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Protein

Receptor-type tyrosine-protein phosphatase S

Gene

Ptprs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547). Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth (PubMed:21454754). Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection (PubMed:15797710, PubMed:19833921, PubMed:19780196, PubMed:21454754, PubMed:22519304, PubMed:22406547). Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2 (PubMed:21454754). Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb (PubMed:10080191). Functions as tyrosine phosphatase (PubMed:7529177). Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases (PubMed:15797710). Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta (PubMed:26231120).By similarity8 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1516SubstrateBy similarity1
Active sitei1548Phosphocysteine intermediateBy similarity1
Binding sitei1592SubstrateBy similarity1
Active sitei1839Phosphocysteine intermediateBy similarity1

GO - Molecular functioni

  • chondroitin sulfate binding Source: UniProtKB
  • heparan sulfate proteoglycan binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • phosphoprotein phosphatase activity Source: MGI
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cerebellum development Source: MGI
  • cerebral cortex development Source: MGI
  • corpus callosum development Source: MGI
  • establishment of endothelial intestinal barrier Source: MGI
  • hippocampus development Source: MGI
  • negative regulation of axon extension Source: UniProtKB
  • negative regulation of axon regeneration Source: UniProtKB
  • negative regulation of collateral sprouting Source: UniProtKB
  • negative regulation of dendritic spine development Source: UniProtKB
  • negative regulation of interferon-alpha production Source: MGI
  • negative regulation of interferon-beta production Source: MGI
  • negative regulation of neuron projection development Source: UniProtKB
  • negative regulation of toll-like receptor 9 signaling pathway Source: MGI
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • protein dephosphorylation Source: MGI
  • spinal cord development Source: MGI

Keywordsi

Molecular functionHeparin-binding, Hydrolase, Protein phosphatase, Receptor
Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-388844. Receptor protein tyrosine phosphatases interactions.
R-MMU-8849932. SALM protein interactions at the synapses.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase S (EC:3.1.3.481 Publication1 Publication)
Short name:
R-PTP-S
Alternative name(s):
PTPNU-3
Receptor-type tyrosine-protein phosphatase sigma
Short name:
R-PTP-sigma
Gene namesi
Name:Ptprs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:97815. Ptprs.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 1257ExtracellularSequence analysisAdd BLAST1228
Transmembranei1258 – 1278HelicalSequence analysisAdd BLAST21
Topological domaini1279 – 1907CytoplasmicSequence analysisAdd BLAST629

GO - Cellular componenti

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Mating heterozygous mice gives rise to Ptprs deficient mice at the expected Mendelian rate, but the pups are somewhat lighter than their littermates at birth and display strongly impaired weight gain (PubMed:10080191). After about three weeks, mutant mice weigh only 50 to 55% of normal littermates, possibly due to reduced Igf1 levels in blood serum (PubMed:10080191). Pups born after crossing Ptprs deficient mice display about 41% lethality during the first day after birth (PubMed:10080191). Adult mutants have a reduced overall brain size, with a dramatic decrease in the size of the olfactory bulb (PubMed:10080191). As a consequence, mutant mice have strongly impaired ability to perceive repellent smells (PubMed:10080191). Females are less often in estrus (PubMed:10080191). Besides, mutant mice display a decreased overall size of the pituitary glands; relative to the total size, the intermediary lobe is enlarged with a concomitant decrease in the size of the anterior and posterior lobes (PubMed:10080191). Likewise, the size of the hypothalamus is decreased (PubMed:10080191). No visible effect on the structure of the retina and the optic nerve (PubMed:15797710). Mutant mice show increased axon outgrowth from retinal ganglion cells after optic nerve transection (PubMed:15797710). Mutant mice display increased axon outgrowth after spinal cord injury (PubMed:19833921, PubMed:19780196). In aging mice, mossy fibers in the CA3C region of the hippocampus show increased sprouting (PubMed:22519304). No difference in mossy fiber sprouting is seen in the CA3A region of the hippocampus (PubMed:22519304). After kainate-induced seizures, mutant mice show increased mossy fiber sprouting in both the CA3C and the CA3A region of the hippocampus (PubMed:22519304). Mutant mice display a slight increase in dendrite length and dendrite spine density in pyramidal cells in the CA1 region of the hippocampus, and subtle changes in miniature AMPAR-mediated excitatory post-synaptic currents (PubMed:22519304). Dorsal root ganglion neurons from mutant mice show decreased stimulation of neurite outgrowth in response to the heparan sulfate proteoglycan GPC2 (PubMed:21454754). Cerebellar granule neurons and dorsal root ganglion neurons from mutant mice show decreased inhibition of neurite outgrowth in response to chondroitin sulfate proteoglycan (PubMed:19833921, PubMed:19780196, PubMed:21454754, PubMed:22406547). Sensory neurons show increased axon outgrowth after spinal cord crush injury (PubMed:19833921). After optic nerve crush injury, mutant mice show no increase in axon regeneration (PubMed:22406547). Combined disruption of Rtn4r, Rtn4rl1 and Ptprs increases axon regeneration after injury (PubMed:22406547).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68 – 72KKGKK → AAGAA: Abolishes binding to chondroitin sulfate proteoglycans. Abolishes receptor oligomerization via binding to large heparan sulfate proteoglycan structures. 2 Publications5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000035832130 – 1907Receptor-type tyrosine-protein phosphatase SAdd BLAST1878

