEECCCCC
17.72-
286 (in isoform 4)Ubiquitination-34.3221906983
289 (in isoform 3)Ubiquitination-19.1521906983
312PhosphorylationINRLAAGSKAPASAQ
CCHHHCCCCCCHHHH
22.40-
313AcetylationNRLAAGSKAPASAQS
CHHHCCCCCCHHHHC
58.4325953088
313UbiquitinationNRLAAGSKAPASAQS
CHHHCCCCCCHHHHC
58.4321906983
313 (in isoform 1)Ubiquitination-58.4321906983
313 (in isoform 2)Ubiquitination-58.4321906983
321DimethylationAPASAQSRGEKRTAH
CCHHHHCCCCHHHHH
45.25-
321MethylationAPASAQSRGEKRTAH
CCHHHHCCCCHHHHH
45.25106701399
323 (in isoform 3)Ubiquitination-37.9521906983
324AcetylationSAQSRGEKRTAHNAI
HHHCCCCHHHHHHHH
58.8512640139
324UbiquitinationSAQSRGEKRTAHNAI
HHHCCCCHHHHHHHH
58.85-
332 (in isoform 3)Ubiquitination-29.1321906983
3332-HydroxyisobutyrylationTAHNAIEKRYRSSIN
HHHHHHHHHHHHHHC
48.92-
333AcetylationTAHNAIEKRYRSSIN
HHHHHHHHHHHHHHC
48.9212640139
337PhosphorylationAIEKRYRSSINDKII
HHHHHHHHHHCHHHH
27.00-
338PhosphorylationIEKRYRSSINDKIIE
HHHHHHHHHCHHHHH
19.2016381800
342UbiquitinationYRSSINDKIIELKDL
HHHHHCHHHHHHHHH
40.89-
343 (in isoform 4)Ubiquitination-3.1021906983
347UbiquitinationNDKIIELKDLVVGTE
CHHHHHHHHHHHHCC
35.9021906983
347 (in isoform 1)Ubiquitination-35.9021906983
347 (in isoform 2)Ubiquitination-35.9021906983
356UbiquitinationLVVGTEAKLNKSAVL
HHHHCCCCCCHHHHH
46.4921906983
356 (in isoform 1)Ubiquitination-46.4921906983
356 (in isoform 2)Ubiquitination-46.4921906983
359UbiquitinationGTEAKLNKSAVLRKA
HCCCCCCHHHHHHHH
50.67-
360PhosphorylationTEAKLNKSAVLRKAI
CCCCCCHHHHHHHHH
23.6529214152
365AcetylationNKSAVLRKAIDYIRF
CHHHHHHHHHHHHHH
45.6025953088
365UbiquitinationNKSAVLRKAIDYIRF
CHHHHHHHHHHHHHH
45.60-
377 (in isoform 4)Ubiquitination-40.6621906983
379UbiquitinationFLQHSNQKLKQENLS
HHHHHCHHHHHHCHH
63.00-
381UbiquitinationQHSNQKLKQENLSLR
HHHCHHHHHHCHHHH
63.70-
386PhosphorylationKLKQENLSLRTAVHK
HHHHHCHHHHHHHHH
27.6429449344
386 (in isoform 4)Ubiquitination-27.6421906983
389 (in isoform 4)Ubiquitination-38.02-
394PhosphorylationLRTAVHKSKSLKDLV
HHHHHHHCCCHHHHH
16.7628857561
395 (in isoform 4)Ubiquitination-65.69-
396PhosphorylationTAVHKSKSLKDLVSA
HHHHHCCCHHHHHHH
47.9828857561
398UbiquitinationVHKSKSLKDLVSACG
HHHCCCHHHHHHHHC
56.99-
402PhosphorylationKSLKDLVSACGSGGN
CCHHHHHHHHCCCCC
25.74-
409 (in isoform 4)Ubiquitination-36.31-
411 (in isoform 4)Ubiquitination-35.24-
418SumoylationDVLMEGVKTEVEDTL
HHHCCCCCCEEEECC
50.23-
418SumoylationDVLMEGVKTEVEDTL
HHHCCCCCCEEEECC
50.23-
419PhosphorylationVLMEGVKTEVEDTLT
HHCCCCCCEEEECCC
42.7428102081
424PhosphorylationVKTEVEDTLTPPPSD
CCCEEEECCCCCCCC
21.0128102081
425 (in isoform 4)Ubiquitination-11.93-
426PhosphorylationTEVEDTLTPPPSDAG
CEEEECCCCCCCCCC
35.5225159151
428 (in isoform 4)Ubiquitination-35.47-
430PhosphorylationDTLTPPPSDAGSPFQ
ECCCCCCCCCCCCCC
45.9616825193
434PhosphorylationPPPSDAGSPFQSSPL
CCCCCCCCCCCCCCC
25.0219126544
439PhosphorylationAGSPFQSSPLSLGSR
CCCCCCCCCCCCCCC
21.0516880739
446 (in isoform 3)Ubiquitination-41.3121906983
448PhosphorylationLSLGSRGSGSGGSGS
CCCCCCCCCCCCCCC
28.7725159151
450PhosphorylationLGSRGSGSGGSGSDS
CCCCCCCCCCCCCCC
41.5025159151
453PhosphorylationRGSGSGGSGSDSEPD
CCCCCCCCCCCCCCC
38.3525159151
455PhosphorylationSGSGGSGSDSEPDSP
CCCCCCCCCCCCCCC
39.3925159151
457PhosphorylationSGGSGSDSEPDSPVF
CCCCCCCCCCCCCCC
53.3725159151
461PhosphorylationGSDSEPDSPVFEDSK
CCCCCCCCCCCCCCC
33.4123663014
467PhosphorylationDSPVFEDSKAKPEQR
CCCCCCCCCCCHHHC
27.5824144214
470UbiquitinationVFEDSKAKPEQRPSL
CCCCCCCCHHHCCCH
53.4721906983
470 (in isoform 1)Ubiquitination-53.4721906983
470 (in isoform 2)Ubiquitination-53.4721906983
500 (in isoform 4)Ubiquitination-3.8221906983
505PhosphorylationLSCNPLASLLGARGL
HHCCHHHHHHCCCCC
31.6324719451
518PhosphorylationGLPSPSDTTSVYHSP
CCCCCCCCCCEEECC
25.8830576142
519O-linked_GlycosylationLPSPSDTTSVYHSPG
CCCCCCCCCEEECCC
22.61OGP
524PhosphorylationDTTSVYHSPGRNVLG
CCCCEEECCCCCCCC
16.0330576142
532PhosphorylationPGRNVLGTESRDGPG
CCCCCCCCCCCCCCC
26.9930576142
563 (in isoform 3)Ubiquitination-3.5921906983
567PhosphorylationSLVLLFVYGEPVTRP
HHHHHHHHCCCCCCC
14.40-
587UbiquitinationVYFWRHRKQADLDLA
EEEEECHHHCCHHHC
43.6521906983
587 (in isoform 1)Ubiquitination-43.6521906983
587 (in isoform 2)Ubiquitination-43.6521906983
617 (in isoform 4)Ubiquitination-34.2421906983
651 (in isoform 3)Ubiquitination-21.2321906983
675UbiquitinationDAALVYHKLHQLHTM
HHHHHHHHHHHHHHC
29.9421906983
675 (in isoform 1)Ubiquitination-29.9421906983
675 (in isoform 2)Ubiquitination-29.9421906983
705 (in isoform 4)Ubiquitination-4.2221906983
727UbiquitinationVAAALRVKTSLPRAL
HHHHHHHHCCHHHHH
26.43-
757 (in isoform 4)Ubiquitination-16.78-
900 (in isoform 3)Ubiquitination-7.4321906983
924MethylationRAALHSFKAARALLG
HHHHHHHHHHHHHHC
44.1224624087
924UbiquitinationRAALHSFKAARALLG
HHHHHHHHHHHHHHC
44.1221906983
924 (in isoform 1)Ubiquitination-44.1221906983
924 (in isoform 2)Ubiquitination-44.1221906983
934UbiquitinationRALLGCAKAESGPAS
HHHHCHHCCCCCCCC
57.68-
947UbiquitinationASLTICEKASGYLQD
CCEEEEHHHCCCCCH
43.36-
954 (in isoform 4)Ubiquitination-42.9221906983
