KIF7_HUMAN - dbPTM
KIF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF7_HUMAN
UniProt AC Q2M1P5
Protein Name Kinesin-like protein KIF7
Gene Name KIF7
Organism Homo sapiens (Human).
Sequence Length 1343
Subcellular Localization Cell projection, cilium . Cytoplasm, cytoskeleton, cilium basal body . Localizes to the cilium tip.
Protein Description Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms. [PubMed: 21633164 Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity]
Protein Sequence MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWRPEAERPPEETASGARGPPRHRSETRIIHRGRRAPGPATASAAAAMRLGAECARYRACTDAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSALSSASGPDSGIESASVEDQAAQGAGGRKEDEGAQQLLTLQNQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELVRPGWGGPRLLNGLPPGSFVPRPHTAPLGGAHAHVLGMVPPACLPGDEVGSEQRGEQVTNGREAGAELLTEVNRLGSGSSAASEEEEEEEEPPRRTLHLRRNRISNCSQRAGARPGSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVGHSRGGEKRSLCSEGRQAPGNEDELHLAPELLWLSPLTEGAPRTREETRDLVHAPLPLTWKRSSLCGEEQGSPEELRQREAAEPLVGRVLPVGEAGLPWNFGPLSKPRRELRRASPGMIDVRKNPL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
161PhosphorylationRDLLEVGTASRDIQL
HHHHHHCCCCCCEEC		27.0023186163
163PhosphorylationLLEVGTASRDIQLRE
HHHHCCCCCCEECCC		30.2623186163
261UbiquitinationAGSERVLKTGSTGER
CCCCCEECCCCCCHH		48.2429967540
311UbiquitinationSKITRILKDSLGGNA
CHHHHHHHHHCCCCC		42.7929967540
398PhosphorylationAPGPATASAAAAMRL
CCCCHHHHHHHHHHH		17.68-
420PhosphorylationRACTDAAYSLLRELQ
HHHHHHHHHHHHHHH		11.1123186163
421PhosphorylationACTDAAYSLLRELQA
HHHHHHHHHHHHHHC		19.0524719451
439UbiquitinationLPGAAARKVRDWLCA
CCHHHHHHHHHHHHH		36.57-
462PhosphorylationSSASGPDSGIESASV
HCCCCCCCCCCCCCH		44.8230377224
466PhosphorylationGPDSGIESASVEDQA
CCCCCCCCCCHHHHH		24.7530377224
468PhosphorylationDSGIESASVEDQAAQ
CCCCCCCCHHHHHHC		35.0130377224
481UbiquitinationAQGAGGRKEDEGAQQ
HCCCCCCCCCHHHHH		73.1829967540
517PhosphorylationLEDAMEQYKLQSDRL
HHHHHHHHHHHHHHH		10.6026074081
521PhosphorylationMEQYKLQSDRLREQQ
HHHHHHHHHHHHHHH		34.8226074081
617PhosphorylationTEVNRLGSGSSAASE
HHHHHCCCCCCCCCH		39.8420363803
619PhosphorylationVNRLGSGSSAASEEE
HHHCCCCCCCCCHHH		20.6427251275
620PhosphorylationNRLGSGSSAASEEEE
HHCCCCCCCCCHHHH		31.2327251275
623PhosphorylationGSGSSAASEEEEEEE
CCCCCCCCHHHHHCC		45.3020363803
645PhosphorylationHLRRNRISNCSQRAG
HHHHHHHCCHHHHCC		28.6626552605
648PhosphorylationRNRISNCSQRAGARP
HHHHCCHHHHCCCCC		27.2726552605
657PhosphorylationRAGARPGSLPERKGP
HCCCCCCCCCCCCCH		43.3528122231
662UbiquitinationPGSLPERKGPELCLE
CCCCCCCCCHHHHHH		76.72-
684PhosphorylationGSRAVGGSKARVQAR
CCCCCCCCCCCEEEE		19.74-
709UbiquitinationRLAQAQQKIRELAIN
HHHHHHHHHHHHHHH		31.48-
720UbiquitinationLAINIRMKEELIGEL
HHHHHHHCHHHHHHH		37.88-
732UbiquitinationGELVRTGKAAQALNR
HHHHHHHHHHHHHHH		39.6829967540
742PhosphorylationQALNRQHSQRIRELE
HHHHHHHHHHHHHHH		16.89-
