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Protein

Sterol regulatory element-binding protein 1

Gene

SREBF1

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 fatty acid and to a lesser degree the cholesterol synthesis pathway (By similarity). Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').By similarity

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:ENSG00000072310-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP36956.
SIGNORiP36956.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol regulatory element-binding protein 1
Short name:
SREBP-1
Alternative name(s):
Class D basic helix-loop-helix protein 1
Short name:
bHLHd1
Sterol regulatory element-binding transcription factor 1
Cleaved into the following chain:
Gene namesi
Name:SREBF1
Synonyms:BHLHD1, SREBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11289. SREBF1.

Subcellular locationi

Processed sterol regulatory element-binding protein 1 :
  • Nucleus By similarity
Isoform SREBP-1aDelta :
Isoform SREBP-1cDelta :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 487CytoplasmicSequence analysisAdd BLAST487
Transmembranei488 – 508HelicalSequence analysisAdd BLAST21
Topological domaini509 – 547LumenalSequence analysisAdd BLAST39
Transmembranei548 – 568HelicalSequence analysisAdd BLAST21
Topological domaini569 – 1147CytoplasmicSequence analysisAdd BLAST579

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
  • integral component of membrane Source: UniProtKB-KW
  • nuclear envelope Source: ProtInc
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi455S → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi456D → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi457S → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi460D → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi466D → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi481G → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi482M → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi483L → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi484 – 487DRSR → AS: Strong reduction of proteolytic processing in response to low sterol. 1 Publication4
Mutagenesisi484D → A: Loss of proteolytic processing in response to low sterol. 1 Publication1
Mutagenesisi485R → A: No effect on proteolytic processing. 1 Publication1
Mutagenesisi527R → A: Loss of proteolytic processing in response to low sterol. 1 Publication1

Organism-specific databases

DisGeNETi6720.
OpenTargetsiENSG00000072310.
PharmGKBiPA335.

Polymorphism and mutation databases

BioMutaiSREBF1.
DMDMi166897633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001274471 – 1147Sterol regulatory element-binding protein 1Add BLAST1147
ChainiPRO_00003140291 – 490Processed sterol regulatory element-binding protein 1Add BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98PhosphoserineBy similarity1
Modified residuei117PhosphoserineCombined sources1
Modified residuei337Phosphoserine; by SIK1By similarity1
Modified residuei338Phosphoserine; by SIK1By similarity1
Modified residuei396Phosphoserine; by AMPKBy similarity1
Modified residuei402Phosphoserine; by SIK1By similarity1
Modified residuei457PhosphoserineBy similarity1
Modified residuei1060PhosphoserineCombined sources1

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.
Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. Phosphorylation at Ser-402 by SIK1 represses activity possibly by inhibiting DNA-binding (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei460 – 461Cleavage; by caspase-3 and caspase-7By similarity2
Sitei490 – 491Cleavage; by S2PBy similarity2
Sitei530 – 531Cleavage; by S1PCurated2

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36956.
PaxDbiP36956.
PeptideAtlasiP36956.
PRIDEiP36956.

PTM databases

iPTMnetiP36956.
PhosphoSitePlusiP36956.

Miscellaneous databases

PMAP-CutDBP36956.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues, most abundant in liver and adrenal gland. In fetal tissues lung and liver shows highest expression. Isoform SREBP-1C predominates in liver, adrenal gland and ovary, whereas isoform SREBP-1A predominates in hepatoma cell lines. Isoform SREBP-1A and isoform SREBP-1C are found in kidney, brain, white fat, and muscle.

Gene expression databases

BgeeiENSG00000072310.
CleanExiHS_SREBF1.
ExpressionAtlasiP36956. baseline and differential.
GenevisibleiP36956. HS.

Organism-specific databases

HPAiCAB005406.
HPA043343.
HPA043878.

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. Interacts with CEBPA, the interaction produces a transcriptional synergy (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CrebbpP454812EBI-948328,EBI-296306From a different organism.
MED15Q96RN56EBI-948328,EBI-394506
SIRT1Q96EB62EBI-948338,EBI-1802965

Protein-protein interaction databases

BioGridi112598. 60 interactors.
DIPiDIP-331N.
IntActiP36956. 16 interactors.
MINTiMINT-2803077.
STRINGi9606.ENSP00000348069.