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 107PROSITE-ProRule annotation
Disulfide bondi156 ↔ 207PROSITE-ProRule annotation
Glycosylationi250N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi253 ↔ 298PROSITE-ProRule annotation
Glycosylationi295N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi720N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi916N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1197 – 1198CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiB0V2N1.
PaxDbiB0V2N1.
PeptideAtlasiB0V2N1.
PRIDEiB0V2N1.

PTM databases

iPTMnetiB0V2N1.
PhosphoSitePlusiB0V2N1.

Expressioni

Tissue specificityi

Detected in brain cortex, cerebellum and thoracic spinal cord (at protein level) (PubMed:19780196, PubMed:22519304). Detected in motor cortex and white matter of the spinal cord, but not in spinal cord gray matter (PubMed:19780196). Isoform 1 and isoform 6 are predominantly expressed in the brain (cerebrum and cerebellum) and to a lesser extent in the heart and skeletal muscle. Also found in neuronal-derived cell lines (PubMed:7529177). Detected in the ganglion cell layer of the retina and in glial cells along the optic nerve (PubMed:15797710). Detected in bone marrow and spleen plasmacytoid dendritic cells (PubMed:26231120).5 Publications

Developmental stagei

Expression is seen in embryos between 8 dpc and 16 dpc and a peak expression is seen at 14 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000013236.
GenevisibleiB0V2N1. MM.

Interactioni

Subunit structurei

Binding to large heparan sulfate proteoglycan structures promotes oligomerization (PubMed:21454754). Binding to chondroitin sulfate proteoglycan does not lead to oligomerization (PubMed:21454754). Interacts (via Ig-like domains) with NTRK3 (PubMed:25385546). Interacts (via Ig-like domains) with NTRK1, but does not form detectable complexes with NTRK2 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

IntActiB0V2N1. 3 interactors.
MINTiMINT-129725.
STRINGi10090.ENSMUSP00000064048.

Structurei

Secondary structure

11907
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1337 – 1358Combined sources22
Helixi1368 – 1371Combined sources4
Turni1373 – 1375Combined sources3
Helixi1376 – 1378Combined sources3
Helixi1388 – 1390Combined sources3
Beta strandi1391 – 1393Combined sources3
Turni1401 – 1404Combined sources4
Beta strandi1405 – 1413Combined sources9
Beta strandi1416 – 1423Combined sources8
Helixi1428 – 1430Combined sources3
Helixi1431 – 1440Combined sources10
Beta strandi1445 – 1448Combined sources4
Beta strandi1452 – 1454Combined sources3
Beta strandi1457 – 1459Combined sources3
Beta strandi1466 – 1472Combined sources7
Beta strandi1475 – 1484Combined sources10
Beta strandi1486 – 1499Combined sources14
Beta strandi1503 – 1511Combined sources9
Beta strandi1516 – 1518Combined sources3
Helixi1524 – 1535Combined sources12
Beta strandi1544 – 1553Combined sources10
Helixi1554 – 1568Combined sources15
Beta strandi1571 – 1574Combined sources4
Helixi1576 – 1584Combined sources9
Helixi1594 – 1609Combined sources16
Helixi1617 – 1619Combined sources3
Helixi1620 – 1627Combined sources8
Helixi1638 – 1644Combined sources7
Turni1657 – 1659Combined sources3
Turni1665 – 1667Combined sources3
Beta strandi1671 – 1673Combined sources3
Turni1677 – 1679Combined sources3
Beta strandi1696 – 1700Combined sources5
Beta strandi1703 – 1705Combined sources3
Beta strandi1709 – 1712Combined sources4
Turni1717 – 1719Combined sources3
Helixi1720 – 1729Combined sources10
Beta strandi1734 – 1737Combined sources4
Beta strandi1744 – 1747Combined sources4
Beta strandi1755 – 1757Combined sources3
Beta strandi1759 – 1761Combined sources3
Beta strandi1764 – 1773Combined sources10
Beta strandi1775 – 1786Combined sources12
Turni1787 – 1789Combined sources3
Beta strandi1792 – 1800Combined sources9
Beta strandi1805 – 1807Combined sources3
Helixi1813 – 1828Combined sources16
Beta strandi1835 – 1843Combined sources9
Helixi1844 – 1861Combined sources18
Helixi1867 – 1875Combined sources9
Helixi1885 – 1900Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SR9X-ray2.40A1326-1901[»]
ProteinModelPortaliB0V2N1.
SMRiB0V2N1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 123Ig-like C2-type 1Add BLAST91
Domaini135 – 224Ig-like C2-type 2Add BLAST90
Domaini232 – 314Ig-like C2-type 3Add BLAST83
Domaini321 – 411Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST91
Domaini416 – 510Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini514 – 603Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST90
Domaini608 – 705Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST98
Domaini710 – 809Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST100
Domaini810 – 906Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST97
Domaini907 – 1008Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST102
Domaini1011 – 1095Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST85
Domaini1352 – 1607Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd BLAST256
Domaini1639 – 1898Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd BLAST260

