Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 167 (11 Dec 2019)
Sequence version 2 (21 Jun 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Transcription factor Sp1

Gene

Sp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. Positively regulates the transcription of the core clock component ARNTL/BMAL1 (By similarity). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter (PubMed:19081374). Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-RNO-6807505 RNA polymerase II transcribes snRNA genes

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transcription factor Sp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Sp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Rat genome database

More...
RGDi
3738 Sp1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000471392 – 786Transcription factor Sp1Add BLAST785

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineCombined sources1
Modified residuei7PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei60PhosphoserineBy similarity1
Modified residuei102Phosphoserine; by ATMBy similarity1
Modified residuei279Phosphothreonine; by MAPK8By similarity1
Modified residuei454Phosphothreonine; by MAPK1 and MAPK3By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi492O-linked (GlcNAc) serineBy similarity1
Modified residuei613Phosphoserine; alternateBy similarity1
Glycosylationi613O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei641Phosphothreonine; alternateBy similarity1
Glycosylationi641O-linked (GlcNAc) threonine; alternateBy similarity1
Modified residuei642Phosphoserine; by PKC/PRKCZ; alternateBy similarity1
Glycosylationi642O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei652Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei669PhosphothreonineBy similarity1
Modified residuei671Phosphoserine; by PKC/PRKCZBy similarity1
Modified residuei682Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei699Phosphoserine; alternateBy similarity1
Glycosylationi699O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei703Phosphoserine; alternateBy similarity1
Glycosylationi703O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei704N6-acetyllysineBy similarity1
Modified residuei740Phosphothreonine; by MAPK1, MAPK3 and MAPK8By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-60 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-102 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-454 and Thr-740 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-279 and Thr-740 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-60 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-60 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues (By similarity).By similarity
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity).By similarity
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity).By similarity
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity).By similarity
O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei64 – 65CleavageBy similarity2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q01714

PRoteomics IDEntifications database

More...
PRIDEi
Q01714

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01714

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q01714

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in all tissues tested, including lung, kidney, spleen and thymus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000014084 Expressed in 10 organ(s), highest expression level in spleen

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01714 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2.

Interacts with SV40 VP2/3 proteins.

Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding.

Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF.

Interacts (deacetylated form) with EP300; the interaction enhances gene expression.

Interacts with HDAC1 and JUN.

Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1 (By similarity).

Interacts with SMARCA4/BRG1 (PubMed:19081374).

Interacts with ATF7IP and TBP.

Interacts with MEIS2 and PBX1.

Interacts with EGR1.

Interacts with RNF112 in an oxidative stress-regulated manner (By similarity).

Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P185762EBI-862787,EBI-862695

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246914, 7 interactors

Protein interaction database and analysis system

More...
IntActi
Q01714, 1 interactor

Molecular INTeraction database

More...
MINTi
Q01714

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000019403

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q01714

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 83Repressor domainBy similarityAdd BLAST82
Regioni147 – 252Transactivation domain A (Gln-rich)By similarityAdd BLAST106
Regioni262 – 496Transactivation domain B (Gln-rich)By similarityAdd BLAST235
Regioni497 – 611Transactivation domain C (highly charged)By similarityAdd BLAST115
Regioni620 – 786VZV IE62-bindingBy similarityAdd BLAST167
Regioni709 – 786Domain DBy similarityAdd BLAST78

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi463 – 4719aaTADBy similarity9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi36 – 144Ser/Thr-richAdd BLAST109
Compositional biasi36 – 138Ser-richAdd BLAST103
Compositional biasi157 – 214Gln-richAdd BLAST58
Compositional biasi272 – 380Ser/Thr-richAdd BLAST109
Compositional biasi272 – 352Ser-richAdd BLAST81
Compositional biasi353 – 481Gln-richAdd BLAST129

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1721 Eukaryota
COG5048 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157804

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234295

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01714

KEGG Orthology (KO)

More...
KOi
K04684

Identification of Orthologs from Complete Genome Data

More...
OMAi
MGIMNFS

Database of Orthologous Groups

More...
OrthoDBi
1085860at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q01714