Structurei

Secondary structure

11147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi321 – 350Combined sources30
Helixi359 – 396Combined sources38

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AM9X-ray2.30A/B/C/D319-400[»]
ProteinModelPortaliP36956.
SMRiP36956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini323 – 373bHLHPROSITE-ProRule annotationAdd BLAST51

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 60Transcriptional activation (acidic)Add BLAST60
Regioni234 – 497Interaction with LMNABy similarityAdd BLAST264
Regioni373 – 394Leucine-zipperAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi61 – 178Pro/Ser-richAdd BLAST118
Compositional biasi427 – 462Gly/Pro/Ser-richAdd BLAST36

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

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiP36956.
KOiK07197.
OMAiGKYTGGH.
OrthoDBiEOG091G01RE.
PhylomeDBiP36956.
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 (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform SREBP-1A (identifier: P36956-1) [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
MDEPPFSEAA LEQALGEPCD LDAALLTDIE DMLQLINNQD SDFPGLFDPP
60 70 80 90 100
YAGSGAGGTD PASPDTSSPG SLSPPPATLS SSLEAFLSGP QAAPSPLSPP
110 120 130 140 150
QPAPTPLKMY PSMPAFSPGP GIKEESVPLS ILQTPTPQPL PGALLPQSFP
160 170 180 190 200
APAPPQFSST PVLGYPSPPG GFSTGSPPGN TQQPLPGLPL ASPPGVPPVS
210 220 230 240 250
LHTQVQSVVP QQLLTVTAAP TAAPVTTTVT SQIQQVPVLL QPHFIKADSL
260 270 280 290 300
LLTAMKTDGA TVKAAGLSPL VSGTTVQTGP LPTLVSGGTI LATVPLVVDA
310 320 330 340 350
EKLPINRLAA GSKAPASAQS RGEKRTAHNA IEKRYRSSIN DKIIELKDLV
360 370 380 390 400
VGTEAKLNKS AVLRKAIDYI RFLQHSNQKL KQENLSLRTA VHKSKSLKDL
410 420 430 440 450
VSACGSGGNT DVLMEGVKTE VEDTLTPPPS DAGSPFQSSP LSLGSRGSGS
460 470 480 490 500
GGSGSDSEPD SPVFEDSKAK PEQRPSLHSR GMLDRSRLAL CTLVFLCLSC
510 520 530 540 550
NPLASLLGAR GLPSPSDTTS VYHSPGRNVL GTESRDGPGW AQWLLPPVVW
560 570 580 590 600
LLNGLLVLVS LVLLFVYGEP VTRPHSGPAV YFWRHRKQAD LDLARGDFAQ
610 620 630 640 650
AAQQLWLALR ALGRPLPTSH LDLACSLLWN LIRHLLQRLW VGRWLAGRAG
660 670 680 690 700
GLQQDCALRV DASASARDAA LVYHKLHQLH TMGKHTGGHL TATNLALSAL
710 720 730 740 750
NLAECAGDAV SVATLAEIYV AAALRVKTSL PRALHFLTRF FLSSARQACL
760 770 780 790 800
AQSGSVPPAM QWLCHPVGHR FFVDGDWSVL STPWESLYSL AGNPVDPLAQ
810 820 830 840 850
VTQLFREHLL ERALNCVTQP NPSPGSADGD KEFSDALGYL QLLNSCSDAA
860 870 880 890 900
GAPAYSFSIS SSMATTTGVD PVAKWWASLT AVVIHWLRRD EEAAERLCPL
910 920 930 940 950
VEHLPRVLQE SERPLPRAAL HSFKAARALL GCAKAESGPA SLTICEKASG
960 970 980 990 1000
YLQDSLATTP ASSSIDKAVQ LFLCDLLLVV RTSLWRQQQP PAPAPAAQGT
1010 1020 1030 1040 1050
SSRPQASALE LRGFQRDLSS LRRLAQSFRP AMRRVFLHEA TARLMAGASP
1060 1070 1080 1090 1100
TRTHQLLDRS LRRRAGPGGK GGAVAELEPR PTRREHAEAL LLASCYLPPG
1110 1120 1130 1140
FLSAPGQRVG MLAEAARTLE KLGDRRLLHD CQQMLMRLGG GTTVTSS
Length:1,147
Mass (Da):121,675
Last modified:February 5, 2008 - v2
Checksum:i58F28870739FF259
GO
Isoform SREBP-1B (identifier: P36956-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,071
Mass (Da):113,562
Checksum:iB71B6010CDB8D1ED
GO
Isoform SREBP-1C (identifier: P36956-3) [UniParc]FASTAAdd to basket

