Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sterol regulatory element-binding protein 2

Gene

SREBF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei468 – 4692Cleavage; by caspase-3 and caspase-7
Sitei484 – 4852Cleavage; by S2P
Sitei522 – 5232Cleavage; by S1P

GO - Molecular functioni

  • E-box binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB

GO - Biological processi

  • cellular response to laminar fluid shear stress Source: BHF-UCL
  • cellular response to starvation Source: ParkinsonsUK-UCL
  • cholesterol metabolic process Source: UniProtKB-KW
  • lipid metabolic process Source: ProtInc
  • negative regulation of cholesterol efflux Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • positive regulation of cholesterol storage Source: BHF-UCL
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of cholesterol homeostasis Source: Ensembl
  • regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  • response to low-density lipoprotein particle Source: BHF-UCL
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:SREBF2
Synonyms:BHLHD2, SREBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11290. SREBF2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 479479CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei480 – 50021HelicalSequence AnalysisAdd
BLAST
Topological domaini501 – 53333LumenalSequence AnalysisAdd
BLAST
Transmembranei534 – 55421HelicalSequence AnalysisAdd
BLAST
Topological domaini555 – 1139585CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • ER to Golgi transport vesicle membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: Reactome
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • SREBP-SCAP-Insig complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi478 – 4814DRSR → AAAA: Loss of cleavage by S2P. 2 Publications
Mutagenesisi478 – 4814DRSR → AS: Loss of cleavage by S2P. 2 Publications
Mutagenesisi478 – 4781D → A: No effect on proteolytic processing in response to low sterol. 1 Publication
Mutagenesisi479 – 4813RSR → AAA: Loss of cleavage by S2P. 1 Publication
Mutagenesisi479 – 4791R → A: No effect on cleavage by S2P. 1 Publication
Mutagenesisi481 – 4811R → A: No effect on cleavage by S2P. 1 Publication
Mutagenesisi484 – 4852LC → FF: No effect on cleavage by S2P. 1 Publication
Mutagenesisi484 – 4841L → A: No effect on cleavage by S2P. 1 Publication
Mutagenesisi485 – 4851C → A: No effect on cleavage by S2P. 1 Publication
Mutagenesisi490 – 4912LC → NP: Restores cleavage by S2P; when associated with F-495 and L-496. No effect on site of cleavage by S2P. 1 Publication
Mutagenesisi495 – 4962NP → FL: Loss of cleavage by S2P. 1 Publication
Mutagenesisi495 – 4951N → F: Reduced cleavage by S2P. 1 Publication
Mutagenesisi496 – 4961P → L: Reduced cleavage by S2P. 1 Publication
Mutagenesisi519 – 5191R → A: Loss of proteolytic processing in response to low sterol. 1 Publication
Mutagenesisi519 – 5191R → K: No effect on proteolytic processing in response to low sterol. 1 Publication

Organism-specific databases

PharmGKBiPA336.

Polymorphism and mutation databases

BioMutaiSREBF2.
DMDMi116242800.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11411141Sterol regulatory element-binding protein 2PRO_0000127452Add
BLAST
Chaini1 – 484484Processed sterol regulatory element-binding protein 2PRO_0000314033Add
BLAST

Post-translational modificationi

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-7.3 Publications
Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12772.
PaxDbiQ12772.
PRIDEiQ12772.

PTM databases

PhosphoSiteiQ12772.

Miscellaneous databases

PMAP-CutDBQ12772.

Expressioni

Tissue specificityi

Ubiquitously expressed in adult and fetal tissues.

Gene expression databases

BgeeiQ12772.
CleanExiHS_SREBF2.
ExpressionAtlasiQ12772. baseline and differential.
GenevisibleiQ12772. HS.

Organism-specific databases

HPAiHPA031962.

Interactioni

Subunit structurei

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-terminal domain) with RNF139.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HNF4AP412352EBI-465059,EBI-1049011
SP1P080473EBI-465059,EBI-298336
TP53P046373EBI-465059,EBI-366083

Protein-protein interaction databases

BioGridi112599. 66 interactions.
DIPiDIP-263N.
IntActiQ12772. 46 interactions.
MINTiMINT-144301.
STRINGi9606.ENSP00000354476.

