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Protein

Sterol regulatory element-binding protein 1

Gene

Srebf1

Organism
Rattus norvegicus (Rat)
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') (PubMed:7739539). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').By similarity1 Publication

GO - Molecular functioni

  • chromatin binding Source: RGD
  • DNA binding Source: UniProtKB
  • protein complex binding Source: RGD
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: RGD
  • sterol response element binding Source: HGNC
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: HGNC

GO - Biological processi

  • aging Source: RGD
  • cellular response to fatty acid Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to starvation Source: HGNC
  • cholesterol metabolic process Source: RGD
  • circadian rhythm Source: Ensembl
  • fat cell differentiation Source: Ensembl
  • insulin receptor signaling pathway Source: Ensembl
  • lipid biosynthetic process Source: UniProtKB
  • lung development Source: RGD
  • mRNA transcription from RNA polymerase II promoter Source: Ensembl
  • negative regulation of insulin secretion Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of cholesterol biosynthetic process Source: Ensembl
  • positive regulation of histone deacetylation Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • positive regulation of triglyceride biosynthetic process Source: UniProtKB
  • regulation of fatty acid metabolic process Source: Ensembl
  • regulation of heart rate by chemical signal Source: Ensembl
  • regulation of mitophagy Source: Ensembl
  • regulation of protein stability Source: Ensembl
  • regulation of protein targeting to mitochondrion Source: Ensembl
  • response to cAMP Source: RGD
  • response to drug Source: RGD
  • response to fatty acid Source: RGD
  • response to food Source: RGD
  • response to glucagon Source: RGD
  • response to glucose Source: Ensembl
  • response to insulin Source: BHF-UCL
  • response to lipid Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to progesterone Source: RGD
  • response to retinoic acid Source: RGD
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

ReactomeiR-RNO-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-RNO-2426168. Activation of gene expression by SREBF (SREBP).

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol regulatory element-binding protein 1
Short name:
SREBP-1
Alternative name(s):
Adipocyte determination- and differentiation-dependent factor 1
Short name:
ADD1
Sterol regulatory element-binding transcription factor 1
Cleaved into the following chain:
Gene namesi
Name:Srebf1
Synonyms:Srebp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi69423. Srebf1.

Subcellular locationi

Processed sterol regulatory element-binding protein 1 :
  • Nucleus By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 481481CytoplasmicSequence analysisAdd
BLAST
Transmembranei482 – 50221HelicalSequence analysisAdd
BLAST
Topological domaini503 – 53634LumenalSequence analysisAdd
BLAST
Transmembranei537 – 55721HelicalSequence analysisAdd
BLAST
Topological domaini558 – 1134577CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • ER to Golgi transport vesicle membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11341134Sterol regulatory element-binding protein 1PRO_0000127450Add
BLAST
Chaini1 – 480480Processed sterol regulatory element-binding protein 1PRO_0000314031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei331 – 3311Phosphoserine; by SIK1By similarity
Modified residuei332 – 3321Phosphoserine; by SIK1By similarity
Modified residuei389 – 3891Phosphoserine; by AMPKBy similarity
Modified residuei395 – 3951Phosphoserine; by SIK1By similarity
Modified residuei448 – 4481PhosphoserineCombined sources

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 (By similarity).By similarity
Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. Phosphorylation at Ser-395 by SIK1 represses activity possibly by inhibiting DNA-binding (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4522Cleavage; by caspase-3 and caspase-7By similarity
Sitei480 – 4812Cleavage; by S2PBy similarity
Sitei519 – 5202Cleavage; by S1PBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP56720.
PRIDEiP56720.

PTM databases

iPTMnetiP56720.
PhosphoSiteiP56720.

Expressioni

Tissue specificityi

Expressed predominantly in brown adipose tissue.

Gene expression databases

ExpressionAtlasiP56720. baseline and differential.
GenevisibleiP56720. RN.

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

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi249376. 8 interactions.
STRINGi10116.ENSRNOP00000050057.