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

Note: Predominantly expressed in liver and adipose tissues.
Show »
Length:1,047
Mass (Da):111,102
Checksum:i05CF039C7707AFB9
GO
Isoform 4 (identifier: P36956-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:1,177
Mass (Da):124,635
Checksum:i1C9257FFC7FC7FEB
GO
Isoform SREBP-1aDelta (identifier: P36956-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     469-470: AK → TE
     471-1147: Missing.

Note: The absence of Golgi proteolytic processing requirement makes this isoform constitutively active in transactivation of lipogenic gene promoters.
Show »
Length:470
Mass (Da):48,276
Checksum:iB6BEDC238A020B8F
GO
Isoform SREBP-1cDelta (identifier: P36956-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MDEPPFSEAALEQALGEPCDLDAALLTDI → MDCTF
     469-470: AK → TE
     471-1147: Missing.

Note: The absence of Golgi proteolytic processing requirement makes this isoform constitutively active in transactivation of lipogenic gene promoters.
Show »
Length:446
Mass (Da):45,816
Checksum:iB1C64DDD71DEEDEC
GO

Sequence cautioni

The sequence AAB28522 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92846 differs from that shown. Intron retention.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038468306N → S.1 PublicationCorresponds to variant rs17855793dbSNPEnsembl.1
Natural variantiVAR_038469309A → T.Corresponds to variant rs35188700dbSNPEnsembl.1
Natural variantiVAR_038470417V → M.Corresponds to variant rs2229590dbSNPEnsembl.1
Natural variantiVAR_038471580V → M.Corresponds to variant rs36215896dbSNPEnsembl.1
Natural variantiVAR_038472746R → H.Corresponds to variant rs2228461dbSNPEnsembl.1
Natural variantiVAR_038473834S → L.1 PublicationCorresponds to variant rs17855792dbSNPEnsembl.1
Natural variantiVAR_0384741000T → A.2 PublicationsCorresponds to variant rs1042017dbSNPEnsembl.1
Natural variantiVAR_0384751008A → P.Corresponds to variant rs35014224dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0021491 – 29MDEPP…LLTDI → MDCTF in isoform SREBP-1C and isoform SREBP-1cDelta. 2 PublicationsAdd BLAST29
Alternative sequenceiVSP_03085930E → EGEVGAGRGRANGLDAPRAG ADRGAMDCTFE in isoform 4. 1 Publication1
Alternative sequenceiVSP_047598469 – 470AK → TE in isoform SREBP-1aDelta and isoform SREBP-1cDelta. 1 Publication2
Alternative sequenceiVSP_047599471 – 1147Missing in isoform SREBP-1aDelta and isoform SREBP-1cDelta. 1 PublicationAdd BLAST677
Alternative sequenceiVSP_0021501035 – 1147VFLHE…TVTSS → LMDVLTSESAWALPQHLGKG FPSPSGHKVPGWHGRMD in isoform SREBP-1B and isoform SREBP-1C. 1 PublicationAdd BLAST113

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00968 mRNA. Translation: AAC50051.2.
S66167 mRNA. Translation: AAB28522.2. Different initiation.
S66168 mRNA. Translation: AAB28523.1.
AB373958 mRNA. Translation: BAG06742.1.
AB373959 mRNA. Translation: BAG06743.1.
AC122129 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55689.1.
CH471196 Genomic DNA. Translation: EAW55690.1.
BC023621 mRNA. Translation: AAH23621.1.
BC026962 mRNA. Translation: AAH26962.1.
BC057388 mRNA. Translation: AAH57388.1.
BC063281 mRNA. Translation: AAH63281.1.
AB209609 mRNA. Translation: BAD92846.1. Sequence problems.
CCDSiCCDS11189.1. [P36956-1]
CCDS32583.1. [P36956-4]
PIRiA48845.
RefSeqiNP_001005291.1. NM_001005291.2. [P36956-4]
NP_004167.3. NM_004176.4. [P36956-1]
UniGeneiHs.592123.
Hs.733635.

