Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

11 structures for Q64487

Entry ID Method Resolution Chain Position Source
4Y61 X-ray 336 A A 21-411 PDB
4YFD X-ray 325 A A 21-511 PDB
4YFE X-ray 197 A A/B 321-511 PDB
4YFG X-ray 349 A A/B 21-511 PDB
4YH7 X-ray 440 A A 21-1265 PDB
5XWT X-ray 418 A A/C 20-410 PDB
5XWU X-ray 316 A A/C 20-321 PDB
5Y32 X-ray 270 A A 21-318 PDB
6KIP X-ray 191 A A 1617-1912 PDB
7CEG X-ray 385 A A 21-411 PDB
AF-Q64487-F1 Predicted AlphaFoldDB

54 variants for Q64487

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388692241 61 G>R No EVA
rs3388690010 92 D>E No EVA
rs3388692829 97 E>D No EVA
rs3388694922 104 V>M No EVA
rs3388689556 204 K>Q No EVA
rs3394543881 207 C>* No EVA
rs3394422882 225 V>G No EVA
rs3388686544 295 R>G No EVA
rs3388689594 335 T>S No EVA
rs249358769 362 N>H No EVA
rs3388686179 362 N>I No EVA
rs231539230 364 E>D No EVA
rs3388690533 375 T>I No EVA
rs3411548040 376 T>I No EVA
rs3388695857 380 V>D No EVA
rs3388693449 388 D>E No EVA
rs3388678501 419 S>N No EVA
rs3388689551 465 N>S No EVA
rs3388690489 490 V>A No EVA
rs3388683794 502 P>T No EVA
rs3388693430 508 Q>L No EVA
rs1132035915 509 V>G No EVA
rs1135202568 510 I>N No EVA
rs1132767154 514 G>V No EVA
rs3388694982 539 P>R No EVA
rs3388686616 653 D>G No EVA
rs28020782 657 F>Y No EVA
rs3388670136 669 T>I No EVA
rs3388692851 834 T>I No EVA
rs3388689517 901 V>SDG* No EVA
rs3411094232 903 F>Y No EVA
rs3388693434 952 T>S No EVA
rs3388695846 964 P>L No EVA
rs3388670146 1023 N>K No EVA
rs3388689548 1030 M>T No EVA
rs219716833 1039 E>D No EVA
rs3388687715 1106 D>G No EVA
rs3388693422 1277 V>E No EVA
rs3388693460 1383 K>M No EVA
rs3388695789 1385 R>T No EVA
rs3388678423 1403 E>* No EVA
rs3388686570 1476 T>S No EVA
rs3388689896 1524 V>I No EVA
rs28052825 1543 P>S No EVA
rs3388692242 1580 D>S No EVA
rs3388695817 1582 Y>F No EVA
rs242157531 1590 A>V No EVA
rs3388686237 1598 T>A No EVA
rs3388691965 1625 L>V No EVA
rs3388670135 1646 L>I No EVA
rs3388691913 1747 R>* No EVA
rs3388692291 1821 I>N No EVA
rs3388686173 1847 G>S No EVA
rs3388686618 1867 E>D No EVA

No associated diseases with Q64487

29 regional properties for Q64487

Type Name Position InterPro Accession
domain Tyrosine-specific protein phosphatase, PTPase domain 1356 - 1614 IPR000242-1
domain Tyrosine-specific protein phosphatase, PTPase domain 1643 - 1905 IPR000242-2
domain Tyrosine-specific protein phosphatases domain 1532 - 1603 IPR000387-1
domain Tyrosine-specific protein phosphatases domain 1821 - 1894 IPR000387-2
domain Protein-tyrosine phosphatase, catalytic 1510 - 1611 IPR003595-1
domain Protein-tyrosine phosphatase, catalytic 1799 - 1902 IPR003595-2
domain Immunoglobulin subtype 2 36 - 105 IPR003598-1
domain Immunoglobulin subtype 2 138 - 214 IPR003598-2
domain Immunoglobulin subtype 2 248 - 309 IPR003598-3
domain Immunoglobulin subtype 30 - 116 IPR003599-1
domain Immunoglobulin subtype 132 - 226 IPR003599-2
domain Immunoglobulin subtype 242 - 320 IPR003599-3
domain Immunoglobulin subtype 509 - 603 IPR003599-4
domain Fibronectin type III 323 - 415 IPR003961-1
domain Fibronectin type III 418 - 516 IPR003961-2
domain Fibronectin type III 516 - 607 IPR003961-3
domain Fibronectin type III 609 - 709 IPR003961-4
domain Fibronectin type III 712 - 822 IPR003961-5
domain Fibronectin type III 823 - 919 IPR003961-6
domain Fibronectin type III 919 - 1016 IPR003961-7
domain Fibronectin type III 1018 - 1095 IPR003961-8
domain Immunoglobulin-like domain 24 - 114 IPR007110-1
domain Immunoglobulin-like domain 126 - 224 IPR007110-2
domain Immunoglobulin-like domain 236 - 318 IPR007110-3
domain Immunoglobulin I-set 24 - 115 IPR013098-1
domain Immunoglobulin I-set 127 - 216 IPR013098-2
active_site Protein-tyrosine phosphatase, active site 1551 - 1561 IPR016130-1
active_site Protein-tyrosine phosphatase, active site 1842 - 1852 IPR016130-2
domain Receptor-type tyrosine-protein phosphatase delta, PTPase domain, repeat 1 1334 - 1617 IPR045905

Functions

Description
EC Number 3.1.3.48 Phosphoric monoester hydrolases
Subcellular Localization
  • Membrane; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
hippocampal mossy fiber to CA3 synapse One of the giant synapses that form between the mossy fiber axons of dentate gyrus granule cells and the large complex spines of CA3 pyramidal cells. It consists of a giant bouton known as the mossy fiber expansion, synapsed to the complex, multiheaded spine (thorny excresence) of a CA3 pyramidal cell.
integral component of presynaptic membrane The component of the presynaptic membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
Schaffer collateral - CA1 synapse A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.

3 GO annotations of molecular function

Name Definition
cell adhesion molecule binding Binding to a cell adhesion molecule.
protein tyrosine phosphatase activity Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
signaling receptor binding Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.

13 GO annotations of biological process

Name Definition
heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules The attachment of an adhesion molecule in one cell to a nonidentical adhesion molecule in an adjacent cell.
modulation of chemical synaptic transmission Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission.
negative regulation of receptor signaling pathway via JAK-STAT Any process that stops, prevents, or reduces the frequency, rate or extent of a receptor signaling pathway via JAK-STAT.
neuron differentiation The process in which a relatively unspecialized cell acquires specialized features of a neuron.
positive regulation of dendrite morphogenesis Any process that activates or increases the frequency, rate or extent of dendrite morphogenesis.
positive regulation of synapse assembly Any process that activates, maintains or increases the frequency, rate or extent of synapse assembly, the aggregation, arrangement and bonding together of a set of components to form a synapse.
presynaptic membrane assembly The aggregation, arrangement and bonding together of a set of components to form a presynaptic membrane, including any proteins associated with the membrane, but excluding other cellular components. A presynaptic membrane is a specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
regulation of immune response Any process that modulates the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus.
regulation of postsynaptic density assembly Any process that modulates the frequency, rate or extent of postsynaptic density assembly, the aggregation, arrangement and bonding together of a set of components to form a postsynaptic density.
regulation of presynapse assembly Any process that modulates the frequency, rate or extent of presynapse assembly.
synaptic membrane adhesion The attachment of presynaptic membrane to postsynaptic membrane via adhesion molecules that are at least partially embedded in the plasma membrane.
trans-synaptic signaling by trans-synaptic complex Cell-cell signaling between presynapse and postsynapse mediated by a trans-synaptic protein complex.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q13332 PTPRS Receptor-type tyrosine-protein phosphatase S Homo sapiens (Human) PR
P10586 PTPRF Receptor-type tyrosine-protein phosphatase F Homo sapiens (Human) PR
Q15262 PTPRK Receptor-type tyrosine-protein phosphatase kappa Homo sapiens (Human) PR
P08575 PTPRC Receptor-type tyrosine-protein phosphatase C Homo sapiens (Human) PR
P28827 PTPRM Receptor-type tyrosine-protein phosphatase mu Homo sapiens (Human) PR
P23468 PTPRD Receptor-type tyrosine-protein phosphatase delta Homo sapiens (Human) PR
P49446 Ptpre Receptor-type tyrosine-protein phosphatase epsilon Mus musculus (Mouse) PR
P35822 Ptprk Receptor-type tyrosine-protein phosphatase kappa Mus musculus (Mouse) PR
10 20 30 40 50 60
MVPVARPLSL LLTFFLCACA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
70 80 90 100 110 120
GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ
130 140 150 160 170 180
IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
190 200 210 220 230 240
ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI
250 260 270 280 290 300
PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY
310 320 330 340 350 360
TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP
370 380 390 400 410 420
KNSEEPYKEI DGIATTRYSV AGLSPYSDYE FRVVAVNNIG RGPASEPVLT QTSEQAPSSA
430 440 450 460 470 480
PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG
490 500 510 520 530 540
NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR
550 560 570 580 590 600
SDTIASYELV YRDGDQGEEQ RITIEPGTSY RLQGLKPNSL YYFRLSARSP QGLGASTAEI
610 620 630 640 650 660
SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSLKYA AVDGEDFKPH
670 680 690 700 710 720
EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTDEDV PSGPPRKVEV
730 740 750 760 770 780
EAVNATAVKV SWRSPVPNKQ HGQIRGYQVH YVKMENGEPK GQPMLKDVML ADAQWEFDDT
790 800 810 820 830 840
TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL
850 860 870 880 890 900
IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK
910 920 930 940 950 960
VGFGEEMVKE ISVPEEIPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGV ITKYTLLYRD
970 980 990 1000 1010 1020
INVPLLPMEH LIVPADTSMT LTGLKSDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF
1030 1040 1050 1060 1070 1080
AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS
1090 1100 1110 1120 1130 1140
YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPD VPANENIKGY
1150 1160 1170 1180 1190 1200
YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP
1210 1220 1230 1240 1250 1260
TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMDHAESKM YATSPYSDPV VSMDLDPQPI
1270 1280 1290 1300 1310 1320
TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESESR KSSLPNSKEV PSHHPTDPVE
1330 1340 1350 1360 1370 1380
LRRLNFQTPG MASHPPIPIL ELADHIERLK ANDNLKFSQE YESIDPGQQF TWEHSNLEVN
1390 1400 1410 1420 1430 1440
KPKNRYANVI AYDHSRVLLS AIEGIPGSDY VNANYIDGYR KQNAYIATQG SLPETFGDFW
1450 1460 1470 1480 1490 1500
RMIWEQRSAT VVMMTKLEER SRVKCDQYWP SRGTETHGLV QVTLLDTVEL ATYCVRTFAL
1510 1520 1530 1540 1550 1560
YKNGSSEKRE VRQFQFTAWP DHGVPEHPTP FLAFLRRVKT CNPPDAGPMV VHCSAGVGRT
1570 1580 1590 1600 1610 1620
GCFIVIDAML ERIKHEKTVD IYGHVTLMRA QRNYMVQTED QYIFIHDALL EAVTCGNTEV
1630 1640 1650 1660 1670 1680
PARNLYAYIQ KLTQIETGEN VTGMELEFKR LASSKAHTSR FISANLPCNK FKNRLVNIMP
1690 1700 1710 1720 1730 1740
YESTRVCLQP IRGVEGSDYI NASFLDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV
1750 1760 1770 1780 1790 1800
VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV
1810 1820 1830 1840 1850 1860
RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV
1870 1880 1890 1900 1910
LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFCYRAA LEYLGSFDHY AT