CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000774
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-Ib 
Protein Synonyms/Alias
 MYH-1c; Myosin I alpha; MMI-alpha; MMIa 
Gene Name
 MYO1B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68LPIYSPEKVEEYRNRubiquitination[1]
131YVAAVCGKGAEVNQVubiquitination[1]
139GAEVNQVKEQLLQSNubiquitination[2]
156LEAFGNAKTVRNDNSubiquitination[1, 2]
241YLSLDSAKVNGVDDAubiquitination[1, 2, 3]
287KLGNIEFKPESRVNGsumoylation[4]
287KLGNIEFKPESRVNGubiquitination[1]
299VNGLDESKIKDKNELubiquitination[2]
354YARDALAKNLYSRLFubiquitination[1, 2]
373NRINESIKAQTKVRKubiquitination[1]
565NPAKINLKRPPTAGSubiquitination[1]
588LMKNLQTKNPNYIRCubiquitination[1, 2]
880TLQRIVQKYFLEMKNubiquitination[1]
952SELFKDKKALYPSSVubiquitination[5]
972GAYLEINKNPKYKKLubiquitination[1, 2, 5]
986LKDAIEEKIIIAEVVubiquitination[1, 2, 5, 6]
995IIAEVVNKINRANGKubiquitination[1]
1021NLLLADQKSGQIKSEubiquitination[1]
1086RTTLSQTKQKLNIEIubiquitination[2]
1116KFIQGNQKNGSVPTCubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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]
 [5] 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]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
Functional Description
 Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport (By similarity). 
Sequence Annotation
 DOMAIN 17 688 Myosin head-like.
 DOMAIN 704 733 IQ 1.
 DOMAIN 728 748 IQ 2.
 DOMAIN 750 779 IQ 3.
 DOMAIN 779 808 IQ 4.
 DOMAIN 808 837 IQ 5.
 DOMAIN 837 866 IQ 6.  
Keyword
 Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1136 AA 
Protein Sequence
MAKMEVKTSL LDNMIGVGDM VLLEPLNEET FINNLKKRFD HSEIYTYIGS VVISVNPYRS 60
LPIYSPEKVE EYRNRNFYEL SPHIFALSDE AYRSLRDQDK DQCILITGES GAGKTEASKL 120
VMSYVAAVCG KGAEVNQVKE QLLQSNPVLE AFGNAKTVRN DNSSRFGKYM DIEFDFKGDP 180
LGGVISNYLL EKSRVVKQPR GERNFHVFYQ LLSGASEELL NKLKLERDFS RYNYLSLDSA 240
KVNGVDDAAN FRTVRNAMQI VGFMDHEAES VLAVVAAVLK LGNIEFKPES RVNGLDESKI 300
KDKNELKEIC ELTGIDQSVL ERAFSFRTVE AKQEKVSTTL NVAQAYYARD ALAKNLYSRL 360
FSWLVNRINE SIKAQTKVRK KVMGVLDIYG FEIFEDNSFE QFIINYCNEK LQQIFIELTL 420
KEEQEEYIRE DIEWTHIDYF NNAIICDLIE NNTNGILAML DEECLRPGTV TDETFLEKLN 480
QVCATHQHFE SRMSKCSRFL NDTSLPHSCF RIQHYAGKVL YQVEGFVDKN NDLLYRDLSQ 540
AMWKASHALI KSLFPEGNPA KINLKRPPTA GSQFKASVAT LMKNLQTKNP NYIRCIKPND 600
KKAAHIFNEA LVCHQIRYLG LLENVRVRRA GYAFRQAYEP CLERYKMLCK QTWPHWKGPA 660
RSGVEVLFNE LEIPVEEYSF GRSKIFIRNP RTLFKLEDLR KQRLEDLATL IQKIYRGWKC 720
RTHFLLMKKS QIVIAAWYRR YAQQKRYQQT KSSALVIQSY IRGWKARKIL RELKHQKRCK 780
EAVTTIAAYW HGTQARRELR RLKEEARNKH AIAVIWAYWL GSKARRELKR LKEEARRKHA 840
VAVIWAYWLG LKVRREYRKF FRANAGKKIY EFTLQRIVQK YFLEMKNKMP SLSPIDKNWP 900
SRPYLFLDST HKELKRIFHL WRCKKYRDQF TDQQKLIYEE KLEASELFKD KKALYPSSVG 960
QPFQGAYLEI NKNPKYKKLK DAIEEKIIIA EVVNKINRAN GKSTSRIFLL TNNNLLLADQ 1020
KSGQIKSEVP LVDVTKVSMS SQNDGFFAVH LKEGSEAASK GDFLFSSDHL IEMATKLYRT 1080
TLSQTKQKLN IEISDEFLVQ FRQDKVCVKF IQGNQKNGSV PTCKRKNNRL LEVAVP 1136 
Gene Ontology
 GO:0005903; C:brush border; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0030175; C:filopodium; ISS:UniProtKB.
 GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
 GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
 GO:0030048; P:actin filament-based movement; ISS:UniProtKB. 
Interpro
 IPR000048; IQ_motif_EF-hand-BS.
 IPR001609; Myosin_head_motor_dom.
 IPR010926; Myosin_tail_2.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00612; IQ
 PF00063; Myosin_head
 PF06017; Myosin_TH1 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.