CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012829
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kinesin-like protein KIF7 
Protein Synonyms/Alias
  
Gene Name
 KIF7 
Gene Synonyms/Alias
 UNQ340/PRO539 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
311SKITRILKDSLGGNAubiquitination[1]
439LPGAAARKVRDWLCAubiquitination[1]
481AQGAGGRKEDEGAQQubiquitination[1]
662PGSLPERKGPELCLEubiquitination[1]
709RLAQAQQKIRELAINubiquitination[1]
720LAINIRMKEELIGELubiquitination[1]
732GELVRTGKAAQALNRubiquitination[1]
772QLRELEGKELQDAGEubiquitination[1]
803QVQVLKEKKQATERLubiquitination[1]
819SLSAQSEKRLQELERubiquitination[1]
858RLEAEMSKRQHRVKEubiquitination[1]
864SKRQHRVKELELKHEubiquitination[1]
869RVKELELKHEQQQKIubiquitination[1]
907VSLEQQQKIEEQKKWubiquitination[2]
913QKIEEQKKWLDQEMEubiquitination[1]
921WLDQEMEKVLQQRRAubiquitination[1]
938ELGEELHKREAILAKubiquitination[1]
983SRLEHLEKELSEKSGubiquitination[1]
988LEKELSEKSGQLRQGubiquitination[1]
1019QEKDSLLKQRLEIDGubiquitination[1]
1027QRLEIDGKLRQGSLLubiquitination[1]
1102ETRALLCKYFDKVVTubiquitination[1]
1106LLCKYFDKVVTLREEubiquitination[1]
1158RQLTLQQKEHEQNMQubiquitination[1]
1195ARIQALEKELGRYMWubiquitination[1]
1208MWINQELKQKLGGVNubiquitination[1, 2, 3]
1210INQELKQKLGGVNAVubiquitination[1]
1278APLPLTWKRSSLCGEubiquitination[1, 4, 5]
1323WNFGPLSKPRRELRRubiquitination[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] 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]
 [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
 Acts as both a negative and positive regulator of sonic hedgehog (Shh) pathway, acting downstream of SMO. Negatively regulates the pathway by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates the pathway by preventing the processing of the transcription factor GLI3 into its repressor form. Required for efficient localization of GLI3 to cilia in response to Shh. Affects microtubular dynamics and acts as a ciliary motor. 
Sequence Annotation
 DOMAIN 12 277 Kinesin-motor.
 NP_BIND 94 101 ATP (Potential).
 REGION 513 775 Sufficient for interaction with NPHP1.  
Keyword
 3D-structure; ATP-binding; Bardet-Biedl syndrome; Cell projection; Ciliopathy; Cilium; Coiled coil; Complete proteome; Disease mutation; Joubert syndrome; Mental retardation; Motor protein; Nucleotide-binding; Obesity; Polymorphism; Reference proteome; Repressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1343 AA 
Protein Sequence
MGLEAQRLPG AEEAPVRVAL RVRPLLPKEL LHGHQSCLQV EPGLGRVTLG RDRHFGFHVV 60
LAEDAGQEAV YQACVQPLLE AFFEGFNATV FAYGQTGSGK TYTMGEASVA SLLEDEQGIV 120
PRAMAEAFKL IDENDLLDCL VHVSYLEVYK EEFRDLLEVG TASRDIQLRE DERGNVVLCG 180
VKEVDVEGLD EVLSLLEMGN AARHTGATHL NHLSSRSHTV FTVTLEQRGR APSRLPRPAP 240
GQLLVSKFHF VDLAGSERVL KTGSTGERLK ESIQINSSLL ALGNVISALG DPQRRGSHIP 300
YRDSKITRIL KDSLGGNAKT VMIACVSPSS SDFDETLNTL NYASRAQNIR NRATVNWRPE 360
AERPPEETAS GARGPPRHRS ETRIIHRGRR APGPATASAA AAMRLGAECA RYRACTDAAY 420
SLLRELQAEP GLPGAAARKV RDWLCAVEGE RSALSSASGP DSGIESASVE DQAAQGAGGR 480
KEDEGAQQLL TLQNQVARLE EENRDFLAAL EDAMEQYKLQ SDRLREQQEE MVELRLRLEL 540
VRPGWGGPRL LNGLPPGSFV PRPHTAPLGG AHAHVLGMVP PACLPGDEVG SEQRGEQVTN 600
GREAGAELLT EVNRLGSGSS AASEEEEEEE EPPRRTLHLR RNRISNCSQR AGARPGSLPE 660
RKGPELCLEE LDAAIPGSRA VGGSKARVQA RQVPPATASE WRLAQAQQKI RELAINIRMK 720
EELIGELVRT GKAAQALNRQ HSQRIRELEQ EAEQVRAELS EGQRQLRELE GKELQDAGER 780
SRLQEFRRRV AAAQSQVQVL KEKKQATERL VSLSAQSEKR LQELERNVQL MRQQQGQLQR 840
RLREETEQKR RLEAEMSKRQ HRVKELELKH EQQQKILKIK TEEIAAFQRK RRSGSNGSVV 900
SLEQQQKIEE QKKWLDQEME KVLQQRRALE ELGEELHKRE AILAKKEALM QEKTGLESKR 960
LRSSQALNED IVRVSSRLEH LEKELSEKSG QLRQGSAQSQ QQIRGEIDSL RQEKDSLLKQ 1020
RLEIDGKLRQ GSLLSPEEER TLFQLDEAIE ALDAAIEYKN EAITCRQRVL RASASLLSQC 1080
EMNLMAKLSY LSSSETRALL CKYFDKVVTL REEQHQQQIA FSELEMQLEE QQRLVYWLEV 1140
ALERQRLEMD RQLTLQQKEH EQNMQLLLQQ SRDHLGEGLA DSRRQYEARI QALEKELGRY 1200
MWINQELKQK LGGVNAVGHS RGGEKRSLCS EGRQAPGNED ELHLAPELLW LSPLTEGAPR 1260
TREETRDLVH APLPLTWKRS SLCGEEQGSP EELRQREAAE PLVGRVLPVG EAGLPWNFGP 1320
LSKPRRELRR ASPGMIDVRK NPL 1343 
Gene Ontology
 GO:0005929; C:cilium; IDA:UniProtKB.
 GO:0005875; C:microtubule associated complex; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
 GO:0007018; P:microtubule-based movement; IEA:InterPro.
 GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
 GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB. 
Interpro
 IPR019821; Kinesin_motor_CS.
 IPR001752; Kinesin_motor_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00225; Kinesin 
SMART
 SM00129; KISc 
PROSITE
 PS00411; KINESIN_MOTOR_DOMAIN1
 PS50067; KINESIN_MOTOR_DOMAIN2 
PRINTS
 PR00380; KINESINHEAVY.