CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017364
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Latent-transforming growth factor beta-binding protein 4 
Protein Synonyms/Alias
 LTBP-4 
Gene Name
 LTBP4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MGDVKALLFVVAmethylation[1]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM) (By similarity). 
Sequence Annotation
 DOMAIN 149 181 EGF-like 1.
 DOMAIN 287 339 TB 1.
 DOMAIN 357 397 EGF-like 2; calcium-binding (Potential).
 DOMAIN 407 459 TB 2.
 DOMAIN 545 586 EGF-like 3.
 DOMAIN 587 628 EGF-like 4; calcium-binding (Potential).
 DOMAIN 629 670 EGF-like 5; calcium-binding (Potential).
 DOMAIN 671 708 EGF-like 6; calcium-binding (Potential).
 DOMAIN 710 751 EGF-like 7; calcium-binding (Potential).
 DOMAIN 752 793 EGF-like 8; calcium-binding (Potential).
 DOMAIN 834 877 EGF-like 9; calcium-binding (Potential).
 DOMAIN 878 919 EGF-like 10; calcium-binding (Potential).
 DOMAIN 920 960 EGF-like 11; calcium-binding (Potential).
 DOMAIN 1049 1090 EGF-like 12; calcium-binding (Potential).
 DOMAIN 1181 1235 TB 3.
 DOMAIN 1253 1295 EGF-like 13; calcium-binding (Potential).
 DOMAIN 1296 1337 EGF-like 14; calcium-binding (Potential).
 DOMAIN 1349 1402 TB 4.
 DOMAIN 1533 1573 EGF-like 15.
 DOMAIN 1574 1618 EGF-like 16.
 CARBOHYD 352 352 N-linked (GlcNAc...) (Potential).
 CARBOHYD 425 425 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1055 1055 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1200 1200 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1339 1339 N-linked (GlcNAc...) (Potential).
 DISULFID 153 163 By similarity.
 DISULFID 157 169 By similarity.
 DISULFID 171 180 By similarity.
 DISULFID 361 372 By similarity.
 DISULFID 367 381 By similarity.
 DISULFID 383 396 By similarity.
 DISULFID 549 561 By similarity.
 DISULFID 556 570 By similarity.
 DISULFID 572 585 By similarity.
 DISULFID 591 603 By similarity.
 DISULFID 598 612 By similarity.
 DISULFID 614 627 By similarity.
 DISULFID 633 645 By similarity.
 DISULFID 640 654 By similarity.
 DISULFID 656 669 By similarity.
 DISULFID 675 687 By similarity.
 DISULFID 682 696 By similarity.
 DISULFID 698 707 By similarity.
 DISULFID 714 726 By similarity.
 DISULFID 721 735 By similarity.
 DISULFID 737 750 By similarity.
 DISULFID 756 768 By similarity.
 DISULFID 763 777 By similarity.
 DISULFID 779 792 By similarity.
 DISULFID 838 851 By similarity.
 DISULFID 845 860 By similarity.
 DISULFID 862 876 By similarity.
 DISULFID 882 894 By similarity.
 DISULFID 888 903 By similarity.
 DISULFID 905 918 By similarity.
 DISULFID 924 935 By similarity.
 DISULFID 930 944 By similarity.
 DISULFID 946 959 By similarity.
 DISULFID 1053 1065 By similarity.
 DISULFID 1059 1074 By similarity.
 DISULFID 1076 1089 By similarity.
 DISULFID 1257 1270 By similarity.
 DISULFID 1265 1279 By similarity.
 DISULFID 1281 1294 By similarity.
 DISULFID 1300 1312 By similarity.
 DISULFID 1307 1321 By similarity.
 DISULFID 1323 1336 By similarity.
 DISULFID 1537 1548 By similarity.
 DISULFID 1543 1557 By similarity.
 DISULFID 1559 1572 By similarity.
 DISULFID 1578 1593 By similarity.
 DISULFID 1588 1602 By similarity.