Structurei

Secondary structure

1
1141
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi346 – 35712Combined sources
Turni366 – 3683Combined sources
Helixi369 – 39931Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKLX-ray3.00C/D/E/F343-403[»]
ProteinModelPortaliQ12772.
SMRiQ12772. Positions 343-403.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini330 – 38051bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5050Transcriptional activation (acidic)Add
BLAST
Regioni237 – 491255Interaction with LMNABy similarityAdd
BLAST
Regioni380 – 40122Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi52 – 12473Gly/Pro/Ser-richAdd
BLAST
Compositional biasi125 – 244120Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the SREBP family.Curated
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242942.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000186198.
HOVERGENiHBG061592.
InParanoidiQ12772.
KOiK09107.
OMAiDVICRWW.
OrthoDBiEOG7D85VS.
PhylomeDBiQ12772.
TreeFamiTF313894.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12772-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDDSGELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFPDLFSEQL
60 70 80 90 100
CSSFPGSGGS GSSSGSSGSS SSSSNGRGSS SGAVDPSVQR SFTQVTLPSF
110 120 130 140 150
SPSAASPQAP TLQVKVSPTS VPTTPRATPI LQPRPQPQPQ PQTQLQQQTV
160 170 180 190 200
MITPTFSTTP QTRIIQQPLI YQNAATSFQV LQPQVQSLVT SSQVQPVTIQ
210 220 230 240 250
QQVQTVQAQR VLTQTANGTL QTLAPATVQT VAAPQVQQVP VLVQPQIIKT
260 270 280 290 300
DSLVLTTLKT DGSPVMAAVQ NPALTALTTP IQTAALQVPT LVGSSGTILT
310 320 330 340 350
TMPVMMGQEK VPIKQVPGGV KQLEPPKEGE RRTTHNIIEK RYRSSINDKI
360 370 380 390 400
IELKDLVMGT DAKMHKSGVL RKAIDYIKYL QQVNHKLRQE NMVLKLANQK
410 420 430 440 450
NKLLKGIDLG SLVDNEVDLK IEDFNQNVLL MSPPASDSGS QAGFSPYSID
460 470 480 490 500
SEPGSPLLDD AKVKDEPDSP PVALGMVDRS RILLCVLTFL CLSFNPLTSL
510 520 530 540 550
LQWGGAHDSD QHPHSGSGRS VLSFESGSGG WFDWMMPTLL LWLVNGVIVL
560 570 580 590 600
SVFVKLLVHG EPVIRPHSRS SVTFWRHRKQ ADLDLARGDF AAAAGNLQTC
610 620 630 640 650
LAVLGRALPT SRLDLACSLS WNVIRYSLQK LRLVRWLLKK VFQCRRATPA
660 670 680 690 700
TEAGFEDEAK TSARDAALAY HRLHQLHITG KLPAGSACSD VHMALCAVNL
710 720 730 740 750
AECAEEKIPP STLVEIHLTA AMGLKTRCGG KLGFLASYFL SRAQSLCGPE
760 770 780 790 800
HSAVPDSLRW LCHPLGQKFF MERSWSVKSA AKESLYCAQR NPADPIAQVH
810 820 830 840 850
QAFCKNLLER AIESLVKPQA KKKAGDQEEE SCEFSSALEY LKLLHSFVDS
860 870 880 890 900
VGVMSPPLSR SSVLKSALGP DIICRWWTSA ITVAISWLQG DDAAVRSHFT
910 920 930 940 950
KVERIPKALE VTESPLVKAI FHACRAMHAS LPGKADGQQS SFCHCERASG
960 970 980 990 1000
HLWSSLNVSG ATSDPALNHV VQLLTCDLLL SLRTALWQKQ ASASQAVGET
1010 1020 1030 1040 1050
YHASGAELAG FQRDLGSLRR LAHSFRPAYR KVFLHEATVR LMAGASPTRT
1060 1070 1080 1090 1100
HQLLEHSLRR RTTQSTKHGE VDAWPGQRER ATAILLACRH LPLSFLSSPG
1110 1120 1130 1140
QRAVLLAEAA RTLEKVGDRR SCNDCQQMIV KLGGGTAIAA S
Length:1,141
Mass (Da):123,688
Last modified:October 17, 2006 - v2
Checksum:i481B1D8E2A2306D2
GO
Isoform 2 (identifier: Q12772-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:681
Mass (Da):73,153
Checksum:i7006587698A23FF8
GO

