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Entry version 120 (11 Dec 2019)
Sequence version 1 (01 May 2000)
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Protein

Insulin receptor

Gene

insr

Organism
Xenopus laevis (African clawed frog)
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

Receptor tyrosine kinase which mediates actions of insulin. May be required for forelimb regeneration.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Autophosphorylation activates the kinase activity.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>Sitei76Insulin-bindingBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1022ATPPROSITE-ProRule annotation1
Binding sitei1046ATPPROSITE-ProRule annotationBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1148Proton donor/acceptorBy similarity1
Binding sitei1166ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi1093 – 1099ATPPROSITE-ProRule annotation7
Nucleotide bindingi1152 – 1153ATPPROSITE-ProRule annotation2

<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 functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

<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:
Insulin receptor (EC:2.7.10.1)
Short name:
IR
Alternative name(s):
XTK-1b
Xe-InsR
Cleaved into the following 2 chains:
<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:insr
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-920741 insr

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini759 – 951ExtracellularSequence analysisAdd BLAST193
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei952 – 972HelicalSequence analysisAdd BLAST21
Topological domaini973 – 1362CytoplasmicSequence analysisAdd BLAST390

Keywords - Cellular componenti

Cell membrane, Membrane

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 37Sequence analysisAdd BLAST37
<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_000004575138 – 754Insulin receptor subunit alphaCuratedAdd BLAST717
ChainiPRO_0000045752759 – 1362Insulin receptor subunit betaCuratedAdd BLAST604

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi45 ↔ 63By similarity
<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>Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi115N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi148N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi163 ↔ 192By similarity
Disulfide bondi196 ↔ 219By similarity
Disulfide bondi206 ↔ 225By similarity
Disulfide bondi229 ↔ 238By similarity
Disulfide bondi233 ↔ 244By similarity
Disulfide bondi245 ↔ 253By similarity
Disulfide bondi249 ↔ 262By similarity
Disulfide bondi265 ↔ 274By similarity
Disulfide bondi278 ↔ 290By similarity
Disulfide bondi296 ↔ 321By similarity
Disulfide bondi303 ↔ 311By similarity
Disulfide bondi325 ↔ 338By similarity
Glycosylationi332N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi341 ↔ 345By similarity
Disulfide bondi349 ↔ 370By similarity
Glycosylationi374N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi434N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi455N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi472 ↔ 505By similarity
Glycosylationi551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi561InterchainBy similarity
Glycosylationi627N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi642N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi660N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi683 ↔ 896By similarity
Glycosylationi707N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi765N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi779N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi822 ↔ 830By similarity
Glycosylationi917N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi930N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei993Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1174Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1178Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1179Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1335Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1341Phosphotyrosine; by autocatalysisBy 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

Autophosphorylated on tyrosine residues in response to insulin.2 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9PVZ4

<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

Localized mainly to the envelope in oocytes. Localized to the animal hemisphere during early embryonic cleavage. Expressed during organogenesis in regions of ecto- and mesodermic origins. Expressed in the entire encephalon, the otic and optic vesicles, the gills, the somites and the pronephric tubules of the embryo. Also found in adult liver, muscle and regenerated forelimbs.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed both maternally and zygotically. Weakly expressed in embryos through gastrulation and neurulation. Expressed in the tailbud stage and in older tadpoles.2 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_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

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain (By similarity).

By similarity

GO - Molecular functioni

<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_and_domains_section">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>Domaini508 – 629Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST122
Domaini633 – 730Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST98
Domaini849 – 944Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini1012 – 1287Protein kinasePROSITE-ProRule annotationAdd BLAST276

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>Regioni38 – 184Leucine-rich regionBy similarityAdd BLAST147
Regioni741 – 749Insulin-bindingBy similarity9

<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

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K04527

Database of Orthologous Groups

More...
OrthoDBi
223327at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063 FN3, 3 hits
cd00064 FU, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 4 hits
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR040969 Insulin_TMD
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016246 Tyr_kinase_insulin-like_rcpt
IPR002011 Tyr_kinase_rcpt_2_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00757 Furin-like, 1 hit
PF17870 Insulin_TMD, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000620 Insulin_receptor, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 2 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 3 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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_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.

Q9PVZ4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQGVLRGEG HPNNNPNSKV GWKSLVGIIT IFMLILCDQS DGKICYSMDI
60 70 80 90 100
RNNISQFSML EDCTVIEGHL QILLMFTSKP ENFRGLRFPK LTTITDYLLL
110 120 130 140 150
FRVYGLESLK DLFPNLTVIR GTRLFFNYAL VIFEMVHXKE IGLYNLMNIT
160 170 180 190 200
RGSVRIEKNN ELCYLSTIDW SIILDSVEDN YIELNRDNKE ECGDVCPGTV
210 220 230 240 250
KGKSKCKHTL VNGALVERCW TQDHCQKVCP SDCKGSGCLP DGQCCHPECL
260 270 280 290 300
GSCRKPNDPS ECTACRHFQN EGVCVTACPK GSYQFQGWRC IDFNTCQELN
310 320 330 340 350
SRCQNSRDNS CPPYVIHKGE CMPDCPSGYI ANSTTRTCTP CAGPCPKVCT
360 370 380 390 400
IFQNVKTIDS VTSAQELRGC TVINGSLIIN LRGGNNIATE LEANLGLIEE
410 420 430 440 450
ISGYLKIRRS YALVSLSFFR KLRLIRGEVL EAGNYSFYAL DNPSLRQLWD
460 470 480 490 500
WHKHNLTIIH GKLFFHHNPR LCLSQIHQME EVTGTKGRQD KNDIATKTNG
510 520 530 540 550
DQASCEDNLL TFNFIKTSHD MVLLRWDAYW PPDYRDLLGF MVHYKEAPFQ
560 570 580 590 600
NVTEFDGQDA CGSNSWTVVD MDAPERSADG KTQSPGCLLR SLKPWTQYAV
610 620 630 640 650
FVKTLVSGSD EGRTYGAKSK IIYIRTNETI PSVPLDPFSV SNSTSQIILK
660 670 680 690 700
WKPPSEPNGN VTHYLVYWQE QPEDSDLYEV DYCNKGLKLP SRTWTPPTEI
710 720 730 740 750
DENGNENQTE HTSVNKCCPC PKTEFQIQKE QDESAFRKTF ENYLHNEVFI
760 770 780 790 800
PRPVRKRRDL FGVANGTLPD PVTAPPLFNV SSTRAPDEPE PKIYSQKVWF
810 820 830 840 850
KESVLISGLK HFTGYRIEIH ACNHELSMGC SVAAYVNART MPEATADKVV
860 870 880 890 900
GPITYEYVEP NIIHLKWQEP KDPNGLIVLY EVHYSRVGGI EEVITCVSQK
910 920 930 940 950
QYNTDKGGKL RVLTPGNYSV KIRATSLAGN GSWTEQAYFQ VPDHPHSNIV
960 970 980 990 1000
KIITGPIIAV FLLLIVLVYC VVQKKKDAEG PAGPLYTSSN PEYLSASEVY
1010 1020 1030 1040 1050
IPDEWEVPRD KINLLRELGQ GSFGMVYEGI AKDIIKGEPE VRVAVKTVNE
1060 1070 1080 1090 1100
SASLRERIEF LNEASVMKAF NCHHVVRLLG VVSKGQPTLV IMELMAHGDL
1110 1120 1130 1140 1150
KSYLRSLRPD AENNPGRLAP TLKEIIQMAA EISDGMAYLN AKKFVHRDLA
1160 1170 1180 1190 1200
ARNCMVADDY AVKIGDFGMT RDIYETDYYR KGGKGLLPVR WMSPESLKDG
1210 1220 1230 1240 1250
VFTAFSDVWS FGVVLWEITS LAEQPYQGLS NEQVLKFVMD GGSLDHPENC
1260 1270 1280 1290 1300
PPRLHSLMQM CWQYNPKMRP TFLEIIDMLK DDLRPSFQDV SFYYSDENKP
1310 1320 1330 1340 1350
PETDDLEIDF ENMESTPLDP SSCSLRDQSS RTNIYEEHIP YTHMNGGRKN
1360
GRILSLPRSS PS
Length:1,362
Mass (Da):153,757
Last modified:May 1, 2000 - 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:i7B8BF2FB7EFDA01B
GO

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
AJ132556 mRNA Translation: CAB46565.1
M64660 mRNA Translation: AAA50006.1

Protein sequence database of the Protein Information Resource

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PIRi
B41122

NCBI Reference Sequences

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RefSeqi
NP_001081702.1, NM_001088233.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
398006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:398006

<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
AJ132556 mRNA Translation: CAB46565.1
M64660 mRNA Translation: AAA50006.1
PIRiB41122
RefSeqiNP_001081702.1, NM_001088233.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

Proteomic databases

PRIDEiQ9PVZ4

Genome annotation databases

GeneIDi398006
KEGGixla:398006

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
398006
XenbaseiXB-GENE-920741 insr

Phylogenomic databases

KOiK04527
OrthoDBi223327at2759

Family and domain databases

CDDicd00063 FN3, 3 hits
cd00064 FU, 1 hit
Gene3Di2.60.40.10, 4 hits
3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR040969 Insulin_TMD
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016246 Tyr_kinase_insulin-like_rcpt
IPR002011 Tyr_kinase_rcpt_2_CS
PfamiView protein in Pfam
PF00757 Furin-like, 1 hit
PF17870 Insulin_TMD, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PIRSFiPIRSF000620 Insulin_receptor, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF49265 SSF49265, 3 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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 nameiINSR_XENLA
<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: Q9PVZ4
Secondary accession number(s): Q99084
<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: January 10, 2006
Last sequence update: May 1, 2000
Last modified: December 11, 2019
This is version 120 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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