RYK_HUMAN » Tyrosine-protein kinase RYK

RYK_HUMAN » Tyrosine-protein kinase RYK
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
RYK_HUMAN » Tyrosine-protein kinase RYK »
Hydrophobic Thickness 36.0 ± 1.8 Å
Tilt Angle 1 ± 0°
ΔGtransfer -45.0 kcal/mol
ΔGfold -21.9 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 225-253 (221-253)
Pathways none
PDB none
OPM none
Complexes none
Interactions

APLP2, Complex: RYK:APLP2, PubMed

CADH2, Complex: RYK:CADH2, PubMed

CD276, Complex: CD276:RYK, PubMed

CDHR1, Complex: CDHR1:RYK, PubMed

DSC2, Complex: RYK:DSC2, PubMed

DSC3, Complex: DSC3:RYK, PubMed

DSG2, Complex: RYK:DSG2, PubMed

EPHA4, Complex: RYK:EPHA4, PubMed

EPHB2, Complex: EPHB2:RYK, PubMed

EPHB3, Complex: RYK:EPHB3, PubMed

FAT3, Complex: FAT3:RYK, PubMed

FAT4, Complex: RYK:FAT4, PubMed

FREM2, Complex: RYK:FREM2, PubMed

ITM2B, Complex: RYK:ITM2B, PubMed

ITM2C, Complex: ITM2C:RYK, PubMed

MIRO2, Complex: MIRO2:RYK, PubMed

NOMO3, Complex: NOMO3:RYK, PubMed

NR3L1, Complex: NR3L1:RYK, PubMed

NRP2, Complex: NRP2:RYK, PubMed

PCD16, Complex: PCD16:RYK, PubMed

PCD20, Complex: RYK:PCD20, PubMed

PCDGB, Complex: PCDGB:RYK, PubMed

PCDH7, Complex: PCDH7:RYK, PubMed

PCDH9, Complex: PCDH9:RYK, PubMed

PTK7, Complex: RYK:PTK7, PubMed

PTPRF, Complex: PTPRF:RYK, PubMed

PTPRS, Complex: PTPRS:RYK, PubMed

TFR1, Complex: TFR1:RYK, PubMed

TIM50, Complex: TIM50:RYK, PubMed

TMEDA, Complex: TMEDA:RYK, PubMed

TMM59, Complex: TMM59:RYK, PubMed

Domains

AA: 63-191, PDBID: 2D3J, Subunit A, Seq Identity:22%, WIF domain

AA: 327-593, PDBID: 1GAG, Subunit A, Seq Identity:33%, Protein tyrosine kinase

UniProt annotation for RYK_HUMAN » Tyrosine-protein kinase RYK
FUNCTION: May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C- terminal cleavage occurs in its transmembrane region and allows the C-terminal intracellular product to translocate from the cytoplasm to the nucleus where it plays a crucial role in neuronal development.

CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

SUBUNIT: Interacts with DVL1 (via PDZ domain).

TISSUE SPECIFICITY: Observed in all the tissues examined.

DOMAIN: The extracellular WIF domain is responsible for Wnt binding.

UniProt features for RYK_HUMAN » Tyrosine-protein kinase RYK
SIGNAL 1 25 Potential.
CHAIN 26 604 Tyrosine-protein kinase RYK.
DOMAIN 63 191 WIF.
DOMAIN 327 600 Protein kinase.
ACT_SITE 462 462 Proton acceptor (By similarity).
Amino Acid Sequence for RYK_HUMAN » Tyrosine-protein kinase RYK
MRGAARLGRP GRSCLPGPAL RAAAAPALLL ARCAVAAAAG LRAAARPRPP ELQSASAGPS VSLYLSEDEV RRLIGLDAEL YYVRNDLISH YALSFNLLVP SETNFLHFTW HAKSKVEYKL GFQVDNVLAM DMPQVNISVQ GEVPRTLSVF RVELSCTGKV DSEVMILMQL NLTVNSSKNF TVLNFKRRKM CYKKLEEVKT SALDKNTSRT IYDPVHAAPT TSTRVFYISV GVCCAVIFLV AIILAVLHLH NMKRIELDDS ISASSSSQGL SQPSTQTTQY LRADTPNNAT PITSYPTLRI EKNDLRSVTL LEAKGKVKDI AISRERITLK DVLQEGTFGR IFHGILIDEK DPNKEKQAFV KTVKDQASEI QVTMMLTESC KLRGLHHRNL LPITHVCIEE GEKPMVILPY MNWGNLKLFL RQCKLVEANN PQAISQQDLV HMAIQIACGM SYLARREVIH KDLAARNCVI DDTLQVKITD NALSRDLFPM DYHCLGDNEN RPVRWMALES LVNNEFSSAS DVWAFGVTLW ELMTLGQTPY VDIDPFEMAA YLKDGYRIAQ PINCPDELFA VMACCWALDP EERPKFQQLV QCLTEFHAAL GAYV