964 (in isoform 4)Ubiquitination-32.10-
977 (in isoform 4)Ubiquitination-1.86-
983PhosphorylationLLLVVRTSLWRQQQP
HHHHHHHHHHHCCCC
18.5124719451
1019PhosphorylationRGFQRDLSSLRRLAQ
HHHHHCHHHHHHHHH
31.4530301811
1020PhosphorylationGFQRDLSSLRRLAQS
HHHHCHHHHHHHHHH
32.9425954137
1027PhosphorylationSLRRLAQSFRPAMRR
HHHHHHHHHHHHHHH
20.0220446291
1049PhosphorylationARLMAGASPTRTHQL
HHHHCCCCCCHHHHH
26.3623312004
1051PhosphorylationLMAGASPTRTHQLLD
HHCCCCCCHHHHHHH
45.7823312004
1053PhosphorylationAGASPTRTHQLLDRS
CCCCCCHHHHHHHHH
19.2226434776
1060PhosphorylationTHQLLDRSLRRRAGP
HHHHHHHHHHHHCCC
26.3729214152
1070UbiquitinationRRAGPGGKGGAVAEL
HHCCCCCCCCCCEEC
61.1521906983
1070 (in isoform 1)Ubiquitination-61.1521906983
1100 (in isoform 4)Ubiquitination-33.9021906983
1121UbiquitinationEAARTLEKLGDRRLL
HHHHHHHHHCCHHHH
61.962190698
1121 (in isoform 1)Ubiquitination-61.9621906983
1151 (in isoform 4)Ubiquitination-21906983

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
39SPhosphorylationKinaseMAPK14Q16539
GPS
59TPhosphorylationKinasePKMP14618
PSP
63SPhosphorylationKinaseP38BQ15759
PSP
63SPhosphorylationKinaseMAPK14Q16539
GPS
63SPhosphorylationKinaseP38GP53778
PSP
81TPhosphorylationKinaseMAPK8P45983
GPS
81TPhosphorylationKinaseMAPK1P28482
GPS
93SPhosphorylationKinaseMAPK1P28482
GPS
93SPhosphorylationKinaseMAPK8P45983
GPS
117SPhosphorylationKinaseMAPK1P28482
GPS
117SPhosphorylationKinaseMAPK3P27361
GPS
117SPhosphorylationKinaseMAPK8P45983
GPS
117SPhosphorylationKinaseJNK2P45984
PSP
314SPhosphorylationKinasePRKACAP17612
GPS
337SPhosphorylationKinaseSIK1P57059
Uniprot
338SPhosphorylationKinasePRKACAP17612
GPS
338SPhosphorylationKinaseSIK1P57059
Uniprot
372SPhosphorylationKinasePRKAA1Q13131
GPS
396SPhosphorylationKinaseAMPKQ9Y478
Uniprot
402TPhosphorylationKinaseMAPK14Q16539
GPS
402SPhosphorylationKinaseSIK1P57059
Uniprot
426TPhosphorylationKinaseP38BQ15759
PSP
426TPhosphorylationKinaseP38GP53778
PSP
426TPhosphorylationKinaseMAPK14Q16539
GPS
426TPhosphorylationKinaseGSK3BP49841
PSP
430SPhosphorylationKinaseGSK3BP49841
PSP
434SPhosphorylationKinaseGSK3BP49841
PSP
439SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
402SPhosphorylation

-

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 SRBP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TWST2_HUMANTWIST2physical
14654692
UBC9_HUMANUBE2Iphysical
12615929
CBP_HUMANCREBBPphysical
8918891
SP1_HUMANSP1physical
10224053
NR0B1_HUMANNR0B1physical
11713202
EP300_HUMANEP300physical
12640139
