dbPTM

SRBP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRBP2_HUMAN
UniProt AC	Q12772
Protein Name	Sterol regulatory element-binding protein 2
Gene Name	SREBF2
Organism	Homo sapiens (Human).
Sequence Length	1141
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 Golgi in
Protein Description	Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes..
Protein Sequence	MDDSGELGGLETMETLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGSGGSGSSSGSSGSSSSSSNGRGSSSGAVDPSVQRSFTQVTLPSFSPSAASPQAPTLQVKVSPTSVPTTPRATPILQPRPQPQPQPQTQLQQQTVMITPTFSTTPQTRIIQQPLIYQNAATSFQVLQPQVQSLVTSSQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTTPIQTAALQVPTLVGSSGTILTTMPVMMGQEKVPIKQVPGGVKQLEPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDNEVDLKIEDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLCLSFNPLTSLLQWGGAHDSDQHPHSGSGRSVLSFESGSGGWFDWMMPTLLLWLVNGVIVLSVFVKLLVHGEPVIRPHSRSSVTFWRHRKQADLDLARGDFAAAAGNLQTCLAVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWLLKKVFQCRRATPATEAGFEDEAKTSARDAALAYHRLHQLHITGKLPAGSACSDVHMALCAVNLAECAEEKIPPSTLVEIHLTAAMGLKTRCGGKLGFLASYFLSRAQSLCGPEHSAVPDSLRWLCHPLGQKFFMERSWSVKSAAKESLYCAQRNPADPIAQVHQAFCKNLLERAIESLVKPQAKKKAGDQEEESCEFSSALEYLKLLHSFVDSVGVMSPPLSRSSVLKSALGPDIICRWWTSAITVAISWLQGDDAAVRSHFTKVERIPKALEVTESPLVKAIFHACRAMHASLPGKADGQQSSFCHCERASGHLWSSLNVSGATSDPALNHVVQLLTCDLLLSLRTALWQKQASASQAVGETYHASGAELAGFQRDLGSLRRLAHSFRPAYRKVFLHEATVRLMAGASPTRTHQLLEHSLRRRTTQSTKHGEVDAWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCNDCQQMIVKLGGGTAIAAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
79	Phosphorylation	SSSNGRGSSSGAVDP CCCCCCCCCCCCCCH	21.70	28674419
80	Phosphorylation	SSNGRGSSSGAVDPS CCCCCCCCCCCCCHH	35.30	-
81	Phosphorylation	SNGRGSSSGAVDPSV CCCCCCCCCCCCHHH	32.25	-
99	Phosphorylation	FTQVTLPSFSPSAAS EEEEECCCCCCCCCC	41.28	26657352
101	Phosphorylation	QVTLPSFSPSAASPQ EEECCCCCCCCCCCC	23.45	27251275
103	Phosphorylation	TLPSFSPSAASPQAP ECCCCCCCCCCCCCC	34.96	27251275
106	Phosphorylation	SFSPSAASPQAPTLQ CCCCCCCCCCCCEEE	19.77	26055452
115	Ubiquitination	QAPTLQVKVSPTSVP CCCEEEEEECCCCCC	24.84	-
117	Phosphorylation	PTLQVKVSPTSVPTT CEEEEEECCCCCCCC	19.42	26055452
119	Phosphorylation	LQVKVSPTSVPTTPR EEEEECCCCCCCCCC	34.55	30108239
120	Phosphorylation	QVKVSPTSVPTTPRA EEEECCCCCCCCCCC	29.50	30108239
123	Phosphorylation	VSPTSVPTTPRATPI ECCCCCCCCCCCCCC	47.48	27732954
124	Phosphorylation	SPTSVPTTPRATPIL CCCCCCCCCCCCCCC	12.52	26055452
128	Phosphorylation	VPTTPRATPILQPRP CCCCCCCCCCCCCCC	16.49	26425664
149	O-linked_Glycosylation	QTQLQQQTVMITPTF CCHHEECEEEECCCC	14.01	31637018
153	Phosphorylation	QQQTVMITPTFSTTP EECEEEECCCCCCCC	9.74	-
155	Phosphorylation	QTVMITPTFSTTPQT CEEEECCCCCCCCCC	22.90	-
157	O-linked_Glycosylation	VMITPTFSTTPQTRI EEECCCCCCCCCCCE	33.57	31637018
171	Phosphorylation	IIQQPLIYQNAATSF EECCCEECCCCCCCH	11.91	-
249	Sumoylation	LVQPQIIKTDSLVLT EECCEEEECCEEEEE	48.16	-
249	Sumoylation	LVQPQIIKTDSLVLT EECCEEEECCEEEEE	48.16	-
252	Phosphorylation	PQIIKTDSLVLTTLK CEEEECCEEEEEEEE	26.13	24173317
314	Acetylation	GQEKVPIKQVPGGVK CCCCCCCCCCCCCCC	38.89	25953088
314	Ubiquitination	GQEKVPIKQVPGGVK CCCCCCCCCCCCCCC	38.89	-
321	Acetylation	KQVPGGVKQLEPPKE CCCCCCCCCCCCCCC	53.06	19828961
333	Phosphorylation	PKEGERRTTHNIIEK CCCCCCCCHHHHHHH	38.33	26074081
334	Phosphorylation	KEGERRTTHNIIEKR CCCCCCCHHHHHHHH	15.89	26074081
340	Ubiquitination	TTHNIIEKRYRSSIN CHHHHHHHHHHHHHC	44.30	-
345	Phosphorylation	IEKRYRSSINDKIIE HHHHHHHHHCCHHHH	19.20	-
349	Ubiquitination	YRSSINDKIIELKDL HHHHHCCHHHHHHHH	40.89	-
354	Ubiquitination	NDKIIELKDLVMGTD CCHHHHHHHHHHCCC	35.90	21906983
