Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q12772

- SRBP2_HUMAN

UniProt

Q12772 - SRBP2_HUMAN

Protein

Sterol regulatory element-binding protein 2

Gene

SREBF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. E-box binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein C-terminus binding Source: UniProtKB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. cellular response to laminar fluid shear stress Source: BHF-UCL
    3. cholesterol metabolic process Source: UniProtKB-KW
    4. lipid metabolic process Source: ProtInc
    5. negative regulation of cholesterol efflux Source: BHF-UCL
    6. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    7. positive regulation of cholesterol storage Source: BHF-UCL
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. regulation of cholesterol homeostasis Source: Ensembl
    10. regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. response to low-density lipoprotein particle Source: BHF-UCL
    12. small molecule metabolic process Source: Reactome
    13. transcription, DNA-templated Source: UniProtKB-KW

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11290. SREBF2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: Reactome
    5. ER to Golgi transport vesicle membrane Source: UniProtKB-SubCell
    6. Golgi membrane Source: Reactome
    7. nucleolus Source: HPA
    8. nucleoplasm Source: Reactome
    9. nucleus Source: UniProtKB
    10. SREBP-SCAP-Insig complex Source: UniProtKB

    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. 1 Publication
    Mutagenesisi478 – 4814DRSR → AS: Loss of cleavage by S2P. 1 Publication
    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.
    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.

    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

    ArrayExpressiQ12772.
    BgeeiQ12772.
    CleanExiHS_SREBF2.
    GenevestigatoriQ12772.

    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
    SP1P080473EBI-465059,EBI-298336
    TP53P046373EBI-465059,EBI-366083

    Protein-protein interaction databases

    BioGridi112599. 57 interactions.
    DIPiDIP-263N.
    IntActiQ12772. 45 interactions.
    MINTiMINT-144301.
    STRINGi9606.ENSP00000354476.

    Structurei

    Secondary structure

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

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ12772.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei480 – 50021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei534 – 55421HelicalSequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000007091.
    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. Align

    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

    MDDSGELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFPDLFSEQL     50
    CSSFPGSGGS GSSSGSSGSS SSSSNGRGSS SGAVDPSVQR SFTQVTLPSF 100
    SPSAASPQAP TLQVKVSPTS VPTTPRATPI LQPRPQPQPQ PQTQLQQQTV 150
    MITPTFSTTP QTRIIQQPLI YQNAATSFQV LQPQVQSLVT SSQVQPVTIQ 200
    QQVQTVQAQR VLTQTANGTL QTLAPATVQT VAAPQVQQVP VLVQPQIIKT 250
    DSLVLTTLKT DGSPVMAAVQ NPALTALTTP IQTAALQVPT LVGSSGTILT 300
    TMPVMMGQEK VPIKQVPGGV KQLEPPKEGE RRTTHNIIEK RYRSSINDKI 350
    IELKDLVMGT DAKMHKSGVL RKAIDYIKYL QQVNHKLRQE NMVLKLANQK 400
    NKLLKGIDLG SLVDNEVDLK IEDFNQNVLL MSPPASDSGS QAGFSPYSID 450
    SEPGSPLLDD AKVKDEPDSP PVALGMVDRS RILLCVLTFL CLSFNPLTSL 500
    LQWGGAHDSD QHPHSGSGRS VLSFESGSGG WFDWMMPTLL LWLVNGVIVL 550
    SVFVKLLVHG EPVIRPHSRS SVTFWRHRKQ ADLDLARGDF AAAAGNLQTC 600
    LAVLGRALPT SRLDLACSLS WNVIRYSLQK LRLVRWLLKK VFQCRRATPA 650
    TEAGFEDEAK TSARDAALAY HRLHQLHITG KLPAGSACSD VHMALCAVNL 700
    AECAEEKIPP STLVEIHLTA AMGLKTRCGG KLGFLASYFL SRAQSLCGPE 750
    HSAVPDSLRW LCHPLGQKFF MERSWSVKSA AKESLYCAQR NPADPIAQVH 800
    QAFCKNLLER AIESLVKPQA KKKAGDQEEE SCEFSSALEY LKLLHSFVDS 850
    VGVMSPPLSR SSVLKSALGP DIICRWWTSA ITVAISWLQG DDAAVRSHFT 900
    KVERIPKALE VTESPLVKAI FHACRAMHAS LPGKADGQQS SFCHCERASG 950
    HLWSSLNVSG ATSDPALNHV VQLLTCDLLL SLRTALWQKQ ASASQAVGET 1000
    YHASGAELAG FQRDLGSLRR LAHSFRPAYR KVFLHEATVR LMAGASPTRT 1050
    HQLLEHSLRR RTTQSTKHGE VDAWPGQRER ATAILLACRH LPLSFLSSPG 1100
    QRAVLLAEAA RTLEKVGDRR SCNDCQQMIV KLGGGTAIAA S 1141
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi116242800.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14023.1. [Q12772-1 ]
    PIRi A49397. A54962.
    RefSeqi NP_004590.2. NM_004599.3. [Q12772-1 ]
    UniGenei Hs.443258.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UKL X-ray 3.00 C/D/E/F 343-403 [» ]
    ProteinModelPortali Q12772.
    SMRi Q12772. Positions 343-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112599. 57 interactions.
    DIPi DIP-263N.
    IntActi Q12772. 45 interactions.
    MINTi MINT-144301.
    STRINGi 9606.ENSP00000354476.

    Chemistry

    BindingDBi Q12772.
    ChEMBLi CHEMBL1795166.

    PTM databases

    PhosphoSitei Q12772.

    Polymorphism databases

    DMDMi 116242800.

    Proteomic databases

    MaxQBi Q12772.
    PaxDbi Q12772.
    PRIDEi Q12772.

    Protocols and materials databases

    DNASUi 6721.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361204 ; ENSP00000354476 ; ENSG00000198911 . [Q12772-1 ]
    GeneIDi 6721.
    KEGGi hsa:6721.
    UCSCi uc003bbi.3. human. [Q12772-1 ]

    Organism-specific databases

    CTDi 6721.
    GeneCardsi GC22P042273.
    HGNCi HGNC:11290. SREBF2.
    HPAi HPA031962.
    MIMi 600481. gene.
    neXtProti NX_Q12772.
    PharmGKBi PA336.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242942.
    HOGENOMi HOG000007091.
    HOVERGENi HBG061592.
    InParanoidi Q12772.
    KOi K09107.
    OMAi DVICRWW.
    OrthoDBi EOG7D85VS.
    PhylomeDBi Q12772.
    TreeFami TF313894.

    Enzyme and pathway databases

    Reactomei REACT_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

    EvolutionaryTracei Q12772.
    GeneWikii SREBF2.
    GenomeRNAii 6721.
    NextBioi 26218.
    PMAP-CutDB Q12772.
    PROi Q12772.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12772.
    Bgeei Q12772.
    CleanExi HS_SREBF2.
    Genevestigatori Q12772.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 152 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