CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024027
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Roundabout homolog 1 
Protein Synonyms/Alias
 Deleted in U twenty twenty; H-Robo-1 
Gene Name
 ROBO1 
Gene Synonyms/Alias
 DUTT1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81PSDLIVSKGEPATLNubiquitination[1]
1055SNKINEMKTFNSPNLubiquitination[1, 2]
1063TFNSPNLKDGRFVNPubiquitination[1]
1110WKPLGQQKQEVAPVQubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development. 
Sequence Annotation
 DOMAIN 68 164 Ig-like C2-type 1.
 DOMAIN 170 257 Ig-like C2-type 2.
 DOMAIN 262 346 Ig-like C2-type 3.
 DOMAIN 351 446 Ig-like C2-type 4.
 DOMAIN 455 541 Ig-like C2-type 5.
 DOMAIN 561 646 Fibronectin type-III 1.
 DOMAIN 673 763 Fibronectin type-III 2.
 DOMAIN 775 864 Fibronectin type-III 3.
 MOD_RES 940 940 Phosphoserine.
 MOD_RES 1038 1038 Phosphotyrosine; by ABL; in vitro.
 MOD_RES 1055 1055 Phosphoserine.
 MOD_RES 1073 1073 Phosphotyrosine; by ABL; in vitro.
 MOD_RES 1114 1114 Phosphotyrosine; by ABL; in vitro.
 MOD_RES 1240 1240 Phosphothreonine.
 MOD_RES 1297 1297 Phosphoserine.
 CARBOHYD 160 160 N-linked (GlcNAc...) (Potential).
 CARBOHYD 463 463 N-linked (GlcNAc...) (Potential).
 CARBOHYD 790 790 N-linked (GlcNAc...) (Potential).
 CARBOHYD 820 820 N-linked (GlcNAc...) (Potential).
 CARBOHYD 827 827 N-linked (GlcNAc...) (Potential).
 DISULFID 89 147
 DISULFID 191 240 Potential.
 DISULFID 283 330 Potential.
 DISULFID 372 428 Potential.
 DISULFID 476 525 Potential.  
Keyword
 3D-structure; Alternative splicing; Chemotaxis; Complete proteome; Developmental protein; Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1651 AA 
Protein Sequence
MKWKHVPFLV MISLLSLSPN HLFLAQLIPD PEDVERGNDH GTPIPTSDND DNSLGYTGSR 60
LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE WYKGGERVET DKDDPRSHRM 120
LLPSGSLFFL RIVHGRKSRP DEGVYVCVAR NYLGEAVSHN ASLEVAILRD DFRQNPSDVM 180
VAVGEPAVME CQPPRGHPEP TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC 240
VGTNMVGERE SEVAELTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTVRWRKDDG 300
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP PHFVVKPRDQ 360
VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ SSSRFSVSQT GDLTITNVQR 420
SDVGYYICQT LNVAGSIITK AYLEVTDVIA DRPPPVIRQG PVNQTVAVDG TFVLSCVATG 480
SPVPTILWRK DGVLVSTQDS RIKQLENGVL QIRYAKLGDT GRYTCIASTP SGEATWSAYI 540
EVQGKVNEFG VPVQPPRPTD PNLIPSAPSK PEVTDVSRNT VTLSWQPNLN SGATPTSYII 600
EAFSHASGSS WQTVAENVKT ETSAIKGLKP NAIYLFLVRA ANAYGISDPS QISDPVKTQD 660
VLPTSQGVDH KQVQRELGNA VLHLHNPTVL SSSSIEVHWT VDQQSQYIQG YKILYRPSGA 720
NHGESDWLVF EVRTPAKNSV VIPDLRKGVN YEIKARPFFN EFQGADSEIK FAKTLEEAPS 780
APPQGVTVSK NDGNGTAILV SWQPPPEDTQ NGMVQEYKVW CLGNETRYHI NKTVDGSTFS 840
VVIPFLVPGI RYSVEVAAST GAGSGVKSEP QFIQLDAHGN PVSPEDQVSL AQQISDVVKQ 900
PAFIAGIGAA CWIILMVFSI WLYRHRKKRN GLTSTYAGIR KVPSFTFTPT VTYQRGGEAV 960
SSGGRPGLLN ISEPAAQPWL ADTWPNTGNN HNDCSISCCT AGNGNSDSNL TTYSRPADCI 1020
ANYNNQLDNK QTNLMLPEST VYGDVDLSNK INEMKTFNSP NLKDGRFVNP SGQPTPYATT 1080
QLIQSNLSNN MNNGSGDSGE KHWKPLGQQK QEVAPVQYNI VEQNKLNKDY RANDTVPPTI 1140
PYNQSYDQNT GGSYNSSDRG SSTSGSQGHK KGARTPKVPK QGGMNWADLL PPPPAHPPPH 1200
SNSEEYNISV DESYDQEMPC PVPPARMYLQ QDELEEEEDE RGPTPPVRGA ASSPAAVSYS 1260
HQSTATLTPS PQEELQPMLQ DCPEETGHMQ HQPDRRRQPV SPPPPPRPIS PPHTYGYISG 1320
PLVSDMDTDA PEEEEDEADM EVAKMQTRRL LLRGLEQTPA SSVGDLESSV TGSMINGWGS 1380
ASEEDNISSG RSSVSSSDGS FFTDADFAQA VAAAAEYAGL KVARRQMQDA AGRRHFHASQ 1440
CPRPTSPVST DSNMSAAVMQ KTRPAKKLKH QPGHLRRETY TDDLPPPPVP PPAIKSPTAQ 1500
SKTQLEVRPV VVPKLPSMDA RTDRSSDRKG SSYKGREVLD GRQVVDMRTN PGDPREAQEQ 1560
QNDGKGRGNK AAKRDLPPAK THLIQEDILP YCRPTFPTSN NPRDPSSSSS MSSRGSGSRQ 1620
REQANVGRRN IAEMQVLGGY ERGEDNNEEL EETES 1655 
Gene Ontology
 GO:0030673; C:axolemma; IEA:Compara.
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0008046; F:axon guidance receptor activity; TAS:ProtInc.
 GO:0042802; F:identical protein binding; IDA:UniProtKB.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
 GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
 GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
 GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; IDA:UniProtKB.
 GO:0007156; P:homophilic cell adhesion; IDA:UniProtKB.
 GO:0060763; P:mammary duct terminal end bud growth; IEA:Compara.
 GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
 GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:BHF-UCL.
 GO:0050925; P:negative regulation of negative chemotaxis; IDA:UniProtKB.
 GO:0050772; P:positive regulation of axonogenesis; IDA:UniProtKB.
 GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR013098; Ig_I-set.
 IPR003598; Ig_sub2.
 IPR003596; Ig_V-set_subgr. 
Pfam
 PF00041; fn3
 PF07679; I-set 
SMART
 SM00060; FN3
 SM00408; IGc2
 SM00406; IGv 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE 
PRINTS