Descriptions

Autoinhibitory domains (AIDs)

Target domain

718-775 (SH3A domain)

Relief mechanism

Assay

Target domain

718-775 (SH3A domain)

Relief mechanism

PTM

Assay

Target domain

1205-1391 (DH domain)

Relief mechanism

Partner binding, Ligand binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for A0A8V0YF29

Entry ID Method Resolution Chain Position Source

25 variants for A0A8V0YF29

Variant ID(s) Position Change Description Diseaes Association Provenance
rs734516689 114 M>L No EVA
rs737369769 130 V>F No EVA
rs3555239502 170 G>A No EVA
rs738023779 365 L>V No EVA
rs740196708 366 E>G No EVA
rs737211162 368 A>G No EVA
rs741343595 641 V>G No EVA
rs731201976 643 Q>K No EVA
rs3387384875 649 W>C No EVA
rs738675751 653 N>K No EVA
rs740712443 664 I>K No EVA
rs731619928 665 I>N No EVA
rs737891064 788 A>V No EVA
rs1058645295 789 E>Q No EVA
rs741272854 863 F>S No EVA
rs738172472 864 T>P No EVA
rs738240701 866 A>P No EVA
rs740257114 867 T>P No EVA
rs731404539 874 S>P No EVA
rs737263832 1161 W>G No EVA
rs732577223 1184 D>A No EVA
rs3387409568 1236 M>V No EVA
rs737206872 1274 S>A No EVA
rs732370290 1305 L>P No EVA
rs314233488 1662 I>R No EVA

No associated diseases with A0A8V0YF29

3 regional properties for A0A8V0YF29

Type Name Position InterPro Accession
domain Protein kinase domain 199 - 527 IPR000719
active_site Serine/threonine-protein kinase, active site 320 - 332 IPR008271
binding_site Protein kinase, ATP binding site 205 - 228 IPR017441

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.

2 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLAKHDQQFH SLKPTSGFIT GDQARNFFFQ SGLPQPVLAQ IWALADMNND GRMDQLEFSI
70 80 90 100 110 120
AMKLIKLKLQ GYQLPSALPP VMKQPPIALP SAPGFGIGGI ASMPSLTTVA PVPMASIPVV
130 140 150 160 170 180
GMSPPLVSSV PAAAVPPLAN GAPAVIQPLP AFAHPATLPK SSSFSRSGPG SQLNTKLQKA
190 200 210 220 230 240
QSFDVASVPP VAEWAVPQSS RLKYRQLFNS HDKTMSGHLT GPQARTILMQ SSLPQAQLAT
250 260 270 280 290 300
IWNLSDIDQD GKLTAEEFIL AMHLIDVAMS GQPLPPVLPP EYIPPSFRRV RSGSGVSAVS
310 320 330 340 350 360
SVSVDQRLPE EPALEEEQQQ LEKKLPVTFE DKKRENFERG NLELEKRRQA LLEQQRKEQE
370 380 390 400 410 420
RLAQLERAEQ ERKERERQEQ ERKRQLELEK QLEKQRELER QREEERRKEI ERREAAKREL
430 440 450 460 470 480
ERQRQLEWER NRRQELLNQR NREQEDIVVL KAKKKTLEFE LEALNDKKNQ LEGKLQDIRC
490 500 510 520 530 540
RLSTQRQEIE STNKSRELRI AEITHLQQQL QESQQMLGKL IPEKQLLNDQ LKQVQQNSLH
550 560 570 580 590 600
RDSLLTIKRA LEAKELARQQ LRDQLDEVEK ETRSKLQEID IFNNQLKELR EIHNRQQLQK
610 620 630 640 650 660
QKNLEAERLK QKEQERKTEL EKQKEAQRRI QDRDKQRLDR VQQEEEPQWQ KKNQEDDKQK
670 680 690 700 710 720
REEIIKKKES EDKGKQEIQE KPSKLFQPHQ EPVKPAVQAP WSNAGKAPLT ISAQEDVKIV
730 740 750 760 770 780
YYRALYPFES RSHDEITIQP GDIVMVDESQ TGEPGWLGGE LKGKTGWFPA NYAEKIPESE
790 800 810 820 830 840
VPASIKPAEA APAPKVSVHE TTTSLGTAAS TECTTTANNW ADFSSTWPAN TNEKPETDNW
850 860 870 880 890 900
DAWAAQPSLT VPSAGQLRQR SAFTPATVTG SSPSPVLGQG EKVEGLQAQA LYPWRAKKDN
910 920 930 940 950 960
HLNFNKNDVI TVLEQQDMWW FGEVQGQKGW FPKSYVKLIS GPIRKSTSMD SGSSESPASL
970 980 990 1000 1010 1020
KRVASPAAKA TMSGEEYVAM YTYESSEQGD LTFQQGDMIL VTKKDGDWWT GTLGDKTGVF
1030 1040 1050 1060 1070 1080
PSNYVRLKDS EASGAAGKTG SLGKKPEIAQ VIASYTATGP EQLTLAPGQL ILIRKKNPGG
1090 1100 1110 1120 1130 1140
WWEGELQGKK RQIGWFPANY VKLLSPGTSK TTPTELPKST ALPSVCQVIG MYDYTAQNDD
1150 1160 1170 1180 1190 1200
ELAFNKGQII NVLNKEDPDW WKGEVNGQVG LFPSNYVKLT TDMDPSQQWC ADLHLLDMLT
1210 1220 1230 1240 1250 1260
PTERKRQGYI HELIVTEENY VNDLQLVTEI FQKPLMESEL LTEKEVAMIF VNWKELIMCN
1270 1280 1290 1300 1310 1320
IKLLKALRVR KKMSGEKMPV KMIGDILTAQ LPHMQPYIRF CSCQLNGAAL IQQKTDEVPE
1330 1340 1350 1360 1370 1380
FKEFVKRLAM DPRCKGMPLS SFLLKPMQRV TRYPLIIKNI IENTPENHPD HSHLKHALEK
1390 1400 1410 1420 1430 1440
AEELCSQVNE GVREKENSDR LEWIQAHVQC EGLSEQLVFN SVTNCLGPRK FLHSGKLYKA
1450 1460 1470 1480 1490 1500
KSNKELYGFL FNDFLLLTQI IKPLGSSGTD KVFSPKSNLQ YKMYKTPIFL NEVLVKLPTD
1510 1520 1530 1540 1550 1560
PSGDEPIFHI SHIDRVYTLR AESINESFKG LMQMYLMYTF RSQRATGIGR LMVNIVEGIE
1570 1580 1590 1600 1610 1620
LKPCRSHGKS NPYCEVTMGS QCHITKTMQD TLNPKWNSNC QFFIKDLEQD VLCITVFERD
1630 1640 1650 1660 1670
QFSPDDFLGR TEIRVADIKK DQGSKGPVTK CLLLHEVPTG EIVVRLDLQL FDEP