CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001466
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Slit homolog 2 protein 
Protein Synonyms/Alias
 Slit-2; Slit homolog 2 protein N-product; Slit homolog 2 protein C-product 
Gene Name
 SLIT2 
Gene Synonyms/Alias
 SLIL3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
72NNITRITKTDFAGLRubiquitination[1]
289NIVDCRGKGLTEIPTubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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. 
Sequence Annotation
 DOMAIN 31 55 LRRNT.
 REPEAT 56 77 LRR 1.
 REPEAT 80 101 LRR 2.
 REPEAT 104 125 LRR 3.
 REPEAT 128 149 LRR 4.
 REPEAT 152 173 LRR 5.
 REPEAT 176 197 LRR 6.
 DOMAIN 209 259 LRRCT 1.
 DOMAIN 264 300 LRRNT 2.
 REPEAT 301 322 LRR 7.
 REPEAT 325 346 LRR 8.
 REPEAT 349 370 LRR 9.
 REPEAT 373 394 LRR 10.
 REPEAT 397 418 LRR 11.
 DOMAIN 430 480 LRRCT 2.
 DOMAIN 497 533 LRRNT 3.
 REPEAT 534 555 LRR 12.
 REPEAT 559 580 LRR 13.
 REPEAT 583 604 LRR 14.
 REPEAT 607 628 LRR 15.
 REPEAT 631 652 LRR 16.
 DOMAIN 664 714 LRRCT 3.
 DOMAIN 718 754 LRRNT 4.
 REPEAT 755 777 LRR 17.
 REPEAT 778 799 LRR 18.
 REPEAT 802 823 LRR 19.
 REPEAT 826 847 LRR 20.
 DOMAIN 859 909 LRRCT 4.
 DOMAIN 918 955 EGF-like 1.
 DOMAIN 957 996 EGF-like 2.
 DOMAIN 998 1034 EGF-like 3; calcium-binding (Potential).
 DOMAIN 1036 1074 EGF-like 4.
 DOMAIN 1076 1112 EGF-like 5; calcium-binding (Potential).
 DOMAIN 1121 1157 EGF-like 6.
 DOMAIN 1160 1333 Laminin G-like.
 DOMAIN 1332 1368 EGF-like 7.
 DOMAIN 1453 1528 CTCK.
 CARBOHYD 66 66 N-linked (GlcNAc...) (Potential).
 CARBOHYD 186 186 N-linked (GlcNAc...) (Potential).
 CARBOHYD 564 564 N-linked (GlcNAc...) (Potential).
 CARBOHYD 623 623 N-linked (GlcNAc...).
 CARBOHYD 794 794 N-linked (GlcNAc...) (Potential).
 CARBOHYD 799 799 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1009 1009 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1010 1010 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1019 1019 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1183 1183 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1266 1266 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1300 1300 N-linked (GlcNAc...) (Potential).
 DISULFID 277 286
 DISULFID 434 457
 DISULFID 436 478
 DISULFID 506 512
 DISULFID 510 519
 DISULFID 668 691
 DISULFID 670 712
 DISULFID 727 733
 DISULFID 731 740
 DISULFID 863 886
 DISULFID 865 907
 DISULFID 922 933 By similarity.
 DISULFID 927 943 By similarity.
 DISULFID 945 954 By similarity.
 DISULFID 961 972 By similarity.
 DISULFID 966 984 By similarity.
 DISULFID 986 995 By similarity.
 DISULFID 1002 1013 By similarity.
 DISULFID 1007 1022 By similarity.
 DISULFID 1024 1033 By similarity.
 DISULFID 1040 1053 By similarity.
 DISULFID 1047 1062 By similarity.
 DISULFID 1064 1073 By similarity.
 DISULFID 1080 1091 By similarity.
 DISULFID 1085 1100 By similarity.
 DISULFID 1102 1111 By similarity.
 DISULFID 1125 1136 By similarity.
 DISULFID 1130 1145 By similarity.
 DISULFID 1147 1156 By similarity.
 DISULFID 1307 1333 By similarity.
 DISULFID 1336 1346 By similarity.
 DISULFID 1341 1356 By similarity.
 DISULFID 1358 1367 By similarity.
 DISULFID 1375 1385 By similarity.
 DISULFID 1380 1395 By similarity.
 DISULFID 1397 1406 By similarity.
 DISULFID 1416 1426 By similarity.
 DISULFID 1421 1436 By similarity.
 DISULFID 1438 1447 By similarity.
 DISULFID 1453 1492 By similarity.
 DISULFID 1471 1506 By similarity.
 DISULFID 1482 1522 By similarity.
 DISULFID 1486 1524 By similarity.  
