SEZ6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEZ6_HUMAN
• UniProt AC: Q53EL9
• Protein Name: Seizure protein 6 homolog
• Gene Name: SEZ6
• Organism: Homo sapiens (Human).
• Sequence Length: 994
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Localized on dendrites and in the synaptic and postsynaptic fraction..
• Protein Description: May play a role in cell-cell recognition and in neuronal membrane signaling. Seems to be important for the achievement of the necessary balance between dendrite elongation and branching during the elaboration of a complex dendritic arbor. Involved in the development of appropriate excitatory synaptic connectivity (By similarity)..
• Protein Sequence: MRPVALLLLPSLLALLAHGLSLEAPTVGKGQAPGIEETDGELTAAPTPEQPERGVHFVTTAPTLKLLNHHPLLEEFLQEGLEKGDEELRPALPFQPDPPAPFTPSPLPRLANQDSRPVFTSPTPAMAAVPTQPQSKEGPWSPESESPMLRITAPLPPGPSMAVPTLGPGEIASTTPPSRAWTPTQEGPGDMGRPWVAEVVSQGAGIGIQGTITSSTASGDDEETTTTTTIITTTITTVQTPGPCSWNFSGPEGSLDSPTDLSSPTDVGLDCFFYISVYPGYGVEIKVQNISLREGETVTVEGLGGPDPLPLANQSFLLRGQVIRSPTHQAALRFQSLPPPAGPGTFHFHYQAYLLSCHFPRRPAYGDVTVTSLHPGGSARFHCATGYQLKGARHLTCLNATQPFWDSKEPVCIAACGGVIRNATTGRIVSPGFPGNYSNNLTCHWLLEAPEGQRLHLHFEKVSLAEDDDRLIIRNGDNVEAPPVYDSYEVEYLPIEGLLSSGKHFFVELSTDSSGAAAGMALRYEAFQQGHCYEPFVKYGNFSSSTPTYPVGTTVEFSCDPGYTLEQGSIIIECVDPHDPQWNETEPACRAVCSGEITDSAGVVLSPNWPEPYGRGQDCIWGVHVEEDKRIMLDIRVLRIGPGDVLTFYDGDDLTARVLGQYSGPRSHFKLFTSMADVTIQFQSDPGTSVLGYQQGFVIHFFEVPRNDTCPELPEIPNGWKSPSQPELVHGTVVTYQCYPGYQVVGSSVLMCQWDLTWSEDLPSCQRVTSCHDPGDVEHSRRLISSPKFPVGATVQYICDQGFVLMGSSILTCHDRQAGSPKWSDRAPKCLLEQLKPCHGLSAPENGARSPEKQLHPAGATIHFSCAPGYVLKGQASIKCVPGHPSHWSDPPPICRAASLDGFYNSRSLDVAKAPAASSTLDAAHIAAAIFLPLVAMVLLVGGVYFYFSRLQGKSSLQLPRPRPRPYNRITIESAFDNPTYETGSLSFAGDERI

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
59	O-linked_Glycosylation	ERGVHFVTTAPTLKL CCCCEEEECHHHHHH	19.12	55829809
60	O-linked_Glycosylation	RGVHFVTTAPTLKLL CCCEEEECHHHHHHH	25.90	55829815
105	Phosphorylation	PPAPFTPSPLPRLAN CCCCCCCCCCCCCCC	35.69	24719451
131	Phosphorylation	PAMAAVPTQPQSKEG CCCCCCCCCCCCCCC	46.40	24043423
135	Phosphorylation	AVPTQPQSKEGPWSP CCCCCCCCCCCCCCC	39.08	24043423
289	N-linked_Glycosylation	GVEIKVQNISLREGE CEEEEEEEEEECCCC	28.89	UniProtKB CARBOHYD
315	Phosphorylation	PLPLANQSFLLRGQV CCCCCCCCCEECCEE	20.05	24719451
365	Phosphorylation	HFPRRPAYGDVTVTS CCCCCCCCCCEEEEE	19.28	17053785
387	Phosphorylation	RFHCATGYQLKGARH EEEECCCCEECCCEE	13.30	17053785
399	N-linked_Glycosylation	ARHLTCLNATQPFWD CEEEEECCCCCCCCC	42.99	UniProtKB CARBOHYD
436	N-linked_Glycosylation	VSPGFPGNYSNNLTC CCCCCCCCCCCCEEE	36.98	UniProtKB CARBOHYD
510	Phosphorylation	KHFFVELSTDSSGAA CEEEEEEECCCCCCH	19.36	22210691
511	Phosphorylation	HFFVELSTDSSGAAA EEEEEEECCCCCCHH	53.15	22210691
513	Phosphorylation	FVELSTDSSGAAAGM EEEEECCCCCCHHHH	30.66	22210691
541	N-linked_Glycosylation	EPFVKYGNFSSSTPT CCEEECCCCCCCCCC	30.45	UniProtKB CARBOHYD
649	Phosphorylation	PGDVLTFYDGDDLTA CCCEEEEECCCCHHH	17.49	25884760
709	Phosphorylation	FEVPRNDTCPELPEI EECCCCCCCCCCCCC	33.24	23403867
785	Phosphorylation	EHSRRLISSPKFPVG HHHHHHCCCCCCCCC	45.22	28060719
786	Phosphorylation	HSRRLISSPKFPVGA HHHHHCCCCCCCCCC	25.72	28060719
904	Phosphorylation	AASLDGFYNSRSLDV HHCCCCCCCCCCCCC	20.12	-
906	Phosphorylation	SLDGFYNSRSLDVAK CCCCCCCCCCCCCCC	16.33	-
981 (in isoform 3)	Phosphorylation	-	16.86	25884760

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SEZ6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEZ6_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SEZ6_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SEZ6_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-365 AND TYR-387, ANDMASS SPECTROMETRY.
PubMed: 17053785