SLIT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLIT3_HUMAN
• UniProt AC: O75094
• Protein Name: Slit homolog 3 protein
• Gene Name: SLIT3
• Organism: Homo sapiens (Human).
• Sequence Length: 1523
• Subcellular Localization: Secreted.
• Protein Description: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors..
• Protein Sequence: MAPGWAGVGAAVRARLALALALASVLSGPPAVACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDRNNITRITKMDFAGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDLSENQIQGIPRKAFRGITDVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTLRLHSNHLYCDCHLAWLSDWLRQRRTVGQFTLCMAPVHLRGFNVADVQKKEYVCPAPHSEPPSCNANSISCPSPCTCSNNIVDCRGKGLMEIPANLPEGIVEIRLEQNSIKAIPAGAFTQYKKLKRIDISKNQISDIAPDAFQGLKSLTSLVLYGNKITEIVKGLFDGLVSLQLLLLNANKINCLRVNTFQDLQNLNLLSLYDNKLQTISKGLFAPLQSIQTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSSPRRLANKRISQIKSKKFRCSGSEDYRSRFSSECFMDLVCPEKCRCEGTIVDCSNQKLVRIPSHLPEYVTDLRLNDNEVSVLEATGIFKKLPNLRKINLSNNKIKEVREGAFDGAASVQELMLTGNQLETVHGRVFRGLSGLKTLMLRSNLIGCVSNDTFAGLSSVRLLSLYDNRITTITPGAFTTLVSLSTINLLSNPFNCNCHLAWLGKWLRKRRIVSGNPRCQKPFFLKEIPIQDVAIQDFTCDGNEESSCQLSPRCPEQCTCMETVVRCSNKGLRALPRGMPKDVTELYLEGNHLTAVPRELSALRHLTLIDLSNNSISMLTNYTFSNMSHLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPEGSFNDLTSLSHLALGTNPLHCDCSLRWLSEWVKAGYKEPGIARCSSPEPMADRLLLTTPTHRFQCKGPVDINIVAKCNACLSSPCKNNGTCTQDPVELYRCACPYSYKGKDCTVPINTCIQNPCQHGGTCHLSDSHKDGFSCSCPLGFEGQRCEINPDDCEDNDCENNATCVDGINNYVCICPPNYTGELCDEVIDHCVPELNLCQHEAKCIPLDKGFSCECVPGYSGKLCETDNDDCVAHKCRHGAQCVDTINGYTCTCPQGFSGPFCEHPPPMVLLQTSPCDQYECQNGAQCIVVQQEPTCRCPPGFAGPRCEKLITVNFVGKDSYVELASAKVRPQANISLQVATDKDNGILLYKGDNDPLALELYQGHVRLVYDSLSSPPTTVYSVETVNDGQFHSVELVTLNQTLNLVVDKGTPKSLGKLQKQPAVGINSPLYLGGIPTSTGLSALRQGTDRPLGGFHGCIHEVRINNELQDFKALPPQSLGVSPGCKSCTVCKHGLCRSVEKDSVVCECRPGWTGPLCDQEARDPCLGHRCHHGKCVATGTSYMCKCAEGYGGDLCDNKNDSANACSAFKCHHGQCHISDQGEPYCLCQPGFSGEHCQQENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQCCQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS

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
72	N-linked_Glycosylation	RLDLDRNNITRITKM HHCCCCCCCCHHEEC	37.59	UniProtKB CARBOHYD
141	Phosphorylation	KLTRLDLSENQIQGI CCEECCCCCCCCCCC	33.88	27732954
187	Phosphorylation	LRDLEILTLNNNNIS HHCCEEEEECCCCEE	32.85	24114839
192	N-linked_Glycosylation	ILTLNNNNISRILVT EEEECCCCEEEEEEE	35.42	UniProtKB CARBOHYD
194	Phosphorylation	TLNNNNISRILVTSF EECCCCEEEEEEEEC	18.52	22210691
199	Phosphorylation	NISRILVTSFNHMPK CEEEEEEEECCCCCC	24.93	28509920
200	Phosphorylation	ISRILVTSFNHMPKI EEEEEEEECCCCCCC	19.30	28509920
209	Phosphorylation	NHMPKIRTLRLHSNH CCCCCCCEEEECCCE	21.50	30576142
330	Phosphorylation	PAGAFTQYKKLKRID CCCHHHCHHCCCCCC	13.66	22817900
417	Phosphorylation	LYDNKLQTISKGLFA HCCCCCCHHHCCCCC	37.34	-
419	Phosphorylation	DNKLQTISKGLFAPL CCCCCHHHCCCCCCH	24.86	-
451	Phosphorylation	HLKWLADYLQDNPIE HHHHHHHHHHCCCCC	10.72	28111955
459	Phosphorylation	LQDNPIETSGARCSS HHCCCCCCCCCCCCC	32.93	28111955
460	Phosphorylation	QDNPIETSGARCSSP HCCCCCCCCCCCCCH	20.05	28111955
465	Phosphorylation	ETSGARCSSPRRLAN CCCCCCCCCHHHHCC	37.51	28111955
466	Phosphorylation	TSGARCSSPRRLANK CCCCCCCCHHHHCCC	26.50	28111955
473	Acetylation	SPRRLANKRISQIKS CHHHHCCCHHHHHHC	45.56	22361369
476	Phosphorylation	RLANKRISQIKSKKF HHCCCHHHHHHCCCC	29.86	24719451
561	Acetylation	KKLPNLRKINLSNNK HHCCCCCCCCCCCCC	38.83	7340095
563	N-linked_Glycosylation	LPNLRKINLSNNKIK CCCCCCCCCCCCCCH	40.21	UniProtKB CARBOHYD
582	Phosphorylation	GAFDGAASVQELMLT CCCCCCCCHHHHHHH	24.65	-
605	Phosphorylation	GRVFRGLSGLKTLML HHHHCCCCHHHHHHH	44.92	24719451
609	Phosphorylation	RGLSGLKTLMLRSNL CCCCHHHHHHHHCCE	23.57	24719451
622	N-linked_Glycosylation	NLIGCVSNDTFAGLS CEEEEECCCCCCCCC	31.76	UniProtKB CARBOHYD
629	Phosphorylation	NDTFAGLSSVRLLSL CCCCCCCCCEEEEEC	26.35	24719451
784	N-linked_Glycosylation	LTLIDLSNNSISMLT CEEEECCCCCCHHHH	54.27	UniProtKB CARBOHYD
792	N-linked_Glycosylation	NSISMLTNYTFSNMS CCCHHHHCCCCCCCC	29.86	UniProtKB CARBOHYD
797	N-linked_Glycosylation	LTNYTFSNMSHLSTL HHCCCCCCCCHHHHH	31.61	UniProtKB CARBOHYD
928	N-linked_Glycosylation	LSSPCKNNGTCTQDP HCCCCCCCCCCCCCH	32.42	UniProtKB CARBOHYD
932	Phosphorylation	CKNNGTCTQDPVELY CCCCCCCCCCHHHHE	35.53	29083192
939	Phosphorylation	TQDPVELYRCACPYS CCCHHHHEEEECCCC	7.08	29083192
945	Phosphorylation	LYRCACPYSYKGKDC HEEEECCCCCCCCCC	25.23	29083192
946	Phosphorylation	YRCACPYSYKGKDCT EEEECCCCCCCCCCE	12.91	29083192
947	Phosphorylation	RCACPYSYKGKDCTV EEECCCCCCCCCCEE	20.23	29083192
1008	N-linked_Glycosylation	EDNDCENNATCVDGI CCCCCCCCCEEEECC	17.84	UniProtKB CARBOHYD
1025	N-linked_Glycosylation	YVCICPPNYTGELCD EEEECCCCCCCHHHH	31.94	UniProtKB CARBOHYD
1067	O-linked_Glycosylation	CECVPGYSGKLCETD CEECCCCCCCCCCCC	35.05	28657654
1173	Phosphorylation	DSYVELASAKVRPQA CCCEEECCCEEECCC	41.04	-
1181	N-linked_Glycosylation	AKVRPQANISLQVAT CEEECCCCEEEEEEE	21.09	UniProtKB CARBOHYD
1247	N-linked_Glycosylation	SVELVTLNQTLNLVV EEEEEECCCEECEEE	24.35	UniProtKB CARBOHYD
1295	O-linked_Glycosylation	LSALRQGTDRPLGGF HHHHHCCCCCCCCCC	22.09	55834889
1385	Phosphorylation	HHGKCVATGTSYMCK CCCCEEECCCCEEEE	22.16	-
1387	Phosphorylation	GKCVATGTSYMCKCA CCEEECCCCEEEECC	16.60	-
1388	Phosphorylation	KCVATGTSYMCKCAE CEEECCCCEEEECCC	16.53	-
1389	Phosphorylation	CVATGTSYMCKCAEG EEECCCCEEEECCCC	13.33	-
1406	N-linked_Glycosylation	GDLCDNKNDSANACS CCCCCCCCCCCCCCC	55.51	UniProtKB CARBOHYD
1425	Phosphorylation	HHGQCHISDQGEPYC CCCEEEECCCCCCEE	10.54	28787133
1431	Phosphorylation	ISDQGEPYCLCQPGF ECCCCCCEEEECCCC	8.18	28787133

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

Oops, there are no upstream regulatory protein records of SLIT3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SLIT3_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 SLIT3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SLIT3_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.