363	Acetylation	LVMGTDAKMHKSGVL HHHCCCHHHCHHCHH	44.33	7712309
363	Ubiquitination	LVMGTDAKMHKSGVL HHHCCCHHHCHHCHH	44.33	-
366	Ubiquitination	GTDAKMHKSGVLRKA CCCHHHCHHCHHHHH	45.46	-
372	Ubiquitination	HKSGVLRKAIDYIKY CHHCHHHHHHHHHHH	45.60	-
378	Ubiquitination	RKAIDYIKYLQQVNH HHHHHHHHHHHHHCH	33.41	-
386	Ubiquitination	YLQQVNHKLRQENMV HHHHHCHHHHHHHHH	39.91	-
395	Ubiquitination	RQENMVLKLANQKNK HHHHHHHHHHHHHCH	33.86	-
400	Ubiquitination	VLKLANQKNKLLKGI HHHHHHHHCHHCCCC	56.72	-
405	Ubiquitination	NQKNKLLKGIDLGSL HHHCHHCCCCCHHHH	65.34	21906983
420	Sumoylation	VDNEVDLKIEDFNQN HCCCCCCCEECCCCC	39.32	-
432	Phosphorylation	NQNVLLMSPPASDSG CCCEEEECCCCCCCC	27.92	14988395
455	Phosphorylation	SIDSEPGSPLLDDAK CCCCCCCCCCCCCCC	24.08	14988395
464	Ubiquitination	LLDDAKVKDEPDSPP CCCCCCCCCCCCCCC	56.52	21906983
464	Sumoylation	LLDDAKVKDEPDSPP CCCCCCCCCCCCCCC	56.52	-
464	Sumoylation	LLDDAKVKDEPDSPP CCCCCCCCCCCCCCC	56.52	28112733
469	Phosphorylation	KVKDEPDSPPVALGM CCCCCCCCCCCHHCC	41.65	23401153
579	Ubiquitination	VTFWRHRKQADLDLA CEEEEEHHHCCHHHH	43.65	21906983
618	Phosphorylation	SRLDLACSLSWNVIR CCHHHHHHHHHHHHH	21.60	25003641
626	Phosphorylation	LSWNVIRYSLQKLRL HHHHHHHHHHHHHHH	11.56	25003641
630	Acetylation	VIRYSLQKLRLVRWL HHHHHHHHHHHHHHH	40.65	7964191
640	Ubiquitination	LVRWLLKKVFQCRRA HHHHHHHHHHHCCCC	48.53	-
660	Ubiquitination	AGFEDEAKTSARDAA CCCCHHHHHHHHHHH	40.75	21906983
731	Ubiquitination	LKTRCGGKLGFLASY CCCCCCCHHHHHHHH	30.62	-
745	Phosphorylation	YFLSRAQSLCGPEHS HHHHHHHHHHCCCCC	25.33	-
768	Ubiquitination	LCHPLGQKFFMERSW HHCHHHCCCHHHCCC	38.48	-
778	Ubiquitination	MERSWSVKSAAKESL HHCCCCHHHHHHHHH	28.94	-
782	Ubiquitination	WSVKSAAKESLYCAQ CCHHHHHHHHHHHHH	47.77	-
805	Ubiquitination	QVHQAFCKNLLERAI HHHHHHHHHHHHHHH	44.15	-
814	Phosphorylation	LLERAIESLVKPQAK HHHHHHHHHHCHHHH	32.14	26546556
817	Ubiquitination	RAIESLVKPQAKKKA HHHHHHHCHHHHHHC	36.38	21906983
821	Ubiquitination	SLVKPQAKKKAGDQE HHHCHHHHHHCCCCH	49.94	-
822	Ubiquitination	LVKPQAKKKAGDQEE HHCHHHHHHCCCCHH	51.36	-
823	Ubiquitination	VKPQAKKKAGDQEEE HCHHHHHHCCCCHHH	57.82	-
840	Phosphorylation	EFSSALEYLKLLHSF HHHHHHHHHHHHHHH	15.24	22817900
846	Phosphorylation	EYLKLLHSFVDSVGV HHHHHHHHHHHHHCC	27.25	24117733
850	Phosphorylation	LLHSFVDSVGVMSPP HHHHHHHHHCCCCCC	18.57	24117733
855	Phosphorylation	VDSVGVMSPPLSRSS HHHHCCCCCCCCHHH	22.44	24117733
859	Phosphorylation	GVMSPPLSRSSVLKS CCCCCCCCHHHHHHH	35.57	24117733
865	Ubiquitination	LSRSSVLKSALGPDI CCHHHHHHHHHCCCH	31.37	-
901	Ubiquitination	AVRSHFTKVERIPKA HHHHHCCCCCCCCCC	40.95	-
907	Ubiquitination	TKVERIPKALEVTES CCCCCCCCCCCCCCC	64.33	21906983
914	Phosphorylation	KALEVTESPLVKAIF CCCCCCCCHHHHHHH	17.73	24719451
918	Ubiquitination	VTESPLVKAIFHACR CCCCHHHHHHHHHHH	43.37	-
934	Ubiquitination	MHASLPGKADGQQSS HHHCCCCCCCCCCCC	41.17	-
989	Ubiquitination	LRTALWQKQASASQA HHHHHHHHHHHHHHH	35.93	21906983
1017	Phosphorylation	GFQRDLGSLRRLAHS HHHHHHHHHHHHHHH	26.46	24719451
1031	Ubiquitination	SFRPAYRKVFLHEAT HHCHHHHHHHHHHHH	25.35	-
1046	Phosphorylation	VRLMAGASPTRTHQL HHHHCCCCCCHHHHH	26.36	23312004
1048	Phosphorylation	LMAGASPTRTHQLLE HHCCCCCCHHHHHHH	45.78	23312004
1057	Phosphorylation	THQLLEHSLRRRTTQ HHHHHHHHHHHCCCC	17.75	-
1067	Ubiquitination	RRTTQSTKHGEVDAW HCCCCCCCCCCCCCC	55.66	21906983
1094	Phosphorylation	ACRHLPLSFLSSPGQ HHHCCCHHHHCCHHH	23.38	21712546
1097	Phosphorylation	HLPLSFLSSPGQRAV CCCHHHHCCHHHHHH	32.26	22167270
1098	Phosphorylation	LPLSFLSSPGQRAVL CCHHHHCCHHHHHHH	34.89	22167270
1115	Ubiquitination	EAARTLEKVGDRRSC HHHHHHHHHCCCCCC	55.41	21906983
1121	Phosphorylation	EKVGDRRSCNDCQQM HHHCCCCCCHHHHHH	20.40	27499020