Sequence cautioni

The sequence AAH51799.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti961 – 9611A → G in AAA50746 (PubMed:7903453).Curated
Sequence conflicti1045 – 10451A → G in AAA50746 (PubMed:7903453).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti273 – 2731A → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036394
Natural varianti347 – 3471N → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036395
Natural varianti536 – 5361M → L.
Corresponds to variant rs17002714 [ dbSNP | Ensembl ].
VAR_049550
Natural varianti595 – 5951G → A.1 Publication
Corresponds to variant rs2228314 [ dbSNP | Ensembl ].
VAR_028440
Natural varianti623 – 6231V → M.
Corresponds to variant rs2229440 [ dbSNP | Ensembl ].
VAR_028441
Natural varianti860 – 8601R → S.
Corresponds to variant rs2228313 [ dbSNP | Ensembl ].
VAR_049551

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei273 – 2753Missing in isoform 2. 1 PublicationVSP_054283
Alternative sequencei589 – 68496DFAAA…GKLPA → VYGKKSGATHSIEEELNIHI SRGTRTRTLLSSRRFCSCCR QPTNLPGSFGPGTAHLPPGP GLQPLLERDPLQPAEATPGA LAAQESLPVPAGHASH in isoform 2. 1 PublicationVSP_054284Add
BLAST
Alternative sequencei685 – 1141457Missing in isoform 2. 1 PublicationVSP_054285Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14023.1. [Q12772-1]
PIRiA49397. A54962.
RefSeqiNP_004590.2. NM_004599.3. [Q12772-1]
UniGeneiHs.443258.

Genome annotation databases

EnsembliENST00000361204; ENSP00000354476; ENSG00000198911. [Q12772-1]
GeneIDi6721.
KEGGihsa:6721.
UCSCiuc003bbi.3. human. [Q12772-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14023.1. [Q12772-1]
PIRiA49397. A54962.
RefSeqiNP_004590.2. NM_004599.3. [Q12772-1]
UniGeneiHs.443258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKLX-ray3.00C/D/E/F343-403[»]
ProteinModelPortaliQ12772.
SMRiQ12772. Positions 343-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112599. 66 interactions.
DIPiDIP-263N.
IntActiQ12772. 46 interactions.
MINTiMINT-144301.
STRINGi9606.ENSP00000354476.

Chemistry

BindingDBiQ12772.
ChEMBLiCHEMBL1795166.

PTM databases

PhosphoSiteiQ12772.

Polymorphism and mutation databases

BioMutaiSREBF2.
DMDMi116242800.

Proteomic databases

MaxQBiQ12772.
PaxDbiQ12772.
PRIDEiQ12772.

Protocols and materials databases

DNASUi6721.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361204; ENSP00000354476; ENSG00000198911. [Q12772-1]
GeneIDi6721.
KEGGihsa:6721.
UCSCiuc003bbi.3. human. [Q12772-1]

Organism-specific databases

CTDi6721.
GeneCardsiGC22P042287.
HGNCiHGNC:11290. SREBF2.
HPAiHPA031962.
MIMi600481. gene.
neXtProtiNX_Q12772.
PharmGKBiPA336.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG242942.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000186198.
HOVERGENiHBG061592.
InParanoidiQ12772.
KOiK09107.
OMAiDVICRWW.
OrthoDBiEOG7D85VS.
PhylomeDBiQ12772.
TreeFamiTF313894.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

EvolutionaryTraceiQ12772.
GeneWikiiSREBF2.
GenomeRNAii6721.
NextBioi26218.
PMAP-CutDBQ12772.
PROiQ12772.
SOURCEiSearch...

Gene expression databases

BgeeiQ12772.
CleanExiHS_SREBF2.
ExpressionAtlasiQ12772. baseline and differential.
GenevisibleiQ12772. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-273 AND LYS-347.

Entry informationi

Entry nameiSRBP2_HUMAN
AccessioniPrimary (citable) accession number: Q12772
Secondary accession number(s): Q05BD5
, Q6GTH7, Q86V36, Q9UH04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.