SLIT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLIT2_HUMAN
• UniProt AC: O94813
• Protein Name: Slit homolog 2 protein
• Gene Name: SLIT2
• Organism: Homo sapiens (Human).
• Sequence Length: 1529
• Subcellular Localization: Secreted . The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.
• 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. SLIT1 and SLIT2 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. In spinal chord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration..
• Protein Sequence: MRGVGWQMLSLSLGLVLAILNKVAPQACPAQCSCSGSTVDCHGLALRSVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRVLQLMENKISTIERGAFQDLKELERLRLNRNHLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSGHQSFMAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNTIKVIPPGAFSPYKKLRRIDLSNNQISELAPDAFQGLRSLNSLVLYGNKITELPKSLFEGLFSLQLLLLNANKINCLRVDAFQDLHNLNLLSLYDNKLQTIAKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYRSKLSGDCFADLACPEKCRCEGTTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPTECTCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNSDPVDFYRCTCPYGFKGQDCDVPIHACISNPCKHGGTCHLKEGEEDGFWCICADGFEGENCEVNVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQDLNPCQHDSKCILTPKGFKCDCTPGYVGEHCDIDFDDCQDNKCKNGAHCTDAVNGYTCICPEGYSGLFCEFSPPMVLPRTSPCDNFDCQNGAQCIVRINEPICQCLPGYQGEKCEKLVSVNFINKESYLQIPSAKVRPQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPGKSNVASLRQAPGQNGTSFHGCIRNLYINSELQDFQKVPMQTGILPGCEPCHKKVCAHGTCQPSSQAGFTCECQEGWMGPLCDQRTNDPCLGNKCVHGTCLPINAFSYSCKCLEGHGGVLCDEEEDLFNPCQAIKCKHGKCRLSGLGQPYCECSSGYTGDSCDREISCRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGCTRCVS

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
66	N-linked_Glycosylation	RLDLNGNNITRITKT CCCCCCCCCEEEECC	38.11	UniProtKB CARBOHYD
72	Ubiquitination	NNITRITKTDFAGLR CCCEEEECCCCCCHH	43.66	-
135	Phosphorylation	KLYRLDLSENQIQAI EEEECCCCHHHHHHC	33.88	-
186	N-linked_Glycosylation	VLTLNNNNITRLSVA EEEECCCCCEEEEEE	38.85	UniProtKB CARBOHYD
289	Ubiquitination	NIVDCRGKGLTEIPT CEEECCCCCCCCCCC	31.25	-
292	Phosphorylation	DCRGKGLTEIPTNLP ECCCCCCCCCCCCCC	40.30	26552605
296	Phosphorylation	KGLTEIPTNLPETIT CCCCCCCCCCCCCCE	55.86	26552605
301	Phosphorylation	IPTNLPETITEIRLE CCCCCCCCCEEEEEE	31.12	26552605
303	Phosphorylation	TNLPETITEIRLEQN CCCCCCCEEEEEECC	32.55	26552605
444	Phosphorylation	HLKWLADYLHTNPIE HHHHHHHHHCCCCCC	8.52	28258704
447	Phosphorylation	WLADYLHTNPIETSG HHHHHHCCCCCCCCC	39.84	28258704
458	Phosphorylation	ETSGARCTSPRRLAN CCCCCCCCCHHHHCC	35.89	22468782
459	Phosphorylation	TSGARCTSPRRLANK CCCCCCCCHHHHCCC	21.75	22468782
466	Acetylation	SPRRLANKRIGQIKS CHHHHCCCCCCCCCC	39.52	22361377
479	Phosphorylation	KSKKFRCSAKEQYFI CCCCCCCCCCCCEEC	37.81	-
484	Phosphorylation	RCSAKEQYFIPGTED CCCCCCCEECCCCHH	12.45	-
489	Phosphorylation	EQYFIPGTEDYRSKL CCEECCCCHHHHHHH	21.96	-
492	Phosphorylation	FIPGTEDYRSKLSGD ECCCCHHHHHHHCCC	15.56	-
563	Phosphorylation	KLPQLRKINFSNNKI HCCHHEECCCCCCCC	5.21	32142685
564	N-linked_Glycosylation	LPQLRKINFSNNKIT CCHHEECCCCCCCCE	37.01	UniProtKB CARBOHYD
567	Phosphorylation	LRKINFSNNKITDIE HEECCCCCCCCEECC	50.07	32142685
571	Phosphorylation	NFSNNKITDIEEGAF CCCCCCCEECCCCCC	32.31	32142685
574	Phosphorylation	NNKITDIEEGAFEGA CCCCEECCCCCCCCC	53.86	32142685
578	Phosphorylation	TDIEEGAFEGASGVN EECCCCCCCCCCCHH	15.19	32142685
582	Phosphorylation	EGAFEGASGVNEILL CCCCCCCCCHHHHHH	54.88	32142685
586	Phosphorylation	EGASGVNEILLTSNR CCCCCHHHHHHCCCC	32.38	32142685
590	Phosphorylation	GVNEILLTSNRLENV CHHHHHHCCCCHHHH	22.10	32142685
607	Phosphorylation	KMFKGLESLKTLMLR HHHCCHHHHHHHHHH	39.96	27135362
615	Phosphorylation	LKTLMLRSNRITCVG HHHHHHHCCCEEEEC	26.88	27135362
623	N-linked_Glycosylation	NRITCVGNDSFIGLS CCEEEECCCCEECCC	22.74	UniProtKB CARBOHYD
630	Phosphorylation	NDSFIGLSSVRLLSL CCCEECCCCEEEEEC	22.90	24719451
757	Phosphorylation	KGIPRDVTELYLDGN CCCCCCCEEEEECCC	25.27	27067055
760	Phosphorylation	PRDVTELYLDGNQFT CCCCEEEEECCCEEE	9.12	27067055
794	N-linked_Glycosylation	NRISTLSNQSFSNMT CCEEHHCCCCCCHHH	44.63	UniProtKB CARBOHYD
799	N-linked_Glycosylation	LSNQSFSNMTQLLTL HCCCCCCHHHHHHHH	35.19	UniProtKB CARBOHYD
899	Phosphorylation	MADKLLLTTPSKKFT HHHHEEECCCCCCEE	36.31	23403867
900	Phosphorylation	ADKLLLTTPSKKFTC HHHEEECCCCCCEEC	26.07	23403867
1009	N-linked_Glycosylation	CEDNDCENNSTCVDG CCCCCCCCCCCCEEC	54.83	UniProtKB CARBOHYD
1010	N-linked_Glycosylation	EDNDCENNSTCVDGI CCCCCCCCCCCEECC	19.19	UniProtKB CARBOHYD
1019	N-linked_Glycosylation	TCVDGINNYTCLCPP CCEECCCCEEEECCH	31.41	UniProtKB CARBOHYD
1051	Phosphorylation	LNPCQHDSKCILTPK CCCCCCCCCEEECCC	27.57	22468782
1056	Phosphorylation	HDSKCILTPKGFKCD CCCCEEECCCCEECC	11.75	22468782
1175	Phosphorylation	ESYLQIPSAKVRPQT CCEEECCCCEECCCC	42.21	24719451
1183	N-linked_Glycosylation	AKVRPQTNITLQIAT CEECCCCCEEEEEEE	21.72	UniProtKB CARBOHYD
1265	Phosphorylation	GGNPKIITNLSKQST CCCCCEEECCCCCCC	33.31	29759185
1266	N-linked_Glycosylation	GNPKIITNLSKQSTL CCCCEEECCCCCCCC	31.73	UniProtKB CARBOHYD
1300	N-linked_Glycosylation	LRQAPGQNGTSFHGC HHCCCCCCCCCHHHH	62.72	UniProtKB CARBOHYD
1349	Phosphorylation	AHGTCQPSSQAGFTC CCCCCCCCCCCCEEE	14.81	22210691
1350	Phosphorylation	HGTCQPSSQAGFTCE CCCCCCCCCCCEEEE	30.63	22210691
1452	Phosphorylation	DSCDREISCRGERIR CCCCCEEEECCHHHH	7.94	28509920
1478	Phosphorylation	CQTTKKVSRLECRGG CCCCCCEEEEECCCC	39.77	24719451
1497	Phosphorylation	QCCGPLRSKRRKYSF CCCCCCCCCCCCEEE	37.89	24719451
1510	Phosphorylation	SFECTDGSSFVDEVE EEECCCCCCHHHHHH	24.34	-

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

Oops, there are no upstream regulatory protein records of SLIT2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SLIT2_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 SLIT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GPC1_HUMAN	GPC1	physical	11375980
LUM_HUMAN	LUM	physical	27173435
RSRC1_HUMAN	RSRC1	physical	27173435
EXOS9_HUMAN	EXOSC9	physical	27173435
EXOS7_HUMAN	EXOSC7	physical	27173435
EXOS2_HUMAN	EXOSC2	physical	27173435
EXOS4_HUMAN	EXOSC4	physical	27173435
LRC47_HUMAN	LRRC47	physical	27173435

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.