CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001106
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Slit homolog 1 protein 
Protein Synonyms/Alias
 Slit-1; Multiple epidermal growth factor-like domains protein 4; Multiple EGF-like domains protein 4 
Gene Name
 SLIT1 
Gene Synonyms/Alias
 KIAA0813; MEGF4; SLIL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78NNITRIHKNDFAGLKubiquitination[1]
85KNDFAGLKQLRVLQLubiquitination[1]
109RGAFDDMKELERLRLubiquitination[1]
166LKNLQLDKNQISCIEubiquitination[1]
298GIVDCRGKGLTAIPAubiquitination[1]
516SDVVCPHKCRCEANVubiquitination[1]
533CSSLKLTKIPERIPQubiquitination[1]
882RWLSSWVKTGYKEPGubiquitination[1]
911LLTTPAKKFECQGPPubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
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 (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. 
Sequence Annotation
 DOMAIN 34 61 LRRNT.
 REPEAT 62 83 LRR 1.
 REPEAT 86 107 LRR 2.
 REPEAT 110 131 LRR 3.
 REPEAT 134 155 LRR 4.
 REPEAT 158 179 LRR 5.
 REPEAT 182 203 LRR 6.
 DOMAIN 215 265 LRRCT 1.
 DOMAIN 273 309 LRRNT 2.
 REPEAT 310 331 LRR 7.
 REPEAT 334 355 LRR 8.
 REPEAT 358 379 LRR 9.
 REPEAT 382 403 LRR 10.
 REPEAT 406 427 LRR 11.
 DOMAIN 439 489 LRRCT 2.
 DOMAIN 504 540 LRRNT 3.
 REPEAT 541 562 LRR 12.
 REPEAT 566 587 LRR 13.
 REPEAT 590 611 LRR 14.
 REPEAT 614 635 LRR 15.
 REPEAT 638 659 LRR 16.
 DOMAIN 671 721 LRRCT 3.
 DOMAIN 725 761 LRRNT 4.
 REPEAT 762 783 LRR 17.
 REPEAT 785 806 LRR 18.
 REPEAT 809 830 LRR 19.
 REPEAT 833 854 LRR 20.
 DOMAIN 866 916 LRRCT 4.
 DOMAIN 927 962 EGF-like 1.
 DOMAIN 964 1003 EGF-like 2.
 DOMAIN 1005 1041 EGF-like 3.
 DOMAIN 1043 1081 EGF-like 4.
 DOMAIN 1083 1119 EGF-like 5.
 DOMAIN 1127 1163 EGF-like 6.
 DOMAIN 1166 1339 Laminin G-like.
 DOMAIN 1340 1374 EGF-like 7.
 DOMAIN 1377 1413 EGF-like 8.
 DOMAIN 1418 1454 EGF-like 9.
 DOMAIN 1459 1534 CTCK.
 CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
 CARBOHYD 192 192 N-linked (GlcNAc...) (Potential).
 CARBOHYD 406 406 N-linked (GlcNAc...) (Potential).
 CARBOHYD 571 571 N-linked (GlcNAc...) (Potential).
 CARBOHYD 630 630 N-linked (GlcNAc...) (Potential).
 CARBOHYD 762 762 N-linked (GlcNAc...) (Potential).
 CARBOHYD 801 801 N-linked (GlcNAc...) (Potential).
 CARBOHYD 806 806 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1026 1026 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1079 1079 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1189 1189 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1259 1259 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1306 1306 N-linked (GlcNAc...) (Potential).
 DISULFID 286 295 By similarity.
 DISULFID 443 466 By similarity.
 DISULFID 445 487 By similarity.
 DISULFID 513 519 By similarity.
 DISULFID 517 526 By similarity.
 DISULFID 675 698 By similarity.
 DISULFID 677 719 By similarity.
 DISULFID 929 940 By similarity.
 DISULFID 934 950 By similarity.
 DISULFID 952 961 By similarity.
 DISULFID 968 979 By similarity.
 DISULFID 973 991 By similarity.
 DISULFID 993 1002 By similarity.
 DISULFID 1009 1020 By similarity.
 DISULFID 1014 1029 By similarity.
 DISULFID 1031 1040 By similarity.
 DISULFID 1047 1060 By similarity.
 DISULFID 1054 1069 By similarity.
 DISULFID 1071 1080 By similarity.
 DISULFID 1087 1098 By similarity.
 DISULFID 1092 1107 By similarity.
 DISULFID 1109 1118 By similarity.
