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Entry version 131 (02 Dec 2020)
Sequence version 1 (01 Feb 1997)
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Protein

Helicase-like transcription factor

Gene

HLTF

Organism
Oryctolagus cuniculus (Rabbit)
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

Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity. This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1, to which this protein can bind directly. Mediates repression by c-Rel through a DNA-looping mechanism. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity). Transcriptional regulator that mediates the ability of prolactin to augment progesterone-dependent transcription of the SCGB1A1/uteroglobin gene through a bipartite progesterone receptor half-site/overlapping Y-box combination (-38/-26) where progesterone activation is attenuated by nuclear factor Y binding. Regulation also involves two GC-rich sequences in the proximal promoter (positions -162/+90) and a RUSH/SMARCA3 site (positions -616/-611) in the 5'-untranslated region.By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi38 – 287By similarityAdd BLAST250
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi294 – 301ATPPROSITE-ProRule annotation8
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 fingeri757 – 798RING-typePROSITE-ProRule annotationAdd BLAST42

<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, Chromatin regulator, DNA-binding, Helicase, Hydrolase, Multifunctional enzyme, Transferase
Biological processTranscription, Ubl conjugation pathway
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<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%5Fand%5Ftaxonomy%5Fsection">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:
Helicase-like transcription factor (EC:2.3.2.27, EC:3.6.4.-)
Alternative name(s):
RING-type E3 ubiquitin transferase HLTFCurated
RUSH-1
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3
Sucrose nonfermenting protein 2-like 3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HLTF
Synonyms:RUSH1, SMARCA3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi767P → S or T: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1
Mutagenesisi768V → R: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1
Mutagenesisi769I → M or P: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1
Mutagenesisi771H → D or K: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1
Mutagenesisi792A → Q: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1
Mutagenesisi793K → P: Abolishes binding to the RFBP isoform of ATP11B. 1 Publication1

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000561861 – 1005Helicase-like transcription factorAdd BLAST1005

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 residuei27Omega-N-methylarginineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei195Phosphotyrosine; by JAK21 Publication1
Cross-linki211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei395PhosphoserineBy similarity1
Modified residuei396PhosphoserineBy similarity1
Modified residuei398PhosphoserineBy similarity1
Modified residuei733PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 serine, threonine, and tyrosine residues. Tyr-195 phosphorylation is catalyzed by JAK2 in response to prolactin treatment. It is required for DNA binding.3 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q95216

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q95216

<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

Isoform 1 is expressed preferentially in bladder, cervix, diaphragm, duodenum, epididymis, heart, kidney, liver, lung, ovary (granulosa cells), prostate, spleen, testis (predominantly in the Sertoli cells of the seminiferous tubules) and vagina. Isoform 2 is expressed preferentially in lactating mammary gland and uterine endometrium.4 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Isoform RUSH 1-alpha expression is increased by progesterone and decreased by estradiol. Progesterone induction is increased in the presence of prolactin. Isoform RUSH 1-beta/RFBP expression is increased by estrogen and decreased by progesterone.3 Publications

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with SP1 and SP3 independently of DNA; the interaction with these transcriptional factors may be required for basal transcription of target genes (By similarity).

Interacts (via the RING-finger) with isoform RFBP of ATP11B. Progesterone-dependent isoform 1 interacts with EGR1; the interaction requires prior binding to DNA and represses c-Rel via a DNA looping mechanism.

Interacts with GATA4.

Interacts with PCNA; the interaction promotes polyubiquitination of PCNA through association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes.

Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000003055

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini427 – 603Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST177
Domaini834 – 999Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166

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>Regioni767 – 772Required for interaction with the RFBP isoform of ATP11B6
Regioni791 – 796Required for interaction with the RFBP isoform of ATP11B6
Regioni922 – 1005Interaction with SP1 and SP3By similarityAdd BLAST84

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>Motifi554 – 557DEGH box4

<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 fingeri757 – 798RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1001, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q95216

Database of Orthologous Groups

More...
OrthoDBi
132523at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit
3.40.50.10810, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014905, HIRAN
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00271, Helicase_C, 1 hit
PF08797, HIRAN, 1 hit
PF00176, SNF2_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SM00910, HIRAN, 1 hit
SM00184, RING, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

<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%5Flength">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>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q95216-1) [UniParc]FASTAAdd to basket
Also known as: RUSH 1-alpha