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
432	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
432	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
432	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
455	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
455	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
455	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:16054087

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRBP2_HUMAN !!

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 SRBP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC9_HUMAN	UBE2I	physical	12615929
CBP_HUMAN	CREBBP	physical	8918891
SRBP2_HUMAN	SREBF2	physical	11283257
CASP3_HUMAN	CASP3	physical	8605870
ARRB1_HUMAN	ARRB1	physical	20936779
EGR1_HUMAN	EGR1	physical	20936779
FHL3_HUMAN	FHL3	physical	20936779
GOGB1_HUMAN	GOLGB1	physical	20936779
GRP78_HUMAN	HSPA5	physical	20936779
ITB4_HUMAN	ITGB4	physical	20936779
ABLM1_HUMAN	ABLIM1	physical	20936779
NFYA_HUMAN	NFYA	physical	20936779
PSMD4_HUMAN	PSMD4	physical	20936779
ATX1_HUMAN	ATXN1	physical	20936779
SP1_HUMAN	SP1	physical	20936779
SPTB2_HUMAN	SPTBN1	physical	20936779
TTC1_HUMAN	TTC1	physical	20936779
UBC9_HUMAN	UBE2I	physical	20936779
ZMYM2_HUMAN	ZMYM2	physical	20936779
ZYX_HUMAN	ZYX	physical	20936779
PIAS1_HUMAN	PIAS1	physical	20936779
S4A4_HUMAN	SLC4A4	physical	20936779
PIAS2_HUMAN	PIAS2	physical	20936779
ARHG1_HUMAN	ARHGEF1	physical	20936779
C8AP2_HUMAN	CASP8AP2	physical	20936779
PIAS3_HUMAN	PIAS3	physical	20936779
OS9_HUMAN	OS9	physical	20936779
CSN5_HUMAN	COPS5	physical	20936779
ZDH17_HUMAN	ZDHHC17	physical	20936779
MCAF1_HUMAN	ATF7IP	physical	20936779
ABLM2_HUMAN	ABLIM2	physical	20936779
LZTR1_HUMAN	LZTR1	physical	20211142
ATF6A_HUMAN	ATF6	physical	14765107
SMAD3_HUMAN	SMAD3	physical	15527767
RN139_HUMAN	RNF139	physical	19706601
HINFP_HUMAN	HINFP	physical	22288532
NPAT_HUMAN	NPAT	physical	22288532
TRRAP_HUMAN	TRRAP	physical	22288532
SRBP2_HUMAN	SREBF2	physical	15798184
HDAC3_HUMAN	HDAC3	physical	18403372

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 SRBP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-840, AND MASSSPECTROMETRY.	17287340 [Abstract]