Genome annotation databases

EnsembliENST00000261646; ENSP00000261646; ENSG00000072310. [P36956-1]
ENST00000355815; ENSP00000348069; ENSG00000072310. [P36956-4]
GeneIDi6720.
KEGGihsa:6720.
UCSCiuc002grt.3. human. [P36956-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Sterol regulatory element-binding protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00968 mRNA. Translation: AAC50051.2.
S66167 mRNA. Translation: AAB28522.2. Different initiation.
S66168 mRNA. Translation: AAB28523.1.
AB373958 mRNA. Translation: BAG06742.1.
AB373959 mRNA. Translation: BAG06743.1.
AC122129 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55689.1.
CH471196 Genomic DNA. Translation: EAW55690.1.
BC023621 mRNA. Translation: AAH23621.1.
BC026962 mRNA. Translation: AAH26962.1.
BC057388 mRNA. Translation: AAH57388.1.
BC063281 mRNA. Translation: AAH63281.1.
AB209609 mRNA. Translation: BAD92846.1. Sequence problems.
CCDSiCCDS11189.1. [P36956-1]
CCDS32583.1. [P36956-4]
PIRiA48845.
RefSeqiNP_001005291.1. NM_001005291.2. [P36956-4]
NP_004167.3. NM_004176.4. [P36956-1]
UniGeneiHs.592123.
Hs.733635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AM9X-ray2.30A/B/C/D319-400[»]
ProteinModelPortaliP36956.
SMRiP36956.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112598. 60 interactors.
DIPiDIP-331N.
IntActiP36956. 16 interactors.
MINTiMINT-2803077.
STRINGi9606.ENSP00000348069.

PTM databases

iPTMnetiP36956.
PhosphoSitePlusiP36956.

Polymorphism and mutation databases

BioMutaiSREBF1.
DMDMi166897633.

Proteomic databases

MaxQBiP36956.
PaxDbiP36956.
PeptideAtlasiP36956.
PRIDEiP36956.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261646; ENSP00000261646; ENSG00000072310. [P36956-1]
ENST00000355815; ENSP00000348069; ENSG00000072310. [P36956-4]
GeneIDi6720.
KEGGihsa:6720.
UCSCiuc002grt.3. human. [P36956-1]

Organism-specific databases

CTDi6720.
DisGeNETi6720.
GeneCardsiSREBF1.
HGNCiHGNC:11289. SREBF1.
HPAiCAB005406.
HPA043343.
HPA043878.
MIMi184756. gene.
neXtProtiNX_P36956.
OpenTargetsiENSG00000072310.
PharmGKBiPA335.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiP36956.
KOiK07197.
OMAiGKYTGGH.
OrthoDBiEOG091G01RE.
PhylomeDBiP36956.
TreeFamiTF313894.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000072310-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP36956.
SIGNORiP36956.

Miscellaneous databases

ChiTaRSiSREBF1. human.
EvolutionaryTraceiP36956.
GeneWikiiSREBF1.
GenomeRNAii6720.
PMAP-CutDBP36956.
PROiP36956.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072310.
CleanExiHS_SREBF1.
ExpressionAtlasiP36956. baseline and differential.
GenevisibleiP36956. 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...

Entry informationi

Entry nameiSRBP1_HUMAN
AccessioniPrimary (citable) accession number: P36956
Secondary accession number(s): B0I4X3
, B0I4X4, D3DXC4, Q16062, Q59F52, Q6P4R7, Q6PFW7, Q6PJ36, Q8TAK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 5, 2008
Last modified: November 2, 2016
This is version 181 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 17
    Human chromosome 17: 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

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 one 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.