TreeFam database of animal gene trees

More...
TreeFami
TF350150

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00096 zf-C2H2, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00355 ZnF_C2H2, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57667 SSF57667, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q01714-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDQDHSMDE VTAVKIEKGV GGNNGGSGNG GGAAFSQTRS SSTGSSSSSG
60 70 80 90 100
GGGGQESQPS PLALLAATCS RIESPNENSN NSQGPSQSGG TGELDLTATQ
110 120 130 140 150
LSQGANGWQI ISSSSGATPT SKEQSGNSTN GSNGSESSKN RTVSGGQYVV
160 170 180 190 200
AATPNLQNQQ VLTGLPGVMP NIQYQVIPQF QTVDGQQLQF AATGAQVQQD
210 220 230 240 250
GSGQIQIIPG ANQQIITNRG SGGNIIAAMP NLLQQAVPLQ GLANNVLSGQ
260 270 280 290 300
TQYVTNVPVA LNGNITLLPV NSVSAATLTP SSQAGTISSS GSQESGSQPV
310 320 330 340 350
TSGTAISSAS LVSSQASSSS FFTNANSYST TTTTSNMGIM NFTSSGSSGT
360 370 380 390 400
SSQGQTSQRV GGLQGSDSLN IQQNQTSGGS LQGSQQKEGE QSQQTQQQQI
410 420 430 440 450
LIQPQLVQGG QALQALQAAP LSGQTFTTQA ISQETLQNLQ LQAVQNSGPI
460 470 480 490 500
IIRTPTVGPN GQVSWQTLQL QNLQVQNPQA QTITLAPMQG VSLGQTSSSN
510 520 530 540 550
TTLTPIASAA SIPAGTVTVN AAQLSSMPGL QTINLSALGT SGIQVHQLPG
560 570 580 590 600
LPLAIANTPG DHGAQLGLHG PGGDGIHDET AGGEEGENSP DPQPQAGRRT
610 620 630 640 650
RREACTCPYC KDSEGRGSGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW
660 670 680 690 700
HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD
710 720 730 740 750
HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGSGTAT PSALITTNMV
760 770 780
AMEAICPEGI ARLANSGINV MQVTELQSIN ISGNGF
Length:786
Mass (Da):80,772
Last modified:June 21, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3DE2AD93F95E7C0B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti78N → NEN in BAA02235 (PubMed:1356762).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D12768 mRNA Translation: BAA02235.1
AB077988 Genomic DNA Translation: BAC05486.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JS0747

NCBI Reference Sequences

More...
RefSeqi
NP_036787.2, NM_012655.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000019403; ENSRNOP00000019403; ENSRNOG00000014084

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24790

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24790

UCSC genome browser

More...
UCSCi
RGD:3738 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12768 mRNA Translation: BAA02235.1
AB077988 Genomic DNA Translation: BAC05486.1
PIRiJS0747
RefSeqiNP_036787.2, NM_012655.2

3D structure databases

SMRiQ01714
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246914, 7 interactors
IntActiQ01714, 1 interactor
MINTiQ01714
STRINGi10116.ENSRNOP00000019403

PTM databases

iPTMnetiQ01714
PhosphoSitePlusiQ01714

Proteomic databases

PaxDbiQ01714
PRIDEiQ01714

Genome annotation databases

EnsembliENSRNOT00000019403; ENSRNOP00000019403; ENSRNOG00000014084
GeneIDi24790
KEGGirno:24790
UCSCiRGD:3738 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6667
RGDi3738 Sp1

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00940000157804
HOGENOMiHOG000234295
InParanoidiQ01714
KOiK04684
OMAiMGIMNFS
OrthoDBi1085860at2759
PhylomeDBiQ01714
TreeFamiTF350150

Enzyme and pathway databases

ReactomeiR-RNO-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-RNO-6807505 RNA polymerase II transcribes snRNA genes

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q01714

Gene expression databases

BgeeiENSRNOG00000014084 Expressed in 10 organ(s), highest expression level in spleen
GenevisibleiQ01714 RN

Family and domain databases

InterProiView protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSP1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01714
Secondary accession number(s): Q8K4R0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 21, 2005
Last modified: December 11, 2019
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again