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

1222-1249 (Activation loop from InterPro)

Target domain

1079-1346 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q09YN5

Entry ID Method Resolution Chain Position Source
AF-Q09YN5-F1 Predicted AlphaFoldDB

No variants for Q09YN5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q09YN5

No associated diseases with Q09YN5

12 regional properties for Q09YN5

Type Name Position InterPro Accession
domain Protein kinase domain 1079 - 1346 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 1080 - 1337 IPR001245
domain Sema domain 27 - 516 IPR001627
repeat Plexin repeat 521 - 562 IPR002165
domain IPT domain 563 - 656 IPR002909-1
domain IPT domain 657 - 740 IPR002909-2
domain IPT domain 742 - 837 IPR002909-3
domain IPT domain 839 - 935 IPR002909-4
active_site Tyrosine-protein kinase, active site 1201 - 1213 IPR008266
domain PSI domain 520 - 563 IPR016201
binding_site Protein kinase, ATP binding site 1085 - 1111 IPR017441
domain Tyrosine-protein kinase, catalytic domain 1079 - 1338 IPR020635

Functions

Description
EC Number 2.7.10.1 Protein-tyrosine kinases
Subcellular Localization
  • Membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
integral component of membrane The component of a 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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
semaphorin receptor activity Combining with a semaphorin, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
transmembrane receptor protein tyrosine kinase activity Combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.

4 GO annotations of biological process

Name Definition
positive chemotaxis The directed movement of a motile cell or organism towards a higher concentration of a chemical.
positive regulation of endothelial cell chemotaxis Any process that activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
semaphorin-plexin signaling pathway The series of molecular signals generated as a consequence of a semaphorin receptor (composed of a plexin and a neurophilin) binding to a semaphorin ligand.
transmembrane receptor protein tyrosine kinase signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKAPAVLAPG ILVLLFTLVP RSHGECKEAL VKSEMNVNMK YQLPNFTAET PIQNVLLHQH
70 80 90 100 110 120
HVYLGAINHI YVLNDKDLQK VAEYTTGPVL EHPDCLPCQD CSSKANSSGA VWKDNINLAL
130 140 150 160 170 180
LVDKYYDDQL ISCGSVNRGT CQRHVLPPDN PADIQSGVYC MFSPQADEEP GQCPDCVVSP
190 200 210 220 230 240
LGAKVLLSKK QRFIYFFVGN TINSSYLPDH SLHSISVRRL KETQDGFKFL TDQSYIDVLP
250 260 270 280 290 300
EFRDSYPIKY VHAFESNHFI YFLTVQKETL DAQTFHTRII RFCSKDSGLH SYMEMPLECI
310 320 330 340 350 360
LTEKRRKRAT REEVFNILQA AYVSKPGAHL ARQIGATPND DILYGVFAQS KPDSAEPMNR
370 380 390 400 410 420
SAVCAFPIKY INEFFNKIVN KNNVKCLQHF YGPNHEHCFN RTLLRNSSDC EARSDEYRTE
430 440 450 460 470 480
LTTALQRVDL FMGQFNQVLL TSISTFIKGD LTIANLGTSE GRFMQVVISR TILNVPHVNF
490 500 510 520 530 540
RLDSHPVSPE VVVEHPLNQN GYTLVVTGNK ITKIPLNGLG CGHFQSCSQC LSAPPFVQCG
550 560 570 580 590 600
WCHDKCVPSE ECPSGTWTQE ICLPAIYKVF PASAPLEGGT TLTICGWDFG FRKNNKFDLK
610 620 630 640 650 660
KTKVLLGNES CALNLSESTT NTLKCTVGAT THEHFNMSIT VSNSRGRTQY STFSYVAPVI
670 680 690 700 710 720
TSISPSYGPK AGGTLLTLTG KYLDSGNSRH ISIGGKTCTL KSMSNSILEC YTPAQTISTE
730 740 750 760 770 780
FPVKLEIDLA SRETSSFSYR EDPIVDEFYP TKSFISGGST ITGVGKNLDS VSVPRMVISV
790 800 810 820 830 840
HEAGSNFTVA CQHRSNSEII CCTTPSLQQL NLHLPLKTKA FFMLDGILSK HFDLTYVHNP
850 860 870 880 890 900
VFKPFEKPVM ISMGNENVLE IKGNDIDPEA VKGEVLKVGN KSCENIHSDS EAVLCTVPND
910 920 930 940 950 960
LLKLNSELNI EWKQAVSSTV LGKVIVQPDQ NFMGLIVGGV SISIILLLLL GLFLWLKKKK
970 980 990 1000 1010 1020
RIKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE SVDYRATFPE DQFPNSSQNG
1030 1040 1050 1060 1070 1080
SCRQVQYPLT DLSPILTSGD SDISSPLLQN TVHIDLSALN PELVQAVQHV VIGPSSLIVH
1090 1100 1110 1120 1130 1140
FSEVIGRGHF GCVYHGTLLD NDGKKIHCAV KSLNRITDIG EVSQFLTEGI IMKDFSHPNV
1150 1160 1170 1180 1190 1200
LSLLGICLRS EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLASKK
1210 1220 1230 1240 1250 1260
FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW MALESLQTQK
1270 1280 1290 1300 1310 1320
FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITVYLLQG RRLLQPEYCP DALYEVMLKC
1330 1340 1350 1360 1370 1380
WHPKAEMRPS FSELVSRIST IFSTFIGEHY VHVNATYVNV KCVAPYPSLL SSQDNVDGTV
DT