ANDR_HUMANARphysical
18245227
SP1_HUMANSP1physical
10235267
EP300_HUMANEP300physical
10235267
CBP_HUMANCREBBPphysical
10235267
MED15_HUMANMED15physical
10235267
MED23_HUMANMED23physical
10235267
MED7_HUMANMED7physical
10235267
MED13_HUMANMED13physical
10235267
MED12_HUMANMED12physical
10235267
MED1_HUMANMED1physical
10235267
MED14_HUMANMED14physical
10235267
MED24_HUMANMED24physical
10235267
MED26_HUMANMED26physical
10235267
MED6_HUMANMED6physical
10235267
CBP_HUMANCREBBPphysical
9765204
HNF4A_HUMANHNF4Aphysical
17636037
MED15_HUMANMED15physical
20534441
TRRAP_HUMANTRRAPphysical
20534441
KAT2A_HUMANKAT2Aphysical
20534441
ATM_HUMANATMphysical
20534441
EP300_HUMANEP300physical
20534441
GCN1_HUMANGCN1L1physical
20534441
TAD2B_HUMANTADA2Bphysical
20534441
TADA3_HUMANTADA3physical
20534441
RUVB2_HUMANRUVBL2physical
20534441
MED12_HUMANMED12physical
11834832
MED13_HUMANMED13physical
11834832
MED23_HUMANMED23physical
11834832
MED14_HUMANMED14physical
11834832
MED15_HUMANMED15physical
11834832
MED24_HUMANMED24physical
11834832
MED25_HUMANMED25physical
11834832
MED17_HUMANMED17physical
11834832
MED26_HUMANMED26physical
11834832
MED7_HUMANMED7physical
11834832
MED6_HUMANMED6physical
11834832
MED21_HUMANMED21physical
11834832
CDK8_HUMANCDK8physical
11834832
FBXW7_HUMANFBXW7physical
19126544
CBP_HUMANCREBBPphysical
16799563
MED15_HUMANMED15physical
16799563
MED1_HUMANMED1physical
16799563
CDK8_HUMANCDK8physical
16799563
MED6_HUMANMED6physical
16799563
MED13_HUMANMED13physical
16799563
MED12_HUMANMED12physical
16799563
MED14_HUMANMED14physical
16799563
MED23_HUMANMED23physical
16799563
MED24_HUMANMED24physical
16799563
MED25_HUMANMED25physical
16799563
MED17_HUMANMED17physical
16799563
MED26_HUMANMED26physical
16799563
SRBP2_HUMANSREBF2physical
15798184
SRBP1_HUMANSREBF1physical
15798184
ZBT7A_HUMANZBTB7Aphysical
18682402
LMNA_HUMANLMNAphysical
19727227
EGF_HUMANEGFphysical
19727227
NDF1_RATNeurod1physical
16055439
SIR1_HUMANSIRT1physical
20817729
ID2_HUMANID2physical
10585876
ID3_HUMANID3physical
10585876
ANM5_HUMANPRMT5physical
26759235
FBXW7_HUMANFBXW7physical
26759235
PRVA_HUMANPVALBphysical
28514442
SORL_HUMANSORL1physical
28514442
PLK1_HUMANPLK1physical
27579997
FBXW7_HUMANFBXW7physical
27579997
RPB1_HUMANPOLR2Aphysical
29033323

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRBP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019 AND SER-1020, ANDMASS SPECTROMETRY.

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