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 72Important for binding to glycosaminoglycan chains2 Publications5
Regioni1548 – 1554Substrate bindingBy similarity7

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG053758.
InParanoidiB0V2N1.
KOiK06778.
OMAiVPGQPMN.
OrthoDBiEOG091G11WG.
PhylomeDBiB0V2N1.
TreeFamiTF312900.

Family and domain databases

CDDicd00063. FN3. 7 hits.
Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 2 hits.
InterProiView protein in InterPro
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
PfamiView protein in Pfam
PF00041. fn3. 6 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiView protein in SMART
SM00060. FN3. 8 hits.
SM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
SM00404. PTPc_motif. 2 hits.
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 2 hits.
PROSITEiView protein in PROSITE
PS50853. FN3. 8 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.

Sequences (6)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: B0V2N1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPTWSPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA
60 70 80 90 100
SFVCQATGDP KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR
110 120 130 140 150
DENVYECVAQ NSVGEITIHA KLTVLREDQL PPGFPNIDMG PQLKVVERTR
160 170 180 190 200
TATMLCAASG NPDPEITWFK DFLPVDPSAS NGRIKQLRSG ALQIESSEET
210 220 230 240 250
DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS HEIMPGGNVN
260 270 280 290 300
ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
310 320 330 340 350
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY
360 370 380 390 400
VIEYKSKSQD GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP
410 420 430 440 450
SESVVTRTGE QAPASAPRNV QARMLSATTM IVQWEEPVEP NGLIRGYRVY
460 470 480 490 500
YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE DETYTVRVLA FTSVGDGPLS
510 520 530 540 550
DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV IKYELLFREG
560 570 580 590 600
DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
610 620 630 640 650
LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS
660 670 680 690 700
EDPDPKEVNN IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV
710 720 730 740 750
RTDEDVPSAP PRKVEAEALN ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM
760 770 780 790 800
EGAEARGPPR IKDIMLADAQ EMVITNLQPE TAYSITVAAY TMKGDGARSK
810 820 830 840 850
PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP VLGYRLQFGR
860 870 880 890 900
EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEAAAALSIP
910 920 930 940 950
EDAPRGFPQI LGAAGNVSAG SVLLRWLPPV PAERNGAIIK YTVSVREAGA
960 970 980 990 1000
PGPATETELA AAAQPGAETA LTLRGLRPET AYELRVRAHT RRGPGPFSPP
1010 1020 1030 1040 1050
LRYRLARDPV SPKNFKVKMI MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL
1060 1070 1080 1090 1100
DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS LGGLQQTVTA RTAFNMLSGK
1110 1120 1130 1140 1150
PSVAPKPDND GFIVVYLPDG QSPVTVQNYF IVMVPLRKSR GGQFPVLLGS
1160 1170 1180 1190 1200
PEDMDLEELI QDISRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
1210 1220 1230 1240 1250
KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP
1260 1270 1280 1290 1300
IVDGEEGLIW VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL
1310 1320 1330 1340 1350
NNADLAPHHP KDPVEMRRIN FQTPGMLSHP PIPITDMAEH MERLKANDSL
1360 1370 1380 1390 1400
KLSQEYESID PGQQFTWEHS NLEANKPKNR YANVIAYDHS RVILQPLEGI
1410 1420 1430 1440 1450
MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE QRSATVVMMT
1460 1470 1480 1490 1500
RLEEKSRIKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
1510 1520 1530 1540 1550
SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPIVVHCSA
1560 1570 1580 1590 1600
GVGRTGCFIV IDAMLERIKT EKTVDVYGHV TLMRSQRNYM VQTEDQYGFI
1610 1620 1630 1640 1650
HEALLEAVGC GNTEVPARSL YTYIQKLAQV EPGEHVTGME LEFKRLASSK
1660 1670 1680 1690 1700
AHTSRFITAS LPCNKFKNRL VNILPYESSR VCLQPIRGVE GSDYINASFI
1710 1720 1730 1740 1750
DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK LREMGREKCH
1760 1770 1780 1790 1800
QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
1810 1820 1830 1840 1850
TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI
1860 1870 1880 1890 1900
TLSIVLERMR YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG

SFDHYAT
Length:1,907
Mass (Da):211,904
Last modified:April 8, 2008 - v1
Checksum:i725C016196E22D1A
GO
Isoform 2 (identifier: B0V2N1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1519-1521: Missing.

Show »
Length:1,904
Mass (Da):211,579
Checksum:i276B40675B8B37FC
GO
Isoform 3 (identifier: B0V2N1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     604-604: K → I
     605-1010: Missing.

Show »
Length:1,501
Mass (Da):168,298
Checksum:i4443E1DDFE83BF41
GO
Isoform 4 (identifier: B0V2N1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     604-604: K → I
     605-1010: Missing.
     1284-1287: Missing.

Show »
Length:1,497
Mass (Da):167,871
Checksum:i07C97C891E1BE761
GO
Isoform 5 (identifier: B0V2N1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1315: Missing.

Show »
Length:592
Mass (Da):68,104
Checksum:iE24908FB00CE3F16
GO
Isoform 6 (identifier: B0V2N1-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     624-669: Missing.

Show »
Length:1,861
Mass (Da):206,825
Checksum:i64C415721228AF18
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti597R → H in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti758P → A in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti834A → G in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti853A → R in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti887A → G in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti981A → G in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti1169 – 1171RSL → QHV in CAA57732 (PubMed:7529177).Curated3
Sequence conflicti1502E → G in CAA57732 (PubMed:7529177).Curated1
Sequence conflicti1609G → S in CAA57732 (PubMed:7529177).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0360571 – 1315Missing in isoform 5. 1 PublicationAdd BLAST1315
Alternative sequenceiVSP_036058604K → I in isoform 3 and isoform 4. 1 Publication1
Alternative sequenceiVSP_036059605 – 1010Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST406
Alternative sequenceiVSP_036060624 – 669Missing in isoform 6. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_0360611284 – 1287Missing in isoform 4. 1 Publication4
Alternative sequenceiVSP_0360621519 – 1521Missing in isoform 2. 1 Publication3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82288 mRNA. Translation: CAA57732.1.
D28530 mRNA. Translation: BAA05886.1.
AK159320 mRNA. Translation: BAE34987.1.
AK169714 mRNA. Translation: BAE41325.1.
CT009637 Genomic DNA. Translation: CAQ12196.1.
CT009637 Genomic DNA. Translation: CAQ12197.1.
BC052462 mRNA. Translation: AAH52462.1.
BC083188 mRNA. Translation: AAH83188.1.
CCDSiCCDS37664.1. [B0V2N1-1]
CCDS57103.1. [B0V2N1-3]
RefSeqiNP_001239382.1. NM_001252453.1. [B0V2N1-3]
NP_001239384.1. NM_001252455.1. [B0V2N1-4]
NP_001239385.1. NM_001252456.1. [B0V2N1-3]
NP_035348.2. NM_011218.2. [B0V2N1-1]
UniGeneiMm.258771.

Genome annotation databases

EnsembliENSMUST00000067538; ENSMUSP00000064048; ENSMUSG00000013236. [B0V2N1-1]
ENSMUST00000086828; ENSMUSP00000084038; ENSMUSG00000013236. [B0V2N1-3]
GeneIDi19280.
KEGGimmu:19280.
UCSCiuc008dbx.3. mouse. [B0V2N1-3]
uc008dby.2. mouse. [B0V2N1-1]
uc008dca.2. mouse. [B0V2N1-4]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPTPRS_MOUSE
AccessioniPrimary (citable) accession number: B0V2N1
Secondary accession number(s): Q3TEC3
, Q3TXC9, Q4JFC7, Q5XJV4, Q64503, Q64699, Q7TT17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 8, 2008
Last modified: June 7, 2017
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families