Q12772 (SRBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sterol regulatory element-binding protein 2
Short name=SREBP-2

Alternative name(s):
Class D basic helix-loop-helix protein 2
Short name=bHLHd2
Sterol regulatory element-binding transcription factor 2

Cleaved into the following chain:

1. Processed sterol regulatory element-binding protein 2

Gene names

Name:	SREBF2
Synonyms:	BHLHD2, SREBP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1141 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 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.
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. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts (via C-terminus domain) with RNF139. Ref.10
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 2: Nucleus.
Tissue specificity	Ubiquitously expressed in adult and fetal tissues.
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. Ref.7 Ref.8 Ref.9 Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression By similarity.
Sequence similarities	Belongs to the SREBP family. Contains 1 bHLH (basic helix-loop-helix) domain.
Sequence caution	The sequence AAH51799.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Sterol metabolism Transcription Transcription regulation
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SREBP signaling pathway Inferred from electronic annotation. Source: Compara cellular response to laminar fluid shear stress Non-traceable author statement PubMed 15358760. Source: BHF-UCL cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Traceable author statement Ref.1. Source: ProtInc negative regulation of cholesterol efflux Inferred from direct assay PubMed 15358760. Source: BHF-UCL positive regulation of cholesterol storage Inferred from direct assay PubMed 15358760. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12242332. Source: UniProtKB regulation of cholesterol homeostasis Inferred from electronic annotation. Source: Compara regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15358760. Source: BHF-UCL response to low-density lipoprotein particle stimulus Inferred from expression pattern PubMed 15358760. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ER to Golgi transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell SREBP-SCAP-Insig complex Inferred from direct assay PubMed 12242332. Source: UniProtKB nucleus Inferred from direct assay PubMed 12202038PubMed 12242332PubMed 12941800. Source: UniProtKB
Molecular_function	E-box binding Inferred from direct assay PubMed 15358760. Source: BHF-UCL RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 15358760. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD3	P84022	3	EBI-465059,EBI-347161
SP1	P08047	3	EBI-465059,EBI-298336
TP53	P04637	3	EBI-465059,EBI-366083

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1141

1141

Sterol regulatory element-binding protein 2

PRO_0000127452

Chain

1 – 484

484

Processed sterol regulatory element-binding protein 2

PRO_0000314033

Regions

Topological domain

1 – 479

479

Cytoplasmic Potential

Transmembrane

480 – 500

21

Helical; Potential

Topological domain

501 – 533

33

Lumenal Potential

Transmembrane

534 – 554

21

Helical; Potential

Topological domain

555 – 1139

585

Cytoplasmic Potential

Domain

330 – 380

51

bHLH

Region

1 – 50

50

Transcriptional activation (acidic)

Region

237 – 491

255

Interaction with LMNA By similarity

Region

380 – 401

22

Leucine-zipper

Compositional bias

52 – 124

73

Gly/Pro/Ser-rich

Compositional bias

125 – 244

120

Gln-rich

Sites

Site

468 – 469

2

Cleavage; by caspase-3 and caspase-7

Site

484 – 485

2

Cleavage; by S2P

Site

522 – 523

2

Cleavage; by S1P

Amino acid modifications

Modified residue

1121

1

Phosphoserine By similarity

Natural variations

Natural variant

273

1

A → S in a breast cancer sample; somatic mutation. Ref.12

VAR_036394

Natural variant

347

1

N → K in a breast cancer sample; somatic mutation. Ref.12

VAR_036395

Natural variant

536

1

M → L.
Corresponds to variant rs17002714 [ dbSNP | Ensembl ].

VAR_049550

Natural variant

595

1

G → A. Ref.1
Corresponds to variant rs2228314 [ dbSNP | Ensembl ].

VAR_028440

Natural variant

623

1

V → M.
Corresponds to variant rs2229440 [ dbSNP | Ensembl ].

VAR_028441

Natural variant

860

1

R → S.
Corresponds to variant rs2228313 [ dbSNP | Ensembl ].

VAR_049551

Experimental info

Mutagenesis

478 – 481

4

DRSR → AAAA: Loss of cleavage by S2P. Ref.6 Ref.8

Mutagenesis

478 – 481

4

DRSR → AS: Loss of cleavage by S2P. Ref.6 Ref.8

Mutagenesis

478

1

D → A: No effect on proteolytic processing in response to low sterol. Ref.6

Mutagenesis

479 – 481

3

RSR → AAA: Loss of cleavage by S2P. Ref.8

Mutagenesis

479

1

R → A: No effect on cleavage by S2P. Ref.8

Mutagenesis

481

1

R → A: No effect on cleavage by S2P. Ref.8

Mutagenesis

484 – 485

2

LC → FF: No effect on cleavage by S2P. Ref.8

Mutagenesis

484

1

L → A: No effect on cleavage by S2P. Ref.8

Mutagenesis

485

1

C → A: No effect on cleavage by S2P. Ref.8

Mutagenesis

490 – 491

2

LC → NP: Restores cleavage by S2P; when associated with F-495 and L-496. No effect on site of cleavage by S2P.

Mutagenesis

495 – 496

2

NP → FL: Loss of cleavage by S2P. Ref.9

Mutagenesis

495

1

N → F: Reduced cleavage by S2P. Ref.9

Mutagenesis

496

1

P → L: Reduced cleavage by S2P. Ref.9

Mutagenesis

519

1

R → A: Loss of proteolytic processing in response to low sterol. Ref.6

Mutagenesis

519

1

R → K: No effect on proteolytic processing in response to low sterol. Ref.6

Sequence conflict

961

1

A → G in AAA50746. Ref.1

Sequence conflict

1045

1

A → G in AAA50746. Ref.1

Secondary structure

1

.

.

.

.

.

.

1141

Helix Strand Turn

Details...

Helix

346 – 357

12

Turn

366 – 368

3

Helix

369 – 399

31

Sequences

	Sequence		Length	Mass (Da)
	Q12772 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 481B1D8E2A2306D2	FASTA	1,141	123,688
	10 20 30 40 50 60 MDDSGELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFPDLFSEQL CSSFPGSGGS 70 80 90 100 110 120 GSSSGSSGSS SSSSNGRGSS SGAVDPSVQR SFTQVTLPSF SPSAASPQAP TLQVKVSPTS 130 140 150 160 170 180 VPTTPRATPI LQPRPQPQPQ PQTQLQQQTV MITPTFSTTP QTRIIQQPLI YQNAATSFQV 190 200 210 220 230 240 LQPQVQSLVT SSQVQPVTIQ QQVQTVQAQR VLTQTANGTL QTLAPATVQT VAAPQVQQVP 250 260 270 280 290 300 VLVQPQIIKT DSLVLTTLKT DGSPVMAAVQ NPALTALTTP IQTAALQVPT LVGSSGTILT 310 320 330 340 350 360 TMPVMMGQEK VPIKQVPGGV KQLEPPKEGE RRTTHNIIEK RYRSSINDKI IELKDLVMGT 370 380 390 400 410 420 DAKMHKSGVL RKAIDYIKYL QQVNHKLRQE NMVLKLANQK NKLLKGIDLG SLVDNEVDLK 430 440 450 460 470 480 IEDFNQNVLL MSPPASDSGS QAGFSPYSID SEPGSPLLDD AKVKDEPDSP PVALGMVDRS 490 500 510 520 530 540 RILLCVLTFL CLSFNPLTSL LQWGGAHDSD QHPHSGSGRS VLSFESGSGG WFDWMMPTLL 550 560 570 580 590 600 LWLVNGVIVL SVFVKLLVHG EPVIRPHSRS SVTFWRHRKQ ADLDLARGDF AAAAGNLQTC 610 620 630 640 650 660 LAVLGRALPT SRLDLACSLS WNVIRYSLQK LRLVRWLLKK VFQCRRATPA TEAGFEDEAK 670 680 690 700 710 720 TSARDAALAY HRLHQLHITG KLPAGSACSD VHMALCAVNL AECAEEKIPP STLVEIHLTA 730 740 750 760 770 780 AMGLKTRCGG KLGFLASYFL SRAQSLCGPE HSAVPDSLRW LCHPLGQKFF MERSWSVKSA 790 800 810 820 830 840 AKESLYCAQR NPADPIAQVH QAFCKNLLER AIESLVKPQA KKKAGDQEEE SCEFSSALEY 850 860 870 880 890 900 LKLLHSFVDS VGVMSPPLSR SSVLKSALGP DIICRWWTSA ITVAISWLQG DDAAVRSHFT 910 920 930 940 950 960 KVERIPKALE VTESPLVKAI FHACRAMHAS LPGKADGQQS SFCHCERASG HLWSSLNVSG 970 980 990 1000 1010 1020 ATSDPALNHV VQLLTCDLLL SLRTALWQKQ ASASQAVGET YHASGAELAG FQRDLGSLRR 1030 1040 1050 1060 1070 1080 LAHSFRPAYR KVFLHEATVR LMAGASPTRT HQLLEHSLRR RTTQSTKHGE VDAWPGQRER 1090 1100 1110 1120 1130 1140 ATAILLACRH LPLSFLSSPG QRAVLLAEAA RTLEKVGDRR SCNDCQQMIV KLGGGTAIAA S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element." Hua X., Yokoyama C., Wu J., Briggs M.R., Brown M.S., Goldstein J.L., Wang X. Proc. Natl. Acad. Sci. U.S.A. 90:11603-11607(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-595.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Skin.
[5]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 91-109.
[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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-478; ARG-519 AND 478-ASP--ARG-481.
[7]	"Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins." Pai J.-T., Brown M.S., Goldstein J.L. Proc. Natl. Acad. Sci. U.S.A. 93:5437-5442(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE AT ASP-468 BY CASPASES.
[8]	"Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning." Duncan E.A., Dave U.P., Sakai J., Goldstein J.L., Brown M.S. J. Biol. Chem. 273:17801-17809(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY S2P, MUTAGENESIS OF ARG-479; ARG-481; LEU-484; CYS-485; 478-ASP--ARG-481; 479-ARG--ARG-481 AND 484-LEU-CYS-485.
[9]	"Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease." Ye J., Dave U.P., Grishin N.V., Goldstein J.L., Brown M.S. Proc. Natl. Acad. Sci. U.S.A. 97:5123-5128(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY S2P, MUTAGENESIS OF ASN-495; PRO-496; 490-LEU-CYS-491 AND 495-ASN-PRO-496.
[10]	"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage." Irisawa M., Inoue J., Ozawa N., Mori K., Sato R. J. Biol. Chem. 284:28995-29004(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF139.
[11]	"The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor." Lee S.J., Sekimoto T., Yamashita E., Nagoshi E., Nakagawa A., Imamoto N., Yoshimura M., Sakai H., Chong K.T., Tsukihara T., Yoneda Y. Science 302:1571-1575(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 343-403.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-273 AND LYS-347.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U02031 mRNA. Translation: AAA50746.1.
CT841522 mRNA. Translation: CAJ86452.1.
AL021453, Z99716 Genomic DNA. Translation: CAI22917.1.
Z99716, AL021453 Genomic DNA. Translation: CAI41688.1.
BC051799 mRNA. Translation: AAH51799.1. Different initiation.
BC056158 mRNA. Translation: AAH56158.1.

