CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015926
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CLIP-associating protein 1 
Protein Synonyms/Alias
 Cytoplasmic linker-associated protein 1; Multiple asters homolog 1; Protein Orbit homolog 1; hOrbit1 
Gene Name
 CLASP1 
Gene Synonyms/Alias
 KIAA0622; MAST1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
228TKFDEVQKSGNMIQSubiquitination[1]
493VLAETIKKGIHDADSubiquitination[2]
873SSNWSERKEGLLGLQubiquitination[2, 3, 4, 5]
1000KVKVAILKYIESLARubiquitination[3, 5]
1191GVTEAIEKFSFRSQEubiquitination[3, 4, 5]
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] 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]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] 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
 Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. 
Sequence Annotation
 REPEAT 87 124 HEAT 1.
 REPEAT 163 200 HEAT 2.
 REPEAT 405 440 HEAT 3.
 REPEAT 441 477 HEAT 4.
 REPEAT 974 1011 HEAT 5.
 REPEAT 1342 1379 HEAT 6.
 REPEAT 1460 1497 HEAT 7.
 REGION 662 785 Interaction with microtubules, MAPRE1 and
 REGION 1254 1538 Interaction with CLIP2 (By similarity).
 REGION 1254 1538 Interaction with PHLDB2 and RSN.
 REGION 1256 1538 Localization to kinetochores.
 MOD_RES 545 545 Phosphoserine (By similarity).
 MOD_RES 598 598 Phosphoserine (By similarity).
 MOD_RES 600 600 Phosphoserine.
 MOD_RES 646 646 Phosphoserine.
 MOD_RES 649 649 Phosphoserine.
 MOD_RES 656 656 Phosphothreonine.
 MOD_RES 684 684 Phosphoserine.
 MOD_RES 688 688 Phosphoserine.
 MOD_RES 695 695 Phosphoserine.
 MOD_RES 711 711 Phosphothreonine.
 MOD_RES 714 714 Phosphoserine.
 MOD_RES 797 797 Phosphoserine.
 MOD_RES 1091 1091 Phosphoserine.
 MOD_RES 1099 1099 Phosphothreonine.
 MOD_RES 1196 1196 Phosphoserine.
 MOD_RES 1223 1223 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore; Microtubule; Mitosis; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1538 AA 
Protein Sequence
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN 60
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD 120
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN 180
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN 240
FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 300
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD 360
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN 420
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL 480
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL 540
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 600
DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR 660
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI 720
PRSQGCSRET SPNRIGLARS SRIPRPSMSQ GCSRDTSRES SRDTSPARGF PPLDRFGLGQ 780
PGRIPGSVNA MRVLSTSTDL EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY 840
GSRNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI 900
FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ 960
KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK YIESLARQMD PTDFVNSSET 1020
RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM LLGALPKTFQ DGATKLLHNH 1080
LKNSSNTSVG SPSNTIGRTP SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP 1140
PFSQPNSIPT APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL 1200
NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT QPPRAFPGPR 1260
ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH SDLVADLLKE LSNHNERVEE 1320
RKGALLELLK ITREDSLGVW EEHFKTILLL LLETLGDKDH SIRALALRVL REILRNQPAR 1380
FKNYAELTIM KTLEAHKDSH KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL 1440
AAIKMQTKVV ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK 1500
PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS 1538 
Gene Ontology
 GO:0031592; C:centrosomal corona; IDA:UniProtKB.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
 GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
 GO:0043515; F:kinetochore binding; IMP:UniProtKB.
 GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0051301; P:cell division; IDA:MGI.
 GO:0051294; P:establishment of spindle orientation; IMP:MGI.
 GO:0010458; P:exit from mitosis; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
 GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
 GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
 GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
 GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR024395; CLASP_N_dom.
 IPR000357; HEAT.
 IPR021133; HEAT_type_2. 
Pfam
 PF12348; CLASP_N
 PF02985; HEAT 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS