W5PTP4

SS
Gene name
ITSN1
Protein name
Intersectin-1
Names
Species
Ovis aries (Sheep)
KEGG Pathway
EC number
Protein Class

Descriptions

Autoinhibitory domains (AIDs)

721-740 (N-terminal linker of SH3A) SS

Target domain

741-805 (SH3A domain)

Relief mechanism

Assay

806-842 (C-terminal linker of SH3A) SS

Target domain

741-805 (SH3A domain)

Relief mechanism

PTM

Assay

1160-1212 (SH3E domain) SS

Target domain

1239-1425 (DH domain)

Relief mechanism

Partner binding, Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for W5PTP4

Entry ID Method Resolution Chain Position Source

19 variants for W5PTP4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1087498793 111 S>R No Ensembl
rs589834280 134 M>V No Ensembl
rs1092909454 147 V>A No Ensembl
rs1090515553 158 L>P No Ensembl
rs604919532 211 P>S No Ensembl
rs159410631 335 S>L No Ensembl
rs591135034 381 E>K No Ensembl
rs1090086516 453 R>Q No Ensembl
rs1090483122 497 Q>K No Ensembl
rs1087843229 672 R>W No Ensembl
rs604024600 689 K>R No Ensembl
rs1093125290 773 G>E No Ensembl
rs600322648 864 N>Y No Ensembl
rs1090295439 1075 G>E No Ensembl
rs593772038 1159 V>M No Ensembl
rs601322493 1326 P>L No Ensembl
rs601642127 1382 Q>H No Ensembl
rs1086099328 1482 G>S No Ensembl
rs1092474941 1656 L>P No Ensembl

No associated diseases with W5PTP4

10 regional properties for W5PTP4

Type Name Position InterPro Accession
domain Protein kinase domain 669 - 918 IPR000719
domain Ephrin receptor ligand binding domain 33 - 236 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 669 - 913 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 212 - 232 IPR001426-1
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 285 - 305 IPR001426-2
domain Sterile alpha motif domain 944 - 1011 IPR001660
domain Fibronectin type III 368 - 485 IPR003961-1
domain Fibronectin type III 486 - 581 IPR003961-2
domain Tyrosine-protein kinase ephrin type A/B receptor-like 305 - 344 IPR011641
domain Ephrin receptor, transmembrane domain 595 - 666 IPR027936

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cell projection A prolongation or process extending from a cell, e.g. a flagellum or axon.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

2 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.

3 GO annotations of biological process

Name Definition
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a part of the plasma membrane to form a new membrane-bounded vesicle.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAQFPTPFGG SLDIWAITVE ERAKHDQQFH SLKPISGFIT GDQARNFFFQ SGLPQPVLAQ
70 80 90 100 110 120
IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSALPP VMKQQPVAIS SAPAFGMGGI
130 140 150 160 170 180
ASMPPLTAVA PVPMGSIPVV GMSPPLVSSV PAAGVPPLAN GAPPVIQPLP AFAHPAATLP
190 200 210 220 230 240
KSSSFSRSGP GSQLNTKLQK AQSFDVASVP PAAEWAVPQS SRLKYRQLFN SHDKTMSGHL
250 260 270 280 290 300
TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP
310 320 330 340 350 360
PEYIPPSFRR VRSGSGISVI SSTSVDQRLP EEPVSEDEQQ QLEKKLPVTF EDKKRENFER
370 380 390 400 410 420
GNLELEKRRQ ALLEQQRKEQ ERLAQLERAE QERKERERQE QERKRQLELE KQLEKQRELE
430 440 450 460 470 480
RQREEERRKE IERREAAKRE LERQRQLEWE RNRRQELLNQ RNKEQEDIVV LKAKKKTLEF
490 500 510 520 530 540
ELEALNDKKH QLEGKLQDIR CRLTTQRQEI ESTNKSRELR IAEITHLQQQ LQESQQMLGR
550 560 570 580 590 600
LIPEKQILND QLKQVQQNSL HRDSLLTLKR ALEAKELARQ QLRDQLDEVE KETRSKLQEI
610 620 630 640 650 660
DIFNNQLKEL REMHNKQQLQ KQKSIEAERL KQKEQERKIL ELEKQKEEAQ RRAQERDQQW
670 680 690 700 710 720
LERMHQEDEQ QRPRKPHEEE KLKREESVKK KDSEEKGKPE MQDKLSRLFH QQQEPAKPAV
730 740 750 760 770 780
QAPWSTAEKG PLTISAQENV KVVYYRALYP FESRSHDEIT IQPGDIVMVE VKGEWVDESQ
790 800 810 820 830 840
TGEPGWLGGE LKGKTGWFPA NYAEKIPENE VPAPVKPVTE VASTPTPKVA VRETPAPSTA
850 860 870 880 890 900
TPAEPSETPN NWADFSSTWP ASTNEKPETD SWDAWATQPS LTVPSAGQLR QRSAFTPATA
910 920 930 940 950 960
TGSSPSPVLG QGEKVEGLQA QALYPWRAKK DNHLNFNKND VITVLEQQDM WWFGEVQGQK
970 980 990 1000 1010 1020
GWFPKSYVKL ISGPIRKSTS MDSGSSESPA SLKRVASPAA KPAVSGEEFI AMYTYESSEQ
1030 1040 1050 1060 1070 1080
GDLTFQQGDV ILVTKKDGDW WTGTVGDKSG VFPSNYVRLK DSEGSGTAGK TGSLGKKPEI
1090 1100 1110 1120 1130 1140
AQVIASYTAT GPEQLTLAPG QLILIRKKNP GGWWEGELQA RGKKRQIGWF PANYVKLLSP
1150 1160 1170 1180 1190 1200
GTSKITPTDP LKPTAFPTVC QVIGMYDYTA QNDDELAFSK GQVINVLSKE DPDWWKGEVH
1210 1220 1230 1240 1250 1260
GQVGLFPSNY VKLTPDTDPS QQWCSDLHLL DMLTPTERKR QGYIHELIVT EENYVNDLQL
1270 1280 1290 1300 1310 1320
VTEIFQKPLM ESELLTEKEG AMIFVNWKEL IMCNIKLLKA LRVRKKMSGE KMPVKMIGDI
1330 1340 1350 1360 1370 1380
LTAQLPHMQP YIRFCSCQLN GAALIQQKTD EAPDFKEFVK RLAMDPRCKG MPLSSFILKP
1390 1400 1410 1420 1430 1440
MQRVTRYPLI IKNILENTPE NHPDHSHLKH ALEKAEELCS QVNEGVREKE NSDRLEWIQA
1450 1460 1470 1480 1490 1500
HVQCEGLSEQ LVFNSVTNCL GPRKFLHSGK LYKAKSNKEL YGFLFNDFLL LTQIIKPLGS
1510 1520 1530 1540 1550 1560
SGTDKVFSPK SNLQYKMYKT PIFLNEVLVK LPTDPSGDEP IFHISHIDRV YTLRAESINE
1570 1580 1590 1600 1610 1620
RTAWVQKIKA ASELYIETEK KKREKAYLVR SQRATGIGRL MVNVVEGIEL KPCRSHGKSN
1630 1640 1650 1660 1670 1680
PYCEVTMGSQ CHITKTIQDT LNPKWNSNCQ FFIRDLEQEV LCITVFERDQ FSPDDFLGRT
1690 1700 1710 1720
EIRVADIKKD QGSKGPVTKC LLLHEVPTGE IVVRLDLQLF DEP