IPI

IPI00328793.

PIR

A54962. A49397.

RefSeq

NP_004590.2. NM_004599.2.

UniGene

Hs.443258.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UKL	X-ray	3.00	C/D/E/F	343-403	[»]

ProteinModelPortal

Q12772.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-263N.

IntAct

Q12772. 45 interactions.

MINT

MINT-144301.

STRING

9606.ENSP00000354476.

PTM databases

PhosphoSite

Q12772.

Polymorphism databases

DMDM

116242800.

Proteomic databases

PaxDb

Q12772.

PRIDE

Q12772.

Protocols and materials databases

DNASU

6721.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361204; ENSP00000354476; ENSG00000198911.

GeneID

6721.

KEGG

hsa:6721.

UCSC

uc003bbi.3. human.

Organism-specific databases

CTD

6721.

GeneCards

GC22P042244.

HGNC

HGNC:11290. SREBF2.

HPA

HPA031962.

MIM

600481. gene.

neXtProt

NX_Q12772.

Orphanet

406. Familial hypercholesterolemia.

PharmGKB

PA336.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG242942.

HOGENOM

HOG000007091.

HOVERGEN

HBG061592.

InParanoid

Q12772.

KO

K09107.

OMA

ECAEEKI.

OrthoDB

EOG40S0F2.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_147768. SREBP2 (SREBF2) is retained in the endoplasmic reticulum by SCAP:INSIG2:oxysterol.
REACT_147840. SREBP1A/1C/2 is retained in the endoplasmic reticulum by SCAP:cholesterol:INSIG.
REACT_147890. SREBP2:SCAP Binds CopII Coat Complex.
REACT_147893. SREBP2:SCAP Transits to the Golgi.

Gene expression databases

ArrayExpress

Q12772.

Bgee

Q12772.

CleanEx

HS_SREBF2.

Genevestigator

Q12772.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q12772.

ChEMBL

CHEMBL1795166.

EvolutionaryTrace

Q12772.

GenomeRNAi

6721.

NextBio

26218.

PMAP-CutDB

Q12772.

SOURCE

Search...

Entry information

Entry name

SRBP2_HUMAN

Accession

Primary (citable) accession number: Q12772
Secondary accession number(s): Q6GTH7, Q86V36, Q9UH04

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.