Reviewed, UniProtKB/Swiss-Prot P36956 (SRBP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Sterol regulatory element-binding protein 1
      Short name=SREBP-1
Alternative name(s):
    Sterol regulatory element-binding transcription factor 1
Cleaved into the following chain:
    1- Recommended name:
            Processed sterol regulatory element-binding protein 1

Gene names

Name:	SREBF1
Synonyms:	SREBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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').
Subunit structure	Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicle › COPII-coated vesicle membrane; Multi-pass membrane protein. Note: Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. Processed sterol regulatory element-binding protein 1: Nucleus.
Tissue specificity	Expressed in a wide variety of tissues, most abundant in liver and adrenal gland. In fetal tissues lung and liver shows highest expression. Isoform SREBP-1C predominates in liver, adrenal gland and ovary, whereas isoform SREBP-1A predominates in hepatoma cell lines. Isoform SREBP-1A and isoform SREBP-1C are found in kidney, brain, white fat, and muscle.
Post-translational modification	At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7.
Sequence similarities	Belongs to the SREBP family. Contains 1 basic helix-loop-helix (bHLH) domain.
Sequence caution	The sequence BAD92846.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Transcription Transcription regulation
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to starvation Inferred from sequence or structural similarity. Source: HGNC cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ER to Golgi transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Traceable author statement. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Traceable author statement. Source: ProtInc
Molecular function	RNA polymerase II transcription factor activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB sterol response element binding Inferred from direct assay. Source: HGNC transcription factor activity Inferred from direct assay. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Crebbp	P45481	1	EBI-948328,EBI-296306	From a different organism.
MED15	Q96RN5	4	EBI-948328,EBI-394506

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform SREBP-1A (identifier: P36956-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform SREBP-1B (identifier: P36956-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1035-1147: VFLHEATARL...LGGGTTVTSS → LMDVLTSESA...KVPGWHGRMD

Isoform SREBP-1C (identifier: P36956-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MDEPPFSEAALEQALGEPCDLDAALLTDI → MDCTF
     1035-1147: VFLHEATARL...LGGGTTVTSS → LMDVLTSESA...KVPGWHGRMD

Isoform 4 (identifier: P36956-4)

The sequence of this isoform differs from the canonical sequence as follows:
     30-30: E → EGEVGAGRGRANGLDAPRAGADRGAMDCTFE

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1147

1147

Sterol regulatory element-binding protein 1

PRO_0000127447

Chain

1 – 490

490

Processed sterol regulatory element-binding protein 1

PRO_0000314029

Regions

Topological domain

1 – 487

487

Cytoplasmic Potential

Transmembrane

488 – 508

21

Potential

Topological domain

509 – 547

39

Lumenal Potential

Transmembrane

548 – 568

21

Potential

Topological domain

569 – 1147

579

Cytoplasmic Potential

Domain

337 – 374

38

Helix-loop-helix motif

Domain

373 – 394

22

Leucine-zipper Potential

DNA binding

323 – 336

14

Basic motif

Region

1 – 60

60

Transcriptional activation (acidic)

Region

234 – 497

264

Interaction with LMNA By similarity

Compositional bias

61 – 178

118

Pro/Ser-rich

Compositional bias

427 – 462

36

Gly/Pro/Ser-rich

Sites

Site

460 – 461

2

Cleavage; by caspase-3 and caspase-7 By similarity

Site

490 – 491

2

Cleavage; by S2P By similarity

Site

530 – 531

2

Cleavage; by S1P Probable

Amino acid modifications

Modified residue

110

1

Phosphotyrosine By similarity

Modified residue

117

1

Phosphoserine Ref.8

Modified residue

1019

1

Phosphoserine Ref.7

Modified residue

1020

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

1 – 29

29

MDEPP…LLTDI → MDCTF in isoform SREBP-1C.

VSP_002149

Alternative sequence

30

1

E → EGEVGAGRGRANGLDAPRAG ADRGAMDCTFE in isoform 4.

VSP_030859

Alternative sequence

1035 – 1147

113

VFLHE…TVTSS → LMDVLTSESAWALPQHLGKG FPSPSGHKVPGWHGRMD in isoform SREBP-1B and isoform SREBP-1C.

VSP_002150

Natural variant

306

1

N → S: dbSNP rs17855793. Ref.4

VAR_038468

Natural variant

309

1

A → T: dbSNP rs35188700.

VAR_038469

Natural variant

417

1

V → M: dbSNP rs2229590.

VAR_038470

Natural variant

580

1

V → M: dbSNP rs36215896.

VAR_038471

Natural variant

746

1

R → H: dbSNP rs2228461.

VAR_038472

Natural variant

834

1

S → L: dbSNP rs17855792. Ref.4

VAR_038473

Natural variant

1000

1

T → A: dbSNP rs1042017. Ref.1 Ref.2

VAR_038474

Natural variant

1008

1

A → P: dbSNP rs35014224.

VAR_038475

Experimental info

Mutagenesis

455

1

S → A: No effect on proteolytic processing.

Mutagenesis

456

1

D → A: No effect on proteolytic processing.

Mutagenesis

457

1

S → A: No effect on proteolytic processing.

Mutagenesis

460

1

D → A: No effect on proteolytic processing.

Mutagenesis

466

1

D → A: No effect on proteolytic processing.

Mutagenesis

481

1

G → A: No effect on proteolytic processing.

Mutagenesis

482

1

M → A: No effect on proteolytic processing.

Mutagenesis

483

1

L → A: No effect on proteolytic processing.

Mutagenesis

484 – 487

4

DRSR → AS: Strong reduction of proteolytic processing in response to low sterol.

Mutagenesis

484

1

D → A: Loss of proteolytic processing in response to low sterol.

Mutagenesis

485

1

R → A: No effect on proteolytic processing.

Mutagenesis

527

1

R → A: Loss of proteolytic processing in response to low sterol.

Secondary structure

1

.

.

.

.

.

1147

Helix Strand Turn

Details...

Helix

321 – 350

30

Helix

359 – 396

38

Sequences

	Sequence		Length	Mass (Da)
	Isoform SREBP-1A [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 58F28870739FF259	FASTA	1,147	121,675
	10 20 30 40 50 60 MDEPPFSEAA LEQALGEPCD LDAALLTDIE DMLQLINNQD SDFPGLFDPP YAGSGAGGTD 70 80 90 100 110 120 PASPDTSSPG SLSPPPATLS SSLEAFLSGP QAAPSPLSPP QPAPTPLKMY PSMPAFSPGP 130 140 150 160 170 180 GIKEESVPLS ILQTPTPQPL PGALLPQSFP APAPPQFSST PVLGYPSPPG GFSTGSPPGN 190 200 210 220 230 240 TQQPLPGLPL ASPPGVPPVS LHTQVQSVVP QQLLTVTAAP TAAPVTTTVT SQIQQVPVLL 250 260 270 280 290 300 QPHFIKADSL LLTAMKTDGA TVKAAGLSPL VSGTTVQTGP LPTLVSGGTI LATVPLVVDA 310 320 330 340 350 360 EKLPINRLAA GSKAPASAQS RGEKRTAHNA IEKRYRSSIN DKIIELKDLV VGTEAKLNKS 370 380 390 400 410 420 AVLRKAIDYI RFLQHSNQKL KQENLSLRTA VHKSKSLKDL VSACGSGGNT DVLMEGVKTE 430 440 450 460 470 480 VEDTLTPPPS DAGSPFQSSP LSLGSRGSGS GGSGSDSEPD SPVFEDSKAK PEQRPSLHSR 490 500 510 520 530 540 GMLDRSRLAL CTLVFLCLSC NPLASLLGAR GLPSPSDTTS VYHSPGRNVL GTESRDGPGW 550 560 570 580 590 600 AQWLLPPVVW LLNGLLVLVS LVLLFVYGEP VTRPHSGPAV YFWRHRKQAD LDLARGDFAQ 610 620 630 640 650 660 AAQQLWLALR ALGRPLPTSH LDLACSLLWN LIRHLLQRLW VGRWLAGRAG GLQQDCALRV 670 680 690 700 710 720 DASASARDAA LVYHKLHQLH TMGKHTGGHL TATNLALSAL NLAECAGDAV SVATLAEIYV 730 740 750 760 770 780 AAALRVKTSL PRALHFLTRF FLSSARQACL AQSGSVPPAM QWLCHPVGHR FFVDGDWSVL 790 800 810 820 830 840 STPWESLYSL AGNPVDPLAQ VTQLFREHLL ERALNCVTQP NPSPGSADGD KEFSDALGYL 850 860 870 880 890 900 QLLNSCSDAA GAPAYSFSIS SSMATTTGVD PVAKWWASLT AVVIHWLRRD EEAAERLCPL 910 920 930 940 950 960 VEHLPRVLQE SERPLPRAAL HSFKAARALL GCAKAESGPA SLTICEKASG YLQDSLATTP 970 980 990 1000 1010 1020 ASSSIDKAVQ LFLCDLLLVV RTSLWRQQQP PAPAPAAQGT SSRPQASALE LRGFQRDLSS 1030 1040 1050 1060 1070 1080 LRRLAQSFRP AMRRVFLHEA TARLMAGASP TRTHQLLDRS LRRRAGPGGK GGAVAELEPR 1090 1100 1110 1120 1130 1140 PTRREHAEAL LLASCYLPPG FLSAPGQRVG MLAEAARTLE KLGDRRLLHD CQQMLMRLGG GTTVTSS
	Isoform SREBP-1B. Checksum: B71B6010CDB8D1ED	FASTA	1,071	113,562
	10 20 30 40 50 60 MDEPPFSEAA LEQALGEPCD LDAALLTDIE DMLQLINNQD SDFPGLFDPP YAGSGAGGTD 70 80 90 100 110 120 PASPDTSSPG SLSPPPATLS SSLEAFLSGP QAAPSPLSPP QPAPTPLKMY PSMPAFSPGP 130 140 150 160 170 180 GIKEESVPLS ILQTPTPQPL PGALLPQSFP APAPPQFSST PVLGYPSPPG GFSTGSPPGN 190 200 210 220 230 240 TQQPLPGLPL ASPPGVPPVS LHTQVQSVVP QQLLTVTAAP TAAPVTTTVT SQIQQVPVLL 250 260 270 280 290 300 QPHFIKADSL LLTAMKTDGA TVKAAGLSPL VSGTTVQTGP LPTLVSGGTI LATVPLVVDA 310 320 330 340 350 360 EKLPINRLAA GSKAPASAQS RGEKRTAHNA IEKRYRSSIN DKIIELKDLV VGTEAKLNKS 370 380 390 400 410 420 AVLRKAIDYI RFLQHSNQKL KQENLSLRTA VHKSKSLKDL VSACGSGGNT DVLMEGVKTE 430 440 450 460 470 480 VEDTLTPPPS DAGSPFQSSP LSLGSRGSGS GGSGSDSEPD SPVFEDSKAK PEQRPSLHSR 490 500 510 520 530 540 GMLDRSRLAL CTLVFLCLSC NPLASLLGAR GLPSPSDTTS VYHSPGRNVL GTESRDGPGW 550 560 570 580 590 600 AQWLLPPVVW LLNGLLVLVS LVLLFVYGEP VTRPHSGPAV YFWRHRKQAD LDLARGDFAQ 