CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018833
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neuronal cell adhesion molecule 
Protein Synonyms/Alias
 Nr-CAM; Neuronal surface protein Bravo; hBravo; NgCAM-related cell adhesion molecule; Ng-CAM-related 
Gene Name
 NRCAM 
Gene Synonyms/Alias
 KIAA0343 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
98KDPLVTMKPGTGTLIubiquitination[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
 Cell adhesion, ankyrin-binding protein involved in neuron-neuron adhesion. May play a role in the molecular assembly of the nodes of Ranvier (By similarity). 
Sequence Annotation
 DOMAIN 46 134 Ig-like 1.
 DOMAIN 141 235 Ig-like 2.
 DOMAIN 267 356 Ig-like 3.
 DOMAIN 361 448 Ig-like 4.
 DOMAIN 454 541 Ig-like 5.
 DOMAIN 545 632 Ig-like 6.
 DOMAIN 647 739 Fibronectin type-III 1.
 DOMAIN 746 840 Fibronectin type-III 2.
 DOMAIN 845 947 Fibronectin type-III 3.
 DOMAIN 952 1046 Fibronectin type-III 4.
 DOMAIN 1061 1153 Fibronectin type-III 5.
 MOD_RES 427 427 Phosphoserine (By similarity).
 MOD_RES 1226 1226 Phosphoserine (By similarity).
 MOD_RES 1271 1271 Phosphoserine (By similarity).
 MOD_RES 1295 1295 Phosphoserine (By similarity).
 CARBOHYD 83 83 N-linked (GlcNAc...) (Potential).
 CARBOHYD 223 223 N-linked (GlcNAc...) (Potential).
 CARBOHYD 245 245 N-linked (GlcNAc...) (Potential).
 CARBOHYD 251 251 N-linked (GlcNAc...) (Potential).
 CARBOHYD 276 276 N-linked (GlcNAc...).
 CARBOHYD 314 314 N-linked (GlcNAc...) (Potential).
 CARBOHYD 433 433 N-linked (GlcNAc...) (Potential).
 CARBOHYD 507 507 N-linked (GlcNAc...) (Potential).
 CARBOHYD 619 619 N-linked (GlcNAc...) (Potential).
 CARBOHYD 716 716 N-linked (GlcNAc...) (Potential).
 CARBOHYD 802 802 N-linked (GlcNAc...) (Potential).
 CARBOHYD 858 858 N-linked (GlcNAc...) (Potential).
 CARBOHYD 993 993 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1009 1009 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1019 1019 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1072 1072 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1083 1083 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1115 1115 N-linked (GlcNAc...) (Potential).
 DISULFID 68 123 Potential.
 DISULFID 167 218 Potential.
 DISULFID 292 340 Potential.
 DISULFID 382 432 Potential.
 DISULFID 476 525 Potential.
 DISULFID 567 616 Potential.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1304 AA 
Protein Sequence
MQLKIMPKKK RLSAGRVPLI LFLCQMISAL EVPLDPKLLE DLVQPPTITQ QSPKDYIIDP 60
RENIVIQCEA KGKPPPSFSW TRNGTHFDID KDPLVTMKPG TGTLIINIMS EGKAETYEGV 120
YQCTARNERG AAVSNNIVVR PSRSPLWTKE KLEPITLQSG QSLVLPCRPP IGLPPPIIFW 180
MDNSFQRLPQ SERVSQGLNG DLYFSNVLPE DTREDYICYA RFNHTQTIQQ KQPISVKVIS 240
VDELNDTIAA NLSDTEFYGA KSSRERPPTF LTPEGNASNK EELRGNVLSL ECIAEGLPTP 300
IIYWAKEDGM LPKNRTVYKN FEKTLQIIHV SEADSGNYQC IAKNALGAIH HTISVRVKAA 360
PYWITAPQNL VLSPGEDGTL ICRANGNPKP RISWLTNGVP IEIAPDDPSR KIDGDTIIFS 420
NVQERSSAVY QCNASNEYGY LLANAFVNVL AEPPRILTPA NTLYQVIANR PALLDCAFFG 480
SPLPTIEWFK GAKGSALHED IYVLHENGTL EIPVAQKDST GTYTCVARNK LGMAKNEVHL 540
EIKDPTWIVK QPEYAVVQRG SMVSFECKVK HDHTLSLTVL WLKDNRELPS DERFTVDKDH 600
LVVADVSDDD SGTYTCVANT TLDSVSASAV LSVVAPTPTP APVYDVPNPP FDLELTDQLD 660
KSVQLSWTPG DDNNSPITKF IIEYEDAMHK PGLWHHQTEV SGTQTTAQLK LSPYVNYSFR 720
VMAVNSIGKS LPSEASEQYL TKASEPDKNP TAVEGLGSEP DNLVITWKPL NGFESNGPGL 780
QYKVSWRQKD GDDEWTSVVV ANVSKYIVSG TPTFVPYLIK VQALNDMGFA PEPAVVMGHS 840
GEDLPMVAPG NVRVNVVNST LAEVHWDPVP LKSIRGHLQG YRIYYWKTQS SSKRNRRHIE 900
KKILTFQGSK THGMLPGLEP FSHYTLNVRV VNGKGEGPAS PDRVFNTPEG VPSAPSSLKI 960
VNPTLDSLTL EWDPPSHPNG ILTEYTLKYQ PINSTHELGP LVDLKIPANK TRWTLKNLNF 1020
STRYKFYFYA QTSAGSGSQI TEEAVTTVDE AGILPPDVGA GKVQAVNPRI SNLTAAAAET 1080
YANISWEYEG PEHVNFYVEY GVAGSKEEWR KEIVNGSRSF FGLKGLMPGT AYKVRVGAVG 1140
DSGFVSSEDV FETGPAMASR QVDIATQGWF IGLMCAVALL ILILLIVCFI RRNKGGKYPV 1200
KEKEDAHADP EIQPMKEDDG TFGEYSDAED HKPLKKGSRT PSDRTVKKED SDDSLVDYGE 1260
GVNGQFNEDG SFIGQYSGKK EKEPAEGNES SEAPSPVNAM NSFV 1304 
Gene Ontology
 GO:0043194; C:axon initial segment; ISS:BHF-UCL.
 GO:0009897; C:external side of plasma membrane; NAS:UniProtKB.
 GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0030506; F:ankyrin binding; IDA:UniProtKB.
 GO:0001525; P:angiogenesis; IEP:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007413; P:axonal fasciculation; NAS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
 GO:0007417; P:central nervous system development; NAS:UniProtKB.
 GO:0045162; P:clustering of voltage-gated sodium channels; IDA:UniProtKB.
 GO:0001764; P:neuron migration; NAS:UniProtKB.
 GO:0019227; P:neuronal action potential propagation; IEA:Compara.
 GO:0045666; P:positive regulation of neuron differentiation; NAS:UniProtKB.
 GO:0008104; P:protein localization; IEA:Compara.
 GO:0030516; P:regulation of axon extension; NAS:UniProtKB.
 GO:0031290; P:retinal ganglion cell axon guidance; IEA:Compara.
 GO:0007416; P:synapse assembly; TAS:UniProtKB. 
Interpro
 IPR026966; Fibronectin_III_C.
 IPR003961; Fibronectin_type3.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003006; Ig/MHC_CS.
 IPR013098; Ig_I-set.
 IPR003599; Ig_sub.
 IPR003598; Ig_sub2. 
Pfam
 PF13882; Bravo_FIGEY
 PF00041; fn3
 PF07679; I-set 
SMART
 SM00060; FN3
 SM00409; IG
 SM00408; IGc2 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE
 PS00290; IG_MHC 
PRINTS