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MSWMFKRDPV WKYLQTVQYG VHGNFSRLSY PTFFPRFEFQ DIIPPDDFLT
60 70 80 90 100
SDEELDSVLF GTLRGHVVGL RYYTGVVNNN EMVALQREPN NPYDKNAIKV
110 120 130 140 150
NNVNGNQVGY LKKELAAALA YIMDNKLAQI EGVVPYGANN AFTMPLQMTF
160 170 180 190 200
WGKEENRKAV LDQLKKHGFK LGPAPKTLGF SLESGWGSGR AGPSYSMPVH
210 220 230 240 250
AAIQMTTEQL KTEFDKLFED LKEDDKTQEM EPAEAVETPL LPHQKQALAW
260 270 280 290 300
MVSRENSREL PPFWELRNDL YYNTITNFSE KDQPENVHGG ILADDMGLGK
310 320 330 340 350
TLTAIAVILT NFHDGKPLPV ERMKKNQVKK ECNSSESDKP GRKDTIKKTD
360 370 380 390 400
GLSKEGSRYS EEPSISDVKK NKYSMSELSS SQPKRKKIAV QYIESSDSEE
410 420 430 440 450
IEISELPQKM KGKLKNVQSE TKRVKVGPSK IKEDTAFACA LTSSASTTTK
460 470 480 490 500
KILKKGASAQ RVQRKLMFEE RPRTTLIICP LSVLSNWIDQ FGQHIKSDVH
510 520 530 540 550
LNFYVYYGPD RIRDPALLSK QDIVLTTYNI LTHDYGTKGD SPLHSIRWLR
560 570 580 590 600
VILDEGHAIR NPNAQQTKAV LDLEAERRWV LTGTPIQNSL KDLWSLLSFL
610 620 630 640 650
KLKPFVDREW WHRTIQRPVT MGDEGGLRRL QSLIKNITLR RTKTSKIKGK
660 670 680 690 700
PVLELPERPV FIQHITLSDE ERKIYQSVKS EGKATIGRYF NEGTVLAHYA
710 720 730 740 750
DVLGLLLRLR QICCHTHLLT NTVSSSGPSG NDTPEELRKK LIKKMKLILS
760 770 780 790 800
SGSDEECAIC LDSLTVPVIT HCAHVFCKPC ICQCIQNEQP HAKCPLCRND
810 820 830 840 850
IHGDNLLECP PEELACDSEK KSNMEWTSSS KINALMHALI DLRTKNPNIK
860 870 880 890 900
SLVVSQFTTF LSLIETPLKA SGFVFTRLDG SMAQKKRVES IQCFQNTEAG
910 920 930 940 950
SPTIMLLSLK AGGVGLNLCA ASRVFLMDPA WNPAAEDQRF DRCHRLGQKQ
960 970 980 990 1000
EVIITKFIVK DSVEENMLKI QNTKRELAAG AFGTKKNANE MKQAKINEIR

TLIDL
Note: Major isoform in progesterone-dominant endometrium.
Length:1,005
Mass (Da):113,582
Last modified:February 1, 1997 - v1
<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:iC741E7117D6BD807
GO
Isoform 2 (identifier: Q95216-2) [UniParc]FASTAAdd to basket
Also known as: RUSH 1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     832-836: INALM → RFLSC
     837-1005: Missing.

Note: Truncated, estrogen-dependent isoform.Curated
Show »
Length:836
Mass (Da):94,842
Checksum:iB0ED6969548035DD
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012923832 – 836INALM → RFLSC in isoform 2. 1 Publication5
Alternative sequenceiVSP_012924837 – 1005Missing in isoform 2. 1 PublicationAdd BLAST169

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U66564 mRNA Translation: AAC18656.1
U66565 mRNA Translation: AAC48693.1

NCBI Reference Sequences

More...
RefSeqi
NP_001075845.1, NM_001082376.1 [Q95216-2]
NP_001108200.1, NM_001114728.1 [Q95216-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009232

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009232

Keywords - Coding sequence diversityi

Alternative splicing

<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
U66564 mRNA Translation: AAC18656.1
U66565 mRNA Translation: AAC48693.1
RefSeqiNP_001075845.1, NM_001082376.1 [Q95216-2]
NP_001108200.1, NM_001114728.1 [Q95216-1]

3D structure databases

Database of comparative protein structure models

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ModBasei
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SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
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Protein-protein interaction databases

STRINGi9986.ENSOCUP00000003055

PTM databases

iPTMnetiQ95216

Proteomic databases

PRIDEiQ95216

Genome annotation databases

GeneIDi100009232
KEGGiocu:100009232

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6596

Phylogenomic databases

eggNOGiKOG1001, Eukaryota
InParanoidiQ95216
OrthoDBi132523at2759

Enzyme and pathway databases

UniPathwayiUPA00143

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.40.50.10810, 2 hits
InterProiView protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014905, HIRAN
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PfamiView protein in Pfam
PF00271, Helicase_C, 1 hit
PF08797, HIRAN, 1 hit
PF00176, SNF2_N, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SM00910, HIRAN, 1 hit
SM00184, RING, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiHLTF_RABIT
<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: Q95216
Secondary accession number(s): Q95217
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: February 1, 1997
Last modified: December 2, 2020
This is version 131 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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