610 620 630 640 650 660 AAQQLWLALR ALGRPLPTSH LDLACSLLWN LIRHLLQRLW VGRWLAGRAG GLQQDCALRV 670 680 690 700 710 720 DASASARDAA LVYHKLHQLH TMGKHTGGHL TATNLALSAL NLAECAGDAV SVATLAEIYV 730 740 750 760 770 780 AAALRVKTSL PRALHFLTRF FLSSARQACL AQSGSVPPAM QWLCHPVGHR FFVDGDWSVL 790 800 810 820 830 840 STPWESLYSL AGNPVDPLAQ VTQLFREHLL ERALNCVTQP NPSPGSADGD KEFSDALGYL 850 860 870 880 890 900 QLLNSCSDAA GAPAYSFSIS SSMATTTGVD PVAKWWASLT AVVIHWLRRD EEAAERLCPL 910 920 930 940 950 960 VEHLPRVLQE SERPLPRAAL HSFKAARALL GCAKAESGPA SLTICEKASG YLQDSLATTP 970 980 990 1000 1010 1020 ASSSIDKAVQ LFLCDLLLVV RTSLWRQQQP PAPAPAAQGT SSRPQASALE LRGFQRDLSS 1030 1040 1050 1060 1070 LRRLAQSFRP AMRRLMDVLT SESAWALPQH LGKGFPSPSG HKVPGWHGRM D
	Isoform SREBP-1C. Checksum: 05CF039C7707AFB9	FASTA	1,047	111,102
	10 20 30 40 50 60 MDCTFEDMLQ LINNQDSDFP GLFDPPYAGS GAGGTDPASP DTSSPGSLSP PPATLSSSLE 70 80 90 100 110 120 AFLSGPQAAP SPLSPPQPAP TPLKMYPSMP AFSPGPGIKE ESVPLSILQT PTPQPLPGAL 130 140 150 160 170 180 LPQSFPAPAP PQFSSTPVLG YPSPPGGFST GSPPGNTQQP LPGLPLASPP GVPPVSLHTQ 190 200 210 220 230 240 VQSVVPQQLL TVTAAPTAAP VTTTVTSQIQ QVPVLLQPHF IKADSLLLTA MKTDGATVKA 250 260 270 280 290 300 AGLSPLVSGT TVQTGPLPTL VSGGTILATV PLVVDAEKLP INRLAAGSKA PASAQSRGEK 310 320 330 340 350 360 RTAHNAIEKR YRSSINDKII ELKDLVVGTE AKLNKSAVLR KAIDYIRFLQ HSNQKLKQEN 370 380 390 400 410 420 LSLRTAVHKS KSLKDLVSAC GSGGNTDVLM EGVKTEVEDT LTPPPSDAGS PFQSSPLSLG 430 440 450 460 470 480 SRGSGSGGSG SDSEPDSPVF EDSKAKPEQR PSLHSRGMLD RSRLALCTLV FLCLSCNPLA 490 500 510 520 530 540 SLLGARGLPS PSDTTSVYHS PGRNVLGTES RDGPGWAQWL LPPVVWLLNG LLVLVSLVLL 550 560 570 580 590 600 FVYGEPVTRP HSGPAVYFWR HRKQADLDLA RGDFAQAAQQ LWLALRALGR PLPTSHLDLA 610 620 630 640 650 660 CSLLWNLIRH LLQRLWVGRW LAGRAGGLQQ DCALRVDASA SARDAALVYH KLHQLHTMGK 670 680 690 700 710 720 HTGGHLTATN LALSALNLAE CAGDAVSVAT LAEIYVAAAL RVKTSLPRAL HFLTRFFLSS 730 740 750 760 770 780 ARQACLAQSG SVPPAMQWLC HPVGHRFFVD GDWSVLSTPW ESLYSLAGNP VDPLAQVTQL 790 800 810 820 830 840 FREHLLERAL NCVTQPNPSP GSADGDKEFS DALGYLQLLN SCSDAAGAPA YSFSISSSMA 850 860 870 880 890 900 TTTGVDPVAK WWASLTAVVI HWLRRDEEAA ERLCPLVEHL PRVLQESERP LPRAALHSFK 910 920 930 940 950 960 AARALLGCAK AESGPASLTI CEKASGYLQD SLATTPASSS IDKAVQLFLC DLLLVVRTSL 970 980 990 1000 1010 1020 WRQQQPPAPA PAAQGTSSRP QASALELRGF QRDLSSLRRL AQSFRPAMRR LMDVLTSESA 1030 1040 WALPQHLGKG FPSPSGHKVP GWHGRMD
	Isoform 4. Checksum: 1C9257FFC7FC7FEB	FASTA	1,177	124,635
	10 20 30 40 50 60 MDEPPFSEAA LEQALGEPCD LDAALLTDIE GEVGAGRGRA NGLDAPRAGA DRGAMDCTFE 70 80 90 100 110 120 DMLQLINNQD SDFPGLFDPP YAGSGAGGTD PASPDTSSPG SLSPPPATLS SSLEAFLSGP 130 140 150 160 170 180 QAAPSPLSPP QPAPTPLKMY PSMPAFSPGP GIKEESVPLS ILQTPTPQPL PGALLPQSFP 190 200 210 220 230 240 APAPPQFSST PVLGYPSPPG GFSTGSPPGN TQQPLPGLPL ASPPGVPPVS LHTQVQSVVP 250 260 270 280 290 300 QQLLTVTAAP TAAPVTTTVT SQIQQVPVLL QPHFIKADSL LLTAMKTDGA TVKAAGLSPL 310 320 330 340 350 360 VSGTTVQTGP