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 Q00PJ8

Entry ID Method Resolution Chain Position Source
AF-Q00PJ8-F1 Predicted AlphaFoldDB

No variants for Q00PJ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q00PJ8

No associated diseases with Q00PJ8

12 regional properties for Q00PJ8

Type Name Position InterPro Accession
domain Protein kinase domain 1079 - 1346 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 1079 - 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
MKASAVLAPG ILVILFTLVQ KSNCECKEAL VKSKMNVNMK YQLPNFTAET PIQNVVLHNH
70 80 90 100 110 120
HIYLGAVNYI YVLSDKTLQK VAEYKTGPVL EHPDCLPCQD CRHKANLSNG IWKDNINMAL
130 140 150 160 170 180
LVDTYYDDQL ISCGSVHRGT CQRHVLPPNN AADIQSEVHC MYTPQPEEEP SQCPDCVVSA
190 200 210 220 230 240
LGTKVLLSEK NRFINFFVGN TINSSYLPDH SLHSMSVRRL KETQDGFKFL TDQSYIDVLP
250 260 270 280 290 300
EFRDSYPIKY IHAFKSNHFI YFLTVQRETL DAQTFHTRII RFCSGDSGLH SYMEMPLECI
310 320 330 340 350 360
LTEKRRKRAA REEVFNILQA AYVSKPGAHL ARQIGASLND DILYGVFAQS KPDSAEPMNR
370 380 390 400 410 420
SAVCAFPIKY VNEFFNKIVN KNNVRCLQHF YGPNHEHCFN RTLLRNSSSC DVRSDEYRTE
430 440 450 460 470 480
FTTALQRVDL FMGQFNQVLL TSISTFIKGD LTIANLGTSE GRFMQVVVSR LGSSTPHVNF
490 500 510 520 530 540
RLDSHPVSPE VIVEHPLNGN DYTLVVTGKK ITKIPLNGLG CEHFQSCSQC LSAPAFVQCG
550 560 570 580 590 600
WCHDKCVQLE ECPSGTWTQE TCLPTIYKVL PTSAPLEGGT TLTICGWDFG FRRNNKFDLK
610 620 630 640 650 660
KTRVFLGNES CTVTLSESST NMLKCTVGPA LYEHFNMSII ISNSRGTVQY STFSYVDPII
670 680 690 700 710 720
TSISPTYGPK TGGTLLTLTG KYLDSGNSRH ISIGGKTCTL KSVSNSILEC YTPPQTTSTE
730 740 750 760 770 780
FPVKLKIDLA NRNTYSFSYQ EDPIIYKIHP IKSFISGGST ITGVGKNLNS VSVLRMVINV
790 800 810 820 830 840
HEAGRNFTVA CQHRSNSEII CCTTPSLQQL DLQLPLTTRA FFMLDGIHSR YFDLIYVHNP
850 860 870 880 890 900
MFKVFEKPVK ISIGIENILE IKGNDIDPEA VKGEVLKVGN KSCENIHSYS ETVLCTVPND
910 920 930 940 950 960
LLKLNSELNI EWKQAVTSTV LGKVIVQPDQ NITEFIVGIL SISGILLTLL GLLLWWKKKK
970 980 990 1000 1010 1020
QIKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE SVDYRATFPE DQFPNSSQNG
1030 1040 1050 1060 1070 1080
SCRQVQYPLT DLSPILTSGD SDISSPLLQN TVHIDLSALN PELVQAVQHV VIGPSSLIVH
1090 1100 1110 1120 1130 1140
FNEVIGRGHF GCVYHGTLLD NDDKKIHCAV KSLNRITDIG EVSQFLTEGI IMKDFSHPNV
1150 1160 1170 1180 1190 1200
LSLLGICLRS EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLASKK
1210 1220 1230 1240 1250 1260
FVHRDLAARN CMLDENFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW MALESLQTQK
1270 1280 1290 1300 1310 1320
FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITVYLLQG RRLLQPEYCP DPLYEVMLKC
1330 1340 1350 1360 1370 1380
WHPKAELRPS FSELVSRISA IFSTFIGEHY VHVNATYVNI KCVAPYPSLL SSQDNFDSEG
NT