Keyword
 3D-structure; Alternative splicing; Chemotaxis; Complete proteome; Developmental protein; Differentiation; Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein; Heparin-binding; Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1529 AA 
Protein Sequence
MRGVGWQMLS LSLGLVLAIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP RNIPRNTERL 60
DLNGNNITRI TKTDFAGLRH LRVLQLMENK ISTIERGAFQ DLKELERLRL NRNHLQLFPE 120
LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA VDIKNLQLDY NQISCIEDGA FRALRDLEVL 180
TLNNNNITRL SVASFNHMPK LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS 240
HLRGHNVAEV QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE 300
TITEIRLEQN TIKVIPPGAF SPYKKLRRID LSNNQISELA PDAFQGLRSL NSLVLYGNKI 360
TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL LSLYDNKLQT IAKGTFSPLR 420
AIQTMHLAQN PFICDCHLKW LADYLHTNPI ETSGARCTSP RRLANKRIGQ IKSKKFRCSA 480
KEQYFIPGTE DYRSKLSGDC FADLACPEKC RCEGTTVDCS NQKLNKIPEH IPQYTAELRL 540
NNNEFTVLEA TGIFKKLPQL RKINFSNNKI TDIEEGAFEG ASGVNEILLT SNRLENVQHK 600
MFKGLESLKT LMLRSNRITC VGNDSFIGLS SVRLLSLYDN QITTVAPGAF DTLHSLSTLN 660
LLANPFNCNC YLAWLGEWLR KKRIVTGNPR CQKPYFLKEI PIQDVAIQDF TCDDGNDDNS 720
CSPLSRCPTE CTCLDTVVRC SNKGLKVLPK GIPRDVTELY LDGNQFTLVP KELSNYKHLT 780
LIDLSNNRIS TLSNQSFSNM TQLLTLILSY NRLRCIPPRT FDGLKSLRLL SLHGNDISVV 840
PEGAFNDLSA LSHLAIGANP LYCDCNMQWL SDWVKSEYKE PGIARCAGPG EMADKLLLTT 900
PSKKFTCQGP VDVNILAKCN PCLSNPCKND GTCNSDPVDF YRCTCPYGFK GQDCDVPIHA 960
CISNPCKHGG TCHLKEGEED GFWCICADGF EGENCEVNVD DCEDNDCENN STCVDGINNY 1020
TCLCPPEYTG ELCEEKLDFC AQDLNPCQHD SKCILTPKGF KCDCTPGYVG EHCDIDFDDC 1080
QDNKCKNGAH CTDAVNGYTC ICPEGYSGLF CEFSPPMVLP RTSPCDNFDC QNGAQCIVRI 1140
NEPICQCLPG YQGEKCEKLV SVNFINKESY LQIPSAKVRP QTNITLQIAT DEDSGILLYK 1200
GDKDHIAVEL YRGRVRASYD TGSHPASAIY SVETINDGNF HIVELLALDQ SLSLSVDGGN 1260
PKIITNLSKQ STLNFDSPLY VGGMPGKSNV ASLRQAPGQN GTSFHGCIRN LYINSELQDF 1320
QKVPMQTGIL PGCEPCHKKV CAHGTCQPSS QAGFTCECQE GWMGPLCDQR TNDPCLGNKC 1380
VHGTCLPINA FSYSCKCLEG HGGVLCDEEE DLFNPCQAIK CKHGKCRLSG LGQPYCECSS 1440
GYTGDSCDRE ISCRGERIRD YYQKQQGYAA CQTTKKVSRL ECRGGCAGGQ CCGPLRSKRR 1500
KYSFECTDGS SFVDEVEKVV KCGCTRCVS 1529 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0045499; F:chemorepellent activity; IEA:Compara.
 GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
 GO:0008201; F:heparin binding; IDA:UniProtKB.
 GO:0043237; F:laminin-1 binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
 GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
 GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:UniProtKB.
 GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
 GO:0016337; P:cell-cell adhesion; IEA:Compara.
 GO:0071504; P:cellular response to heparin; IDA:UniProtKB.
 GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
 GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; IDA:UniProtKB.
 GO:0021972; P:corticospinal neuron axon guidance through spinal cord; IMP:BHF-UCL.
 GO:0033563; P:dorsal/ventral axon guidance; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0050929; P:induction of negative chemotaxis; IDA:UniProtKB.
 GO:0060763; P:mammary duct terminal end bud growth; IEA:Compara.
 GO:0001656; P:metanephros development; IEA:Compara.
 GO:0008045; P:motor neuron axon guidance; IDA:UniProtKB.
 GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0090288; P:negative regulation of cellular response to growth factor stimulus; IDA:BHF-UCL.
 GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
 GO:0010596; P:negative regulation of endothelial cell migration; IDA:UniProtKB.
 GO:0010629; P:negative regulation of gene expression; IEA:Compara.
 GO:0010593; P:negative regulation of lamellipodium assembly; IDA:UniProtKB.
 GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:BHF-UCL.
 GO:0071676; P:negative regulation of mononuclear cell migration; IDA:BHF-UCL.
 GO:0090024; P:negative regulation of neutrophil chemotaxis; IDA:UniProtKB.
 GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
 GO:0090260; P:negative regulation of retinal ganglion cell axon guidance; IDA:UniProtKB.
 GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IDA:UniProtKB.
 GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IDA:BHF-UCL.
 GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO:0050772; P:positive regulation of axonogenesis; TAS:UniProtKB.
 GO:0051414; P:response to cortisol stimulus; IEP:UniProtKB.
 GO:0031290; P:retinal ganglion cell axon guidance; IDA:UniProtKB.
 GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
 GO:0001657; P:ureteric bud development; IMP:UniProtKB. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR000483; Cys-rich_flank_reg_C.
 IPR006207; Cys_knot_C.
 IPR000742; EG-like_dom.
 IPR001881; EGF-like_Ca-bd.
 IPR013032; EGF-like_CS.
 IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 IPR018097; EGF_Ca-bd_CS.
 IPR003645; Fol_N.
 IPR001791; Laminin_G.
 IPR001611; Leu-rich_rpt.
 IPR003591; Leu-rich_rpt_typical-subtyp.
 IPR000372; LRR-contain_N. 
Pfam
 PF00008; EGF
 PF02210; Laminin_G_2
 PF00560; LRR_1
 PF01463; LRRCT
 PF01462; LRRNT 
SMART
 SM00041; CT
 SM00181; EGF
 SM00179; EGF_CA
 SM00274; FOLN
 SM00282; LamG
 SM00369; LRR_TYP
 SM00082; LRRCT
 SM00013; LRRNT 
PROSITE
 PS00010; ASX_HYDROXYL
 PS01185; CTCK_1
 PS01225; CTCK_2
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS50025; LAM_G_DOMAIN
 PS51450; LRR 
PRINTS