SLIT1_HUMAN - dbPTM
SLIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLIT1_HUMAN
UniProt AC O75093
Protein Name Slit homolog 1 protein
Gene Name SLIT1
Organism Homo sapiens (Human).
Sequence Length 1534
Subcellular Localization Secreted.
Protein Description Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb..
Protein Sequence MALTPGWGSSAGPVRPELWLLLWAAAWRLGASACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLHMLPELLFQNNQALSRLDLSENAIQAIPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAGRVPTCTLSSGSCPAMCTCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETSGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYQLNSECNSDVVCPHKCRCEANVVECSSLKLTKIPERIPQSTAELRLNNNEISILEATGMFKKLTHLKKINLSNNKVSEIEDGAFEGAASVSELHLTANQLESIRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNQITTVSPGAFDTLQSLSTLNLLANPFNCNCQLAWLGGWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEGGCLPRPQCPQECACLDTVVRCSNKHLRALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDISTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPQDMEGKLLLTTPAKKFECQGPPTLAVQAKCDLCLSSPCQNQGTCHNDPLEVYRCACPSGYKGRDCEVSLDSCSSGPCENGGTCHAQEGEDAPFTCSCPTGFEGPTCGVNTDDCVDHACANGGVCVDGVGNYTCQCPLQYEGKACEQLVDLCSPDLNPCQHEAQCVGTPDGPRCECMPGYAGDNCSENQDDCRDHRCQNGAQCMDEVNSYSCLCAEGYSGQLCEIPPHLPAPKSPCEGTECQNGANCVDQGNRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVAFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTGFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPMCHCEAGWVGLHCDQPADGPCHGHKCVHGQCVPLDALSYSCQCQDGYSGALCNQAGALAEPCRGLQCLHGHCQASGTKGAHCVCDPGFSGELCEQESECRGDPVRDFHQVQRGYAICQTTRPLSWVECRGSCPGQGCCQGLRLKRRKFTFECSDGTSFAEEVEKPTKCGCALCA
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
4Phosphorylation----MALTPGWGSSA
----CCCCCCCCCCC
27.1525002506
9PhosphorylationALTPGWGSSAGPVRP
CCCCCCCCCCCCCCH
15.5425002506
10PhosphorylationLTPGWGSSAGPVRPE
CCCCCCCCCCCCCHH
33.0525002506
72N-linked_GlycosylationRLELNGNNITRIHKN
CEEECCCCCEEECCC
38.11UniProtKB CARBOHYD
74PhosphorylationELNGNNITRIHKNDF
EECCCCCEEECCCCC
26.20-
78AcetylationNNITRIHKNDFAGLK
CCCEEECCCCCCHHH
56.707374123
78UbiquitinationNNITRIHKNDFAGLK
CCCEEECCCCCCHHH
56.70-
85AcetylationKNDFAGLKQLRVLQL
CCCCCHHHHHHHHHH
46.507374133
85UbiquitinationKNDFAGLKQLRVLQL
CCCCCHHHHHHHHHH
46.50-
109UbiquitinationRGAFDDMKELERLRL
HCCCCCHHHHHHHCC
67.17-
160UbiquitinationFRGATDLKNLQLDKN
HCCCCCCCCCCCCHH
59.42-
166UbiquitinationLKNLQLDKNQISCIE
CCCCCCCHHHCHHHH
60.38-
192N-linked_GlycosylationVLTLNNNNITTIPVS
EEEECCCCEEEEECH
34.80UniProtKB CARBOHYD
298UbiquitinationGIVDCRGKGLTAIPA
CEEECCCCCCCEECC
31.25-
332PhosphorylationPPGAFSPYRKLRRID
CCCCCCHHHCEECCC
21.12-
406N-linked_GlycosylationDAFQDLQNLSLLSLY
HHHHHHHHHHHHHHH
38.60UniProtKB CARBOHYD
475AcetylationSPRRLANKRIGQIKS
CHHHHCCCCCCCCCC
39.5222361361
488PhosphorylationKSKKFRCSAKEQYFI
CCCCCCCCCCCCEEC
37.81-
493PhosphorylationRCSAKEQYFIPGTED
CCCCCCCEECCCCCC
12.45-
498O-linked_GlycosylationEQYFIPGTEDYQLNS
CCEECCCCCCCCCCC
21.96OGP
498PhosphorylationEQYFIPGTEDYQLNS
CCEECCCCCCCCCCC
21.96-
516UbiquitinationSDVVCPHKCRCEANV
CCCCCCCCCCEECCE
14.44-
533UbiquitinationCSSLKLTKIPERIPQ
ECCCEECCCCCCCCC
67.70-
553PhosphorylationRLNNNEISILEATGM
ECCCCEEEHHHHHCH
18.23-
565PhosphorylationTGMFKKLTHLKKINL
HCHHHHHHCCEECCC
33.76-
571N-linked_GlycosylationLTHLKKINLSNNKVS
HHCCEECCCCCCCCE
46.42UniProtKB CARBOHYD
630N-linked_GlycosylationNRISCIHNDSFTGLR
CEEEEEECCCCCCCC
27.06UniProtKB CARBOHYD
690UbiquitinationGGWLRKRKIVTGNPR
HHHHHCEEEECCCCC
44.56-
762N-linked_GlycosylationLPKGIPKNVTELYLD
CCCCCCCCCEEEEEC
40.36UniProtKB CARBOHYD
801N-linked_GlycosylationNKISSLSNSSFTNMS
CCCHHHCCCCCCCHH
47.14UniProtKB CARBOHYD
806N-linked_GlycosylationLSNSSFTNMSQLTTL
HCCCCCCCHHHHHHH
26.54UniProtKB CARBOHYD
882UbiquitinationRWLSSWVKTGYKEPG
HHHHHHHHHCCCCCC
29.94-
911UbiquitinationLLTTPAKKFECQGPP
EEECCCHHCCCCCCC
48.80-
1026N-linked_GlycosylationVCVDGVGNYTCQCPL
EEECCCCCEEEECCC
26.91UniProtKB CARBOHYD
1079N-linked_GlycosylationMPGYAGDNCSENQDD
CCCCCCCCCCCCCHH
30.23UniProtKB CARBOHYD
1175PhosphorylationVNFVDRDTYLQFTDL
CCEECCCCEEEEECC
27.3325599653
1189N-linked_GlycosylationLQNWPRANITLQVST
CCCCCCCCEEEEEEE
29.11UniProtKB CARBOHYD
1259N-linked_GlycosylationVAFDQMVNLSIDGGS
EEECCCCCEEECCCC
23.80UniProtKB CARBOHYD
1306N-linked_GlycosylationFRLWQILNGTGFHGC
HHHHHHHHCCCCCHH
47.84UniProtKB CARBOHYD

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 SLIT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLIT1_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 SLIT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SLIT1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLIT1_HUMAN

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Related Literatures of Post-Translational Modification

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