LPTLVSGGTI LATVPLVVDA EKLPINRLAA GSKAPASAQS RGEKRTAHNA 370 380 390 400 410 420 IEKRYRSSIN DKIIELKDLV VGTEAKLNKS AVLRKAIDYI RFLQHSNQKL KQENLSLRTA 430 440 450 460 470 480 VHKSKSLKDL VSACGSGGNT DVLMEGVKTE VEDTLTPPPS DAGSPFQSSP LSLGSRGSGS 490 500 510 520 530 540 GGSGSDSEPD SPVFEDSKAK PEQRPSLHSR GMLDRSRLAL CTLVFLCLSC NPLASLLGAR 550 560 570 580 590 600 GLPSPSDTTS VYHSPGRNVL GTESRDGPGW AQWLLPPVVW LLNGLLVLVS LVLLFVYGEP 610 620 630 640 650 660 VTRPHSGPAV YFWRHRKQAD LDLARGDFAQ AAQQLWLALR ALGRPLPTSH LDLACSLLWN 670 680 690 700 710 720 LIRHLLQRLW VGRWLAGRAG GLQQDCALRV DASASARDAA LVYHKLHQLH TMGKHTGGHL 730 740 750 760 770 780 TATNLALSAL NLAECAGDAV SVATLAEIYV AAALRVKTSL PRALHFLTRF FLSSARQACL 790 800 810 820 830 840 AQSGSVPPAM QWLCHPVGHR FFVDGDWSVL STPWESLYSL AGNPVDPLAQ VTQLFREHLL 850 860 870 880 890 900 ERALNCVTQP NPSPGSADGD KEFSDALGYL QLLNSCSDAA GAPAYSFSIS SSMATTTGVD 910 920 930 940 950 960 PVAKWWASLT AVVIHWLRRD EEAAERLCPL VEHLPRVLQE SERPLPRAAL HSFKAARALL 970 980 990 1000 1010 1020 GCAKAESGPA SLTICEKASG YLQDSLATTP ASSSIDKAVQ LFLCDLLLVV RTSLWRQQQP 1030 1040 1050 1060 1070 1080 PAPAPAAQGT SSRPQASALE LRGFQRDLSS LRRLAQSFRP AMRRVFLHEA TARLMAGASP 1090 1100 1110 1120 1130 1140 TRTHQLLDRS LRRRAGPGGK GGAVAELEPR PTRREHAEAL LLASCYLPPG FLSAPGQRVG 1150 1160 1170 MLAEAARTLE KLGDRRLLHD CQQMLMRLGG GTTVTSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene." Yokoyama C., Wang X., Briggs M.R., Admon A., Wu J., Hua X., Goldstein J.L., Brown M.S. Cell 75:187-197(1993) [PubMed: 8402897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SREBP-1A), NUCLEOTIDE SEQUENCE [MRNA] OF 1-29 (ISOFORM SREBP-1C), NUCLEOTIDE SEQUENCE [MRNA] OF 1035-1147 (ISOFORMS SREBP-1B AND SREBP-1C), PARTIAL PROTEIN SEQUENCE, VARIANT ALA-1000. Tissue: Cervix carcinoma.
[2]	"Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13." Hua X., Wu J., Goldstein J.L., Brown M.S., Hobbs H.H. Genomics 25:667-673(1995) [PubMed: 7759101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-1000. Tissue: Fetal brain.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM SREBP-1A).
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SREBP-1A AND 4), VARIANTS SER-306 AND LEU-834. Tissue: Brain, Placenta and Uterus.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-1147 (ISOFORM SREBP-1A/4). Tissue: Spleen.
[6]	"Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane." Hua X., Sakai J., Brown M.S., Goldstein J.L. J. Biol. Chem. 271:10379-10384(1996) [PubMed: 8626610] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019 AND SER-1020, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY.
[9]	"Co-crystal structure of sterol regulatory element binding protein 1a at 2.3-A resolution." Parraga A., Bellsolell L., Ferre-D'Amare A.R., Burley S.K. Structure 6:661-672(1998) [PubMed: 9634703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 319-394.
+	Additional computationally mapped references.