 DISULFID 1131 1142 By similarity.
 DISULFID 1136 1151 By similarity.
 DISULFID 1153 1162 By similarity.
 DISULFID 1313 1339 By similarity.
 DISULFID 1342 1352 By similarity.
 DISULFID 1347 1362 By similarity.
 DISULFID 1364 1373 By similarity.
 DISULFID 1381 1391 By similarity.
 DISULFID 1386 1401 By similarity.
 DISULFID 1403 1412 By similarity.
 DISULFID 1422 1432 By similarity.
 DISULFID 1427 1442 By similarity.
 DISULFID 1444 1453 By similarity.
 DISULFID 1459 1498 By similarity.
 DISULFID 1477 1512 By similarity.
 DISULFID 1488 1528 By similarity.
 DISULFID 1492 1530 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Developmental protein; Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1534 AA 
Protein Sequence
MALTPGWGSS AGPVRPELWL LLWAAAWRLG ASACPALCTC TGTTVDCHGT GLQAIPKNIP 60
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ 120
LHMLPELLFQ NNQALSRLDL SENAIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL 180
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT 240
QCSGPASLRG LNVAEVQKSE FSCSGQGEAG RVPTCTLSSG SCPAMCTCSN GIVDCRGKGL 300
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN 360
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL 420
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI 480
KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ANVVECSSLK LTKIPERIPQ 540
STAELRLNNN EISILEATGM FKKLTHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ 600
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIT TVSPGAFDTL 660
QSLSTLNLLA NPFNCNCQLA WLGGWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE 720
EGQEEGGCLP RPQCPQECAC LDTVVRCSNK HLRALPKGIP KNVTELYLDG NQFTLVPGQL 780
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH 840
GNDISTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPQDME 900
GKLLLTTPAK KFECQGPPTL AVQAKCDLCL SSPCQNQGTC HNDPLEVYRC ACPSGYKGRD 960
CEVSLDSCSS GPCENGGTCH AQEGEDAPFT CSCPTGFEGP TCGVNTDDCV DHACANGGVC 1020
VDGVGNYTCQ CPLQYEGKAC EQLVDLCSPD LNPCQHEAQC VGTPDGPRCE CMPGYAGDNC 1080
SENQDDCRDH RCQNGAQCMD EVNSYSCLCA EGYSGQLCEI PPHLPAPKSP CEGTECQNGA 1140
NCVDQGNRPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN 1200
GILLYNGDND HIAVELYQGH VRVSYDPGSY PSSAIYSAET INDGQFHTVE LVAFDQMVNL 1260
SIDGGSPMTM DNFGKHYTLN SEAPLYVGGM PVDVNSAAFR LWQILNGTGF HGCIRNLYIN 1320
NELQDFTKTQ MKPGVVPGCE PCRKLYCLHG ICQPNATPGP MCHCEAGWVG LHCDQPADGP 1380
CHGHKCVHGQ CVPLDALSYS CQCQDGYSGA LCNQAGALAE PCRGLQCLHG HCQASGTKGA 1440
HCVCDPGFSG ELCEQESECR GDPVRDFHQV QRGYAICQTT RPLSWVECRG SCPGQGCCQG 1500
LRLKRRKFTF ECSDGTSFAE EVEKPTKCGC ALCA 1534 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005615; C:extracellular space; NAS:UniProtKB.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
 GO:0033563; P:dorsal/ventral axon guidance; IEA:Compara.
 GO:0040023; P:establishment of nucleus localization; IEA:Compara.
 GO:0048853; P:forebrain morphogenesis; NAS:UniProtKB.
 GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
 GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
 GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Compara.
 GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
 GO:0031290; P:retinal ganglion cell axon guidance; IEA:Compara.
 GO:0021510; P:spinal cord development; IEA:Compara.
 GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Compara. 
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.
 IPR025875; Leu-rich_rpt_4.
 IPR003591; Leu-rich_rpt_typical-subtyp.
 IPR000372; LRR-contain_N. 
Pfam
 PF00008; EGF
 PF12661; hEGF
 PF02210; Laminin_G_2
 PF00560; LRR_1
 PF12799; LRR_4
 PF01463; LRRCT
 PF01462; LRRNT 
SMART
 SM00041; CT
 SM00181; EGF
 SM00179; EGF_CA
 SM00274; FOLN
 SM00282; LamG
 SM00369; LRR_TYP
 SM00082; LRRCT
 SM00013; LRRNT 
PROSITE
 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