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Q12772 (SRBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:SREBF2
Synonyms:BHLHD2, SREBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 vesicleCOPII-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 processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
Transcription
Transcription regulation
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

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

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19098903. 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: Ensembl

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

Inferred from expression pattern PubMed 15358760. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentER to Golgi transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

SREBP-SCAP-Insig complex

Inferred from direct assay PubMed 12242332. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12941800. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from direct assay PubMed 12202038PubMed 12941800. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12202038PubMed 12242332PubMed 12941800. Source: UniProtKB

   Molecular_functionE-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

protein C-terminus binding

Inferred from physical interaction PubMed 9242699. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12772-1)

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 2 (identifier: Q12772-2)

The sequence of this isoform differs from the canonical sequence as follows:
     273-275: Missing.
     589-684: DFAAAAGNLQ...QLHITGKLPA → VYGKKSGATH...LPVPAGHASH
     685-1141: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11411141Sterol regulatory element-binding protein 2
PRO_0000127452
Chain1 – 484484Processed sterol regulatory element-binding protein 2
PRO_0000314033

Regions

Topological domain1 – 479479Cytoplasmic Potential
Transmembrane480 – 50021Helical; Potential
Topological domain501 – 53333Lumenal Potential
Transmembrane534 – 55421Helical; Potential
Topological domain555 – 1139585Cytoplasmic Potential
Domain330 – 38051bHLH
Region1 – 5050Transcriptional activation (acidic)
Region237 – 491255Interaction with LMNA By similarity
Region380 – 40122Leucine-zipper
Compositional bias52 – 12473Gly/Pro/Ser-rich
Compositional bias125 – 244120Gln-rich

Sites

Site468 – 4692Cleavage; by caspase-3 and caspase-7
Site484 – 4852Cleavage; by S2P
Site522 – 5232Cleavage; by S1P

Natural variations

Alternative sequence273 – 2753Missing in isoform 2.
VSP_054283
Alternative sequence589 – 68496DFAAA…GKLPA → VYGKKSGATHSIEEELNIHI SRGTRTRTLLSSRRFCSCCR QPTNLPGSFGPGTAHLPPGP GLQPLLERDPLQPAEATPGA LAAQESLPVPAGHASH in isoform 2.
VSP_054284
Alternative sequence685 – 1141457Missing in isoform 2.
VSP_054285
Natural variant2731A → S in a breast cancer sample; somatic mutation. Ref.12
VAR_036394
Natural variant3471N → K in a breast cancer sample; somatic mutation. Ref.12
VAR_036395
Natural variant5361M → L.
Corresponds to variant rs17002714 [ dbSNP | Ensembl ].
VAR_049550
Natural variant5951G → A. Ref.1
Corresponds to variant rs2228314 [ dbSNP | Ensembl ].
VAR_028440
Natural variant6231V → M.
Corresponds to variant rs2229440 [ dbSNP | Ensembl ].
VAR_028441
Natural variant8601R → S.
Corresponds to variant rs2228313 [ dbSNP | Ensembl ].
VAR_049551

Experimental info

Mutagenesis478 – 4814DRSR → AAAA: Loss of cleavage by S2P. Ref.6 Ref.8
Mutagenesis478 – 4814DRSR → AS: Loss of cleavage by S2P. Ref.6 Ref.8
Mutagenesis4781D → A: No effect on proteolytic processing in response to low sterol. Ref.6
Mutagenesis479 – 4813RSR → AAA: Loss of cleavage by S2P. Ref.8
Mutagenesis4791R → A: No effect on cleavage by S2P. Ref.8
Mutagenesis4811R → A: No effect on cleavage by S2P. Ref.8
Mutagenesis484 – 4852LC → FF: No effect on cleavage by S2P. Ref.8
Mutagenesis4841L → A: No effect on cleavage by S2P. Ref.8
Mutagenesis4851C → A: No effect on cleavage by S2P. Ref.8
Mutagenesis490 – 4912LC → NP: Restores cleavage by S2P; when associated with F-495 and L-496. No effect on site of cleavage by S2P.
Mutagenesis495 – 4962NP → FL: Loss of cleavage by S2P. Ref.9
Mutagenesis4951N → F: Reduced cleavage by S2P. Ref.9
Mutagenesis4961P → L: Reduced cleavage by S2P. Ref.9
Mutagenesis5191R → A: Loss of proteolytic processing in response to low sterol. Ref.6
Mutagenesis5191R → K: No effect on proteolytic processing in response to low sterol. Ref.6
Sequence conflict9611A → G in AAA50746. Ref.1
Sequence conflict10451A → G in AAA50746. Ref.1

Secondary structure

...... 1141
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 481B1D8E2A2306D2

FASTA1,141123,688
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7006587698A23FF8
Show »

FASTA68173,153

References

« Hide '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] (ISOFORM 1), 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] (ISOFORM 1).
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
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. expand/collapse author list , 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.
BC051385 mRNA. Translation: AAH51385.1.
BC051799 mRNA. Translation: AAH51799.1. Different initiation.
BC056158 mRNA. Translation: AAH56158.1.
PIRA54962. A49397.
RefSeqNP_004590.2. NM_004599.3.
UniGeneHs.443258.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKLX-ray3.00C/D/E/F343-403[»]
ProteinModelPortalQ12772.
SMRQ12772. Positions 343-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112599. 57 interactions.
DIPDIP-263N.
IntActQ12772. 45 interactions.
MINTMINT-144301.
STRING9606.ENSP00000354476.

Chemistry

BindingDBQ12772.
ChEMBLCHEMBL1795166.

PTM databases

PhosphoSiteQ12772.

Polymorphism databases

DMDM116242800.

Proteomic databases

PaxDbQ12772.
PRIDEQ12772.

Protocols and materials databases

DNASU6721.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361204; ENSP00000354476; ENSG00000198911.
GeneID6721.
KEGGhsa:6721.
UCSCuc003bbi.3. human.

Organism-specific databases

CTD6721.
GeneCardsGC22P042273.
HGNCHGNC:11290. SREBF2.
HPAHPA031962.
MIM600481. gene.
neXtProtNX_Q12772.
PharmGKBPA336.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242942.
HOGENOMHOG000007091.
HOVERGENHBG061592.
InParanoidQ12772.
KOK09107.
OMADVICRWW.
OrthoDBEOG7D85VS.
PhylomeDBQ12772.
TreeFamTF313894.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressQ12772.
BgeeQ12772.
CleanExHS_SREBF2.
GenevestigatorQ12772.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12772.
GeneWikiSREBF2.
GenomeRNAi6721.
NextBio26218.
PMAP-CutDBQ12772.
PROQ12772.
SOURCESearch...

Entry information

Entry nameSRBP2_HUMAN
AccessionPrimary (citable) accession number: Q12772
Secondary accession number(s): Q05BD5 expand/collapse secondary AC list , Q6GTH7, Q86V36, Q9UH04
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM