UNC5B_HUMAN - dbPTM
UNC5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UNC5B_HUMAN
UniProt AC Q8IZJ1
Protein Name Netrin receptor UNC5B
Gene Name UNC5B
Organism Homo sapiens (Human).
Sequence Length 945
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Membrane raft . Associated with lipid rafts.
Protein Description Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Functions as netrin receptor that negatively regulates vascular branching during angiogenesis. Mediates retraction of tip cell filopodia on endothelial growth cones in response to netrin (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. [PubMed: 12598906 Mediates apoptosis by activating DAPK1. In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (By similarity]
Protein Sequence MGARSGARGALLLALLLCWDPRLSQAGTDSGSEVLPDSFPSAPAEPLPYFLQEPQDAYIVKNKPVELRCRAFPATQIYFKCNGEWVSQNDHVTQEGLDEATGLRVREVQIEVSRQQVEELFGLEDYWCQCVAWSSAGTTKSRRAYVRIAYLRKNFDQEPLGKEVPLDHEVLLQCRPPEGVPVAEVEWLKNEDVIDPTQDTNFLLTIDHNLIIRQARLSDTANYTCVAKNIVAKRRSTTATVIVYVNGGWSSWAEWSPCSNRCGRGWQKRTRTCTNPAPLNGGAFCEGQAFQKTACTTICPVDGAWTEWSKWSACSTECAHWRSRECMAPPPQNGGRDCSGTLLDSKNCTDGLCMQNKKTLSDPNSHLLEASGDAALYAGLVVAIFVVVAILMAVGVVVYRRNCRDFDTDITDSSAALTGGFHPVNFKTARPSNPQLLHPSVPPDLTASAGIYRGPVYALQDSTDKIPMTNSPLLDPLPSLKVKVYSSSTTGSGPGLADGADLLGVLPPGTYPSDFARDTHFLHLRSASLGSQQLLGLPRDPGSSVSGTFGCLGGRLSIPGTGVSLLVPNGAIPQGKFYEMYLLINKAESTLPLSEGTQTVLSPSVTCGPTGLLLCRPVILTMPHCAEVSARDWIFQLKTQAHQGHWEEVVTLDEETLNTPCYCQLEPRACHILLDQLGTYVFTGESYSRSAVKRLQLAVFAPALCTSLEYSLRVYCLEDTPVALKEVLELERTLGGYLVEEPKPLMFKDSYHNLRLSLHDLPHAHWRSKLLAKYQEIPFYHIWSGSQKALHCTFTLERHSLASTELTCKICVRQVEGEGQIFQLHTTLAETPAGSLDTLCSAPGSTVTTQLGPYAFKIPLSIRQKICNSLDAPNSRGNDWRMLAQKLSMDRYLNYFATKASPTGVILDLWEALQQDDGDLNSLASALEEMGKSEMLVAVATDGDC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
41O-linked_GlycosylationVLPDSFPSAPAEPLP
CCCCCCCCCCCCCCC
44.89OGP
101UbiquitinationQEGLDEATGLRVREV
CCCHHHHHCCEEEEE
34.4023503661
139UbiquitinationAWSSAGTTKSRRAYV
EECCCCCCHHHHHHH
26.5522817900
220PhosphorylationRQARLSDTANYTCVA
ECCHHCCCCCCEEEE
17.2728152594
222N-linked_GlycosylationARLSDTANYTCVAKN
CHHCCCCCCEEEEEE
34.44UniProtKB CARBOHYD
223PhosphorylationRLSDTANYTCVAKNI
HHCCCCCCEEEEEEE
10.0728152594
224PhosphorylationLSDTANYTCVAKNIV
HCCCCCCEEEEEEEH
10.5828152594
341PhosphorylationGGRDCSGTLLDSKNC
CCCCCCCCCCCCCCC
14.09-
347N-linked_GlycosylationGTLLDSKNCTDGLCM
CCCCCCCCCCCCCCC
37.56UniProtKB CARBOHYD
403S-palmitoylationVVVYRRNCRDFDTDI
HHHCCCCCCCCCCCC
4.1318582460
411PhosphorylationRDFDTDITDSSAALT
CCCCCCCCCCHHHHH
32.4127732954
413PhosphorylationFDTDITDSSAALTGG
CCCCCCCCHHHHHCC
17.1527732954
414PhosphorylationDTDITDSSAALTGGF
CCCCCCCHHHHHCCC
21.9927732954
416 (in isoform 2)Ubiquitination-13.96-
416UbiquitinationDITDSSAALTGGFHP
CCCCCHHHHHCCCCC
13.9623503661
422UbiquitinationAALTGGFHPVNFKTA
HHHHCCCCCCCCCCC
28.7723503661
427UbiquitinationGFHPVNFKTARPSNP
CCCCCCCCCCCCCCC
35.7523503661
428PhosphorylationFHPVNFKTARPSNPQ
CCCCCCCCCCCCCCC
24.6224719451
452PhosphorylationLTASAGIYRGPVYAL
CCCCCCCCCCCEEEE
14.4825884760
454UbiquitinationASAGIYRGPVYALQD
CCCCCCCCCEEEECC
10.0722817900
454 (in isoform 2)Ubiquitination-10.0721906983
457PhosphorylationGIYRGPVYALQDSTD
CCCCCCEEEECCCCC
12.5321945579
460UbiquitinationRGPVYALQDSTDKIP
CCCEEEECCCCCCCC
34.1422817900
462PhosphorylationPVYALQDSTDKIPMT
CEEEECCCCCCCCCC
26.0821945579
463PhosphorylationVYALQDSTDKIPMTN
EEEECCCCCCCCCCC
49.9921945579
465 (in isoform 1)Ubiquitination-49.1221906983
465UbiquitinationALQDSTDKIPMTNSP
EECCCCCCCCCCCCC
49.1222817900
469PhosphorylationSTDKIPMTNSPLLDP
CCCCCCCCCCCCCCC
27.4727732954
471PhosphorylationDKIPMTNSPLLDPLP
CCCCCCCCCCCCCCC
14.0425159151
479PhosphorylationPLLDPLPSLKVKVYS
CCCCCCCCCEEEEEE
48.8024719451
511PhosphorylationGVLPPGTYPSDFARD
CCCCCCCCCCHHHCC
13.4725884760
526PhosphorylationTHFLHLRSASLGSQQ
CCEEEEEECCCCCHH
28.6828450419
528PhosphorylationFLHLRSASLGSQQLL
EEEEEECCCCCHHHH
34.2129743597
531PhosphorylationLRSASLGSQQLLGLP
EEECCCCCHHHHCCC
21.7522617229
581PhosphorylationQGKFYEMYLLINKAE
CCCEEEEEEEEECCC
6.09-
679PhosphorylationILLDQLGTYVFTGES
HHHHHCCCEEECCCC
25.7123312004
680PhosphorylationLLDQLGTYVFTGESY
HHHHCCCEEECCCCC
7.5623312004
683PhosphorylationQLGTYVFTGESYSRS
HCCCEEECCCCCCHH
29.9623312004
686PhosphorylationTYVFTGESYSRSAVK
CEEECCCCCCHHHHH
29.7423312004
687PhosphorylationYVFTGESYSRSAVKR
EEECCCCCCHHHHHH
12.1023312004
688PhosphorylationVFTGESYSRSAVKRL
EECCCCCCHHHHHHH
29.1023312004
690PhosphorylationTGESYSRSAVKRLQL
CCCCCCHHHHHHHHH
31.3223312004
711PhosphorylationLCTSLEYSLRVYCLE
HHHHHHEEEEEEECC
10.5824719451
733PhosphorylationEVLELERTLGGYLVE
HHHHHHHHHCCCCCC
22.0018452278
737PhosphorylationLERTLGGYLVEEPKP
HHHHHCCCCCCCCCC
13.0318452278
757PhosphorylationSYHNLRLSLHDLPHA
CCCCEEEEHHHCCCH
19.7526356563
768PhosphorylationLPHAHWRSKLLAKYQ
CCCHHHHHHHHHHHC
23.5926356563
800PhosphorylationTFTLERHSLASTELT
EEEEEECCCCCCEEE
31.67-
803PhosphorylationLERHSLASTELTCKI
EEECCCCCCEEEEEE
27.92-
804PhosphorylationERHSLASTELTCKIC
EECCCCCCEEEEEEE
29.43-
807PhosphorylationSLASTELTCKICVRQ
CCCCCEEEEEEEEEE
12.91-
835PhosphorylationLAETPAGSLDTLCSA
EEECCCCCHHHHCCC
25.7728348404
838PhosphorylationTPAGSLDTLCSAPGS
CCCCCHHHHCCCCCC
34.6528348404
841PhosphorylationGSLDTLCSAPGSTVT
CCHHHHCCCCCCEEE
40.3828348404
869PhosphorylationIRQKICNSLDAPNSR
HHHHHHHCCCCCCCC
24.1827732954
875PhosphorylationNSLDAPNSRGNDWRM
HCCCCCCCCCCHHHH
40.2727732954
892PhosphorylationQKLSMDRYLNYFATK
HHHCHHHHHHHHHCC
8.6025884760
895PhosphorylationSMDRYLNYFATKASP
CHHHHHHHHHCCCCC
7.6225884760

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UNC5B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UNC5B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UNC5B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAB_HUMANPPP2R1Bphysical
21172653
DAPK1_HUMANDAPK1physical
21172653
CIP2A_HUMANKIAA1524physical
21172653

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UNC5B_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Lipid raft localization and palmitoylation: identification of tworequirements for cell death induction by the tumor suppressorsUNC5H.";
Maisse C., Rossin A., Cahuzac N., Paradisi A., Klein C., Haillot M.L.,Herincs Z., Mehlen P., Hueber A.O.;
Exp. Cell Res. 314:2544-2552(2008).
Cited for: PALMITOYLATION AT CYS-403, SUBCELLULAR LOCATION, AND INTERACTION WITHDAPK1.

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