Web resources

Wikipedia

Sterol regulatory element-binding protein entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

U00968 mRNA. Translation: AAC50051.2.
S66167 mRNA. Translation: AAB28522.2. Different initiation.
S66168 mRNA. Translation: AAB28523.1.
CH471196 Genomic DNA. Translation: EAW55689.1.
BC023621 mRNA. Translation: AAH23621.1.
BC026962 mRNA. Translation: AAH26962.1.
BC057388 mRNA. Translation: AAH57388.1.
BC063281 mRNA. Translation: AAH63281.1.
AB209609 mRNA. Translation: BAD92846.1.

IPI

IPI00220878.
IPI00418428.
IPI00419318.
IPI00795043.

PIR

A48845.

RefSeq

NP_001005291.1.
NP_004167.3.

UniGene

Hs.592123
Hs.655395

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AM9	X-ray	2.30	A/B/C/D	319-400	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P36956. 13 interactions.

PTM databases

PhosphoSite

P36956.

Proteomic databases

PRIDE

P36956.

Genome annotation databases

Ensembl

ENSG00000072310. Homo sapiens. [Contig view]

GeneID

6720.

KEGG

hsa:6720.

Organism-specific databases

GeneCards

GC17M017655.

HGNC

HGNC:11289. SREBF1.

HPA

CAB005406.

MIM

184756. gene.

PharmGKB

PA335.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P36956.

OMA

P36956. DCTFEDM.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Gene expression databases

Bgee

P36956.

CleanEx

HS_SREBF1.

GermOnline

ENSG00000072310. Homo sapiens.

Family and domain databases

InterPro

IPR001092. HLH_basic.
IPR011598. HLH_DNA_bd.
[Graphical view]

Gene3D

G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

PROSITE

PS50888. HLH. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

26212.

PMAP-CutDB

P36956.

SOURCE

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Entry information

Entry name

SRBP1_HUMAN

Accession

Primary (citable) accession number: P36956
Secondary accession number(s): Q16062 , Q59F52, Q6P4R7, Q6PFW7, Q6PJ36, Q8TAK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 5, 2008
Last modified:	June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)