Structurei

3D structure databases

ProteinModelPortaliP56720.
SMRiP56720. Positions 313-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini317 – 36751bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Transcriptional activation (acidic)By similarityAdd
BLAST
Regioni227 – 487261Interaction with LMNABy similarityAdd
BLAST
Regioni367 – 38822Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 176116Pro/Ser-richAdd
BLAST
Compositional biasi420 – 45334Gly/Pro/Ser-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

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiP56720.
KOiK07197.
OMAiGKYTGGH.
OrthoDBiEOG7D85VS.
PhylomeDBiP56720.
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 SREBP-1A (identifier: P56720-2) [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
MDELPFGEAA LEQALAEVCE MDAALLTDIE DMLQLINNQD SDFPGLFDAP
60 70 80 90 100
YAGGETGDTG PSSPGASSPE SFSSPASLGS SLEAFLGGPK VTPAPLSPPP
110 120 130 140 150
SAPTAVKMYP SVPPFSPGPG IKEEPVPLTI LQPPAPQPSP GTLLPPSFPP
160 170 180 190 200
PPVQLSPAPV LGYSSLPSGF SGTLPGNTQQ TPSSLPLGST PGISPTPLHT
210 220 230 240 250
QVQSSAAQQP PPASAAPRMS TVASQIQQVP VVLQPHFIKA DSLLLTAVKT
260 270 280 290 300
DTGATMKTAG INTLAPGTAV QAGPLQTLVS GGTILATVPL VVDTDKLPIH
310 320 330 340 350
RLAAGGKALG SAQSRGEKRT AHNAIEKRYR SSINDKIVEL KDLVVGTEAK
360 370 380 390 400
LNKSAVLRKA IDYIRFLQHS NQKLKQENLT LRSAHKSKSL KDLVSACGSG
410 420 430 440 450
GGTDVSMEGM KPEVVETLTP PPSDAGSPSQ SSPLSLGSRG SSSGGSDSEP
460 470 480 490 500
DSPAFEDNQV KAQRLPSHSR GMLDRSRLAL CVLVFLCLTC NPLASLFGWG
510 520 530 540 550
ILTPSDASGV HRSSGRSMLE AESRDGSNWT QWLLPPLVWL ANGLLVLACL
560 570 580 590 600
ALLFVYGEPV TRPHSGPAVH FWRHRKQADL DLARGDFAQA AQQLWLALQA
610 620 630 640 650
LGRPLPTSNL DLACSLLWNL VRHLLQRLWV GRWLAGQAGG LQRDYRLRKD
660 670 680 690 700
ARASARDAAV VYHKLHQLHA MGKYTGGHLV ASNLALSALN LAECAGDAIS
710 720 730 740 750
MATLAEIYVA AALRVKTSLP RALHFLTRFF LSSARQACLA QSGAVPLAMQ
760 770 780 790 800
WLCHPVGHRF FVDGDWAVHG APQESLYSVA GNPVDPLAQV TRLFCEHLLE
810 820 830 840 850
RALNCIAQPS PGAADGDREF SDALGYLQLL NSCSDAVGAP ACSFSVSSSM
860 870 880 890 900
ATTTGTDPVA KWWASLTAVV IHWLRRDEEA AERLYPLVEH IPQVLQETER
910 920 930 940 950
PLPRAALYSF KAARALLDHR KVESSPASLA ICEKASGYLR DSLASTSTAS
960 970 980 990 1000
SIDKAMQLLL CDLLLVARTS LWRRQQSAAS AQGAHGTSNG PQASALELRG
1010 1020 1030 1040 1050
FQHDLSSLRR LAQSFRPAMR RVFLHEATAR LMAGASPART HQLLDRSLRR
1060 1070 1080 1090 1100
RAGSSGKGGA AAELEPRPTW REHTEALLLA SCYLPPAFLS APGQRVSMLA
1110 1120 1130
EAARTVEKLG DHRLLLDCQQ MLLRLGGGTT VTSS
Length:1,134
Mass (Da):120,521
Last modified:February 5, 2008 - v3
Checksum:i1D31A9AD3C36AB29
GO
Isoform SREBP-1C (identifier: P56720-1) [UniParc]FASTAAdd to basket

Also known as: ADD1

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MDELPFGEAALEQALAEVCEMDAALLTDI → MDCTF

Show »
Length:1,110
Mass (Da):118,027
Checksum:iC7CDAE780EA056D3
GO

Sequence cautioni

The sequence L16995 differs from that shown. Reason: Frameshift at positions 902, 939, 956, 972 and 1016. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671G → A in L16995 (PubMed:15057822).Curated
Sequence conflicti475 – 4751R → P in L16995 (PubMed:15057822).Curated
Sequence conflicti817 – 8171D → H in L16995 (PubMed:15057822).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti779 – 7791V → M in spontaneously hypertensive rats. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MDELP…LLTDI → MDCTF in isoform SREBP-1C. 2 PublicationsVSP_030860Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073826 Genomic DNA. No translation available.
AABR03076830 Genomic DNA. No translation available.
L16995 mRNA. No translation available.
AF286469 mRNA. Translation: AAG28733.2.
AF286470 mRNA. Translation: AAG28734.2. Different termination.
RefSeqiNP_001263636.1. NM_001276707.1. [P56720-2]
UniGeneiRn.198857.

Genome annotation databases

EnsembliENSRNOT00000004753; ENSRNOP00000004753; ENSRNOG00000003463. [P56720-1]
ENSRNOT00000047053; ENSRNOP00000050057; ENSRNOG00000003463. [P56720-2]
GeneIDi78968.
KEGGirno:78968.
UCSCiRGD:69423. rat. [P56720-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073826 Genomic DNA. No translation available.
AABR03076830 Genomic DNA. No translation available.
L16995 mRNA. No translation available.
AF286469 mRNA. Translation: AAG28733.2.
AF286470 mRNA. Translation: AAG28734.2. Different termination.
RefSeqiNP_001263636.1. NM_001276707.1. [P56720-2]
UniGeneiRn.198857.

3D structure databases

ProteinModelPortaliP56720.
SMRiP56720. Positions 313-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249376. 8 interactions.
STRINGi10116.ENSRNOP00000050057.

PTM databases

iPTMnetiP56720.
PhosphoSiteiP56720.

Proteomic databases

PaxDbiP56720.
PRIDEiP56720.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004753; ENSRNOP00000004753; ENSRNOG00000003463. [P56720-1]
ENSRNOT00000047053; ENSRNOP00000050057; ENSRNOG00000003463. [P56720-2]
GeneIDi78968.
KEGGirno:78968.
UCSCiRGD:69423. rat. [P56720-2]

Organism-specific databases

CTDi6720.
RGDi69423. Srebf1.

Phylogenomic databases

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
GeneTreeiENSGT00390000017651.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiP56720.
KOiK07197.
OMAiGKYTGGH.
OrthoDBiEOG7D85VS.
PhylomeDBiP56720.
TreeFamiTF313894.

Enzyme and pathway databases

ReactomeiR-RNO-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-RNO-2426168. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

PROiP56720.

Gene expression databases

ExpressionAtlasiP56720. baseline and differential.
GenevisibleiP56720. RN.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "ADD1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation."
    Tontonoz P., Kim J.B., Graves R.A., Spiegelman B.M.
    Mol. Cell. Biol. 13:4753-4759(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1046 (ISOFORM SREBP-1C).
    Tissue: Adipocyte.
  3. "Identification of a mutation in ADD1/SREBP-1 in the spontaneously hypertensive rat."
    Pravenec M., Jansa P., Kostka V., Zidek V., Kren V., Forejt J., Kurtz T.W.
    Mamm. Genome 12:295-298(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1012 (ISOFORM SREBP-1C), VARIANT MET-779.
    Strain: BN-Lx/Cub and SHR/Ola.
  4. "Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino acid in the basic helix-loop-helix domain."
    Kim J.B., Spotts G.D., Halvorsen Y.D., Shih H.M., Ellenberger T., Towle H.C., Spiegelman B.M.
    Mol. Cell. Biol. 15:2582-2588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRBP1_RAT
AccessioniPrimary (citable) accession number: P56720
Secondary accession number(s): Q99PI6, Q99PI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.