CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005620
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein 4 
Protein Synonyms/Alias
 MAP-4 
Gene Name
 MAP4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56PLLDVDEKTGNSESKubiquitination[1]
312DMELPTEKEVALVKDubiquitination[1]
332ETDVSSAKNVVLPTEubiquitination[1]
346ETEVAPAKDVTLLKEubiquitination[1, 2, 3]
368KMDLAPSKDMGPPKEubiquitination[2, 3]
464NVILTKDKALPLEAEubiquitination[1]
476EAEVAPVKDMAQLPEubiquitination[1]
490ETEIAPAKDVAPSTVubiquitination[1]
498DVAPSTVKEVGLLKDubiquitination[2, 3]
560KTEAPLAKDGVLTLAubiquitination[1]
574ANNVTPAKDVPPLSEubiquitination[1]
838PKKPTAIKTEGKPAEsumoylation[4]
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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] 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]
 [4] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634] 
Functional Description
 Non-neuronal microtubule-associated protein. Promotes microtubule assembly. 
Sequence Annotation
 REPEAT 248 261 1.
 REPEAT 262 275 2.
 REPEAT 276 289 3.
 REPEAT 290 303 4.
 REPEAT 304 317 5.
 REPEAT 318 331 6.
 REPEAT 332 345 7.
 REPEAT 346 351 8; truncated.
 REPEAT 352 377 26 residues 1.
 REPEAT 378 403 26 residues 2.
 REPEAT 408 421 9.
 REPEAT 422 433 10.
 REPEAT 434 447 11.
 REPEAT 448 461 12.
 REPEAT 462 475 13.
 REPEAT 476 489 14.
 REPEAT 490 503 15.
 REPEAT 504 517 16.
 REPEAT 532 545 17.
 REPEAT 923 953 Tau/MAP 1.
 REPEAT 992 1022 Tau/MAP 2.
 REPEAT 1023 1053 Tau/MAP 3.
 REPEAT 1054 1085 Tau/MAP 4.
 REGION 248 545 17 X 14 AA tandem repeats.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 282 282 Phosphothreonine.
 MOD_RES 354 354 Phosphothreonine.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 380 380 Phosphothreonine.
 MOD_RES 384 384 Phosphoserine.
 MOD_RES 507 507 Phosphoserine.
 MOD_RES 510 510 Phosphoserine.
 MOD_RES 521 521 Phosphothreonine.
 MOD_RES 526 526 Phosphothreonine.
 MOD_RES 571 571 Phosphothreonine.
 MOD_RES 580 580 Phosphoserine.
 MOD_RES 585 585 Phosphothreonine.
 MOD_RES 624 624 Phosphoserine.
 MOD_RES 636 636 Phosphoserine.
 MOD_RES 643 643 Phosphoserine (By similarity).
 MOD_RES 656 656 Phosphoserine (By similarity).
 MOD_RES 696 696 Phosphoserine.
 MOD_RES 787 787 Phosphoserine.
 MOD_RES 797 797 Phosphoserine.
 MOD_RES 811 811 Phosphothreonine (By similarity).
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 827 827 Phosphoserine.
 MOD_RES 874 874 Phosphothreonine (By similarity).
 MOD_RES 928 928 Phosphoserine.
 MOD_RES 941 941 Phosphoserine.
 MOD_RES 942 942 Phosphothreonine.
 MOD_RES 1000 1000 Phosphoserine.
 MOD_RES 1073 1073 Phosphoserine.
 MOD_RES 1145 1145 Phosphoserine.
 MOD_RES 1151 1151 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1152 AA 
Protein Sequence
MADLSLADAL TEPSPDIEGE IKRDFIATLE AEAFDDVVGE TVGKTDYIPL LDVDEKTGNS 60
ESKKKPCSET SQIEDTPSSK PTLLANGGHG VEGSDTTGSP TEFLEEKMAY QEYPNSQNWP 120
EDTNFCFQPE QVVDPIQTDP FKMYHDDDLA DLVFPSSATA DTSIFAGQND PLKDSYGMSP 180
CNTAVVPQGW SVEALNSPHS ESFVSPEAVA EPPQPTAVPL ELAKEIEMAS EERPPAQALE 240
IMMGLKTTDM APSKETEMAL AKDMALATKT EVALAKDMES PTKLDVTLAK DMQPSMESDM 300
ALVKDMELPT EKEVALVKDV RWPTETDVSS AKNVVLPTET EVAPAKDVTL LKETERASPI 360
KMDLAPSKDM GPPKENKKET ERASPIKMDL APSKDMGPPK ENKIVPAKDL VLLSEIEVAQ 420
ANDIISSTEI SSAEKVALSS ETEVALARDM TLPPETNVIL TKDKALPLEA EVAPVKDMAQ 480
LPETEIAPAK DVAPSTVKEV GLLKDMSPLS ETEMALGKDV TPPPETEVVL IKNVCLPPEM 540
EVALTEDQVP ALKTEAPLAK DGVLTLANNV TPAKDVPPLS ETEATPVPIK DMEIAQTQKG 600
ISEDSHLESL QDVGQSAAPT FMISPETVTG TGKKCSLPAE EDSVLEKLGE RKPCNSQPSE 660
LSSETSGIAR PEEGRPVVSG TGNDITTPPN KELPPSPEKK TKPLATTQPA KTSTSKAKTQ 720
PTSLPKQPAP TTIGGLNKKP MSLASGLVPA APPKRPAVAS ARPSILPSKD VKPKPIADAK 780
APEKRASPSK PASAPASRSG SKSTQTVAKT TTAAAVASTG PSSRSPSTLL PKKPTAIKTE 840
GKPAEVKKMT AKSVPADLSR PKSTSTSSMK KTTTLSGTAP AAGVVPSRVK ATPMPSRPST 900
TPFIDKKPTS AKPSSTTPRL SRLATNTSAP DLKNVRSKVG STENIKHQPG GGRAKVEKKT 960
EAAATTRKPE SNAVTKTAGP IASAQKQPAG KVQIVSKKVS YSHIQSKCGS KDNIKHVPGG 1020
GNVQIQNKKV DISKVSSKCG SKANIKHKPG GGDVKIESQK LNFKEKAQAK VGSLDNVGHL 1080
PAGGAVKTEG GGSEAPLCPG PPAGEEPAIS EAAPEAGAPT SASGLNGHPT LSGGGDQREA 1140
QTLDSQIQET SI 1152 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; TAS:ProtInc.
 GO:0072686; C:mitotic spindle; IDA:MGI.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0051301; P:cell division; IMP:MGI.
 GO:0051294; P:establishment of spindle orientation; IMP:MGI.
 GO:0051012; P:microtubule sliding; IMP:MGI.
 GO:0007052; P:mitotic spindle organization; IMP:MGI. 
Interpro
 IPR027324; MAP2/MAP4/Tau.
 IPR027323; MAP4.
 IPR001084; Tau/MAP_tubulin-bd_rpt. 
Pfam
 PF00418; Tubulin-binding 
SMART
  
PROSITE
 PS00229; TAU_MAP_1
 PS51491; TAU_MAP_2 
PRINTS