772UbiquitinationQLRELEGKELQDAGE
HHHHHCCHHHHCHHH		45.9729967540
801UbiquitinationQSQVQVLKEKKQATE
HHHHHHHHHHHHHHH		69.5029967540
803UbiquitinationQVQVLKEKKQATERL
HHHHHHHHHHHHHHH		48.90-
819UbiquitinationSLSAQSEKRLQELER
HCHHHHHHHHHHHHH		64.75-
858UbiquitinationRLEAEMSKRQHRVKE
HHHHHHHHHHHHHHH		55.56-
864UbiquitinationSKRQHRVKELELKHE
HHHHHHHHHHHHHHH		57.44-
869UbiquitinationRVKELELKHEQQQKI
HHHHHHHHHHHHHHH		35.40-
875UbiquitinationLKHEQQQKILKIKTE
HHHHHHHHHHHCCHH		45.7429967540
880UbiquitinationQQKILKIKTEEIAAF
HHHHHHCCHHHHHHH		48.5829967540
893PhosphorylationAFQRKRRSGSNGSVV
HHHHHHHCCCCCCCC		51.0830266825
895PhosphorylationQRKRRSGSNGSVVSL
HHHHHCCCCCCCCCH		38.9830266825
898PhosphorylationRRSGSNGSVVSLEQQ
HHCCCCCCCCCHHHH		24.4830266825
901PhosphorylationGSNGSVVSLEQQQKI
CCCCCCCCHHHHHHH		24.8423403867
907UbiquitinationVSLEQQQKIEEQKKW
CCHHHHHHHHHHHHH		47.98-
913UbiquitinationQKIEEQKKWLDQEME
HHHHHHHHHHHHHHH		53.3229967540
921UbiquitinationWLDQEMEKVLQQRRA
HHHHHHHHHHHHHHH		47.1129967540
938UbiquitinationELGEELHKREAILAK
HHHHHHHHHHHHHHH		65.6429967540
954PhosphorylationEALMQEKTGLESKRL
HHHHHHHHCCCHHHH		46.3726437602
963PhosphorylationLESKRLRSSQALNED
CCHHHHHHHHHHCHH		31.2428122231
964PhosphorylationESKRLRSSQALNEDI
CHHHHHHHHHHCHHH		17.0328122231
983UbiquitinationSRLEHLEKELSEKSG
HHHHHHHHHHHHHHC		71.02-
986PhosphorylationEHLEKELSEKSGQLR
HHHHHHHHHHHCCCC		44.03-
988UbiquitinationLEKELSEKSGQLRQG
HHHHHHHHHCCCCCC		57.4129967540
989PhosphorylationEKELSEKSGQLRQGS
HHHHHHHHCCCCCCC		27.93-
999PhosphorylationLRQGSAQSQQQIRGE
CCCCCHHHHHHHHHH		29.6730576142
1014UbiquitinationIDSLRQEKDSLLKQR
HHHHHHHHHHHHHHH		44.2529967540
1016PhosphorylationSLRQEKDSLLKQRLE
HHHHHHHHHHHHHHH		46.8224719451
1019UbiquitinationQEKDSLLKQRLEIDG
HHHHHHHHHHHHHCC		38.3729967540
1027UbiquitinationQRLEIDGKLRQGSLL
HHHHHCCCCCCCCCC		36.43-
1035PhosphorylationLRQGSLLSPEEERTL
CCCCCCCCHHHHHHH		35.2426091039
1089PhosphorylationMNLMAKLSYLSSSET
HHHHHHHHHHCCHHH		24.2621406692
1090PhosphorylationNLMAKLSYLSSSETR
HHHHHHHHHCCHHHH		22.5021406692
1092PhosphorylationMAKLSYLSSSETRAL
HHHHHHHCCHHHHHH		24.4721406692
1093PhosphorylationAKLSYLSSSETRALL
HHHHHHCCHHHHHHH		29.6021406692
1094PhosphorylationKLSYLSSSETRALLC
HHHHHCCHHHHHHHH		39.3421406692
1096PhosphorylationSYLSSSETRALLCKY
HHHCCHHHHHHHHHH		24.1621406692
1102UbiquitinationETRALLCKYFDKVVT
HHHHHHHHHHHHHEH		49.25-
1103PhosphorylationTRALLCKYFDKVVTL
HHHHHHHHHHHHEHH		18.9321406692
1106UbiquitinationLLCKYFDKVVTLREE
HHHHHHHHHEHHCHH		28.80-
1136PhosphorylationEEQQRLVYWLEVALE
HHHHHHHHHHHHHHH		14.63-
1154PhosphorylationLEMDRQLTLQQKEHE
HHHHHHHHHHHHHHH		17.7427174698
1158UbiquitinationRQLTLQQKEHEQNMQ
HHHHHHHHHHHHHHH		48.34-
1171PhosphorylationMQLLLQQSRDHLGEG
HHHHHHHHHHHHCCC		27.0727174698
1195UbiquitinationARIQALEKELGRYMW
HHHHHHHHHHHHHHH		60.1229967540
1208MethylationMWINQELKQKLGGVN
HHHCHHHHHHHCCCC		44.