 DISULFID 1604 1617 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Growth factor binding; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1624 AA 
Protein Sequence
MGDVKALLFV VAARARRLGG AAASESLAVS EAFCRVRSCQ PKKCAGPQRC LNPVPAVPSP 60
SPSVRKRQVS LNWQPLTLQE ARALLKRRRP RGPGGRGLLR RRPPQRAPAG KAPVLCPLIC 120
HNGGVCVKPD RCLCPPDFAG KFCQLHSSGA RPPAPAVPGL TRSVYTMPLA NHRDDEHGVA 180
SMVSVHVEHP QEASVVVHQV ERVSGPWEEA DAEAVARAEA AARAEAAAPY TVLAQSAPRE 240
DGYSDASGFG YCFRELRGGE CASPLPGLRT QEVCCRGAGL AWGVHDCQLC SERLGNSERV 300
SAPDGPCPTG FERVNGSCED VDECATGGRC QHGECANTRG GYTCVCPDGF LLDSSRSSCI 360
SQHVISEAKG PCFRVLRDGG CSLPILRNIT KQICCCSRVG KAWGRGCQLC PPFGSEGFRE 420
ICPAGPGYHY SASDLRYNTR PLGQEPPRVS LSQPRTLPAT SRPSAGFLPT HRLEPRPEPR 480
PDPRPGPELP LPSIPAWTGP EIPESGPSSG MCQRNPQVCG PGRCISRPSG YTCACDSGFR 540
LSPQGTRCID VDECRRVPPP CAPGRCENSP GSFRCVCGPG FRAGPRAAEC LDVDECHRVP 600
PPCDLGRCEN TPGSFLCVCP AGYQAAPHGA SCQDVDECTQ SPGLCGRGAC KNLPGSFRCV 660
CPAGFRGSAC EEDVDECAQE PPPCGPGRCD NTAGSFHCAC PAGFRSRGPG APCQDVDECA 720
RSPPPCTYGR CENTEGSFQC VCPMGFQPNT AGSECEDVDE CENHLACPGQ ECVNSPGSFQ 780
CRTCPSGHHL HRGRCTDVDE CSSGAPPCGP HGHCTNTEGS FRCSCAPGYR APSGRPGPCA 840
DVNECLEGDF CFPHGECLNT DGSFACTCAP GYRPGPRGAS CLDVDECSEE DLCQSGICTN 900
TDGSFECICP PGHRAGPDLA SCLDVDECRE RGPALCGSQR CENSPGSYRC VRDCDPGYHA 960
GPEGTCDDVD ECQEYGPEIC GAQRCENTPG SYRCTPACDP GYQPTPGGGC QDVDECRNRS 1020
FCGAHAVCQN LPGSFQCLCD QGYEGARDGR HCVDVNECET LQGVCGAALC ENVEGSFLCV 1080
CPNSPEEFDP MTGRCVPPRT SAGTFPGSQP QAPASPVLPA RPPPPPLPRR PSTPRQGPVG 1140
SGRRECYFDT AAPDACDNIL ARNVTWQECC CTVGEGWGSG CRIQQCPGTE TAEYQSLCPH 1200
GRGYLAPSGD LSLRRDVDEC QLFRDQVCKS GVCVNTAPGY SCYCSNGYYY HTQRLECIDN 1260
DECADEEPAC EGGRCVNTVG SYHCTCEPPL VLDGSQRRCV SNESQSLDDN LGVCWQEVGA 1320
DLVCSHPRLD RQATYTECCC LYGEAWGMDC ALCPAQDSDD FEALCNVLRP PAYSPPRPGG 1380
FGLPYEYGPD LGPPYQGLPY GPELYPPPAL PYDPYPPPPG PFARREAPYG APRFDMPDFE 1440
DDGGPYGESE APAPPGPGTR WPYRSRDTRR SFPEPEEPPE GGSYAGSLAE PYEELEAEEC 1500
GILDGCTNGR CVRVPEGFTC RCFDGYRLDM TRMACVDINE CDEAEAASPL CVNARCLNTD 1560
GSFRCICRPG FAPTHQPHHC APARPRA 1587 
Gene Ontology
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0005578; C:proteinaceous extracellular matrix; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0005539; F:glycosaminoglycan binding; NAS:UniProtKB.
 GO:0005178; F:integrin binding; NAS:UniProtKB.
 GO:0050431; F:transforming growth factor beta binding; IDA:UniProtKB.
 GO:0005024; F:transforming growth factor beta-activated receptor activity; NAS:UniProtKB.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0030252; P:growth hormone secretion; TAS:UniProtKB.
 GO:0007275; P:multicellular organismal development; TAS:UniProtKB.
 GO:0006457; P:protein folding; TAS:UniProtKB.
 GO:0045595; P:regulation of cell differentiation; TAS:UniProtKB.
 GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
 GO:0030162; P:regulation of proteolysis; IDA:UniProtKB.
 GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; TAS:UniProtKB.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Compara. 
Interpro
 IPR026823; cEGF.
 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.
 IPR017878; TB_dom. 
Pfam
 PF12662; cEGF
 PF07645; EGF_CA
 PF00683; TB 
SMART
 SM00181; EGF
 SM00179; EGF_CA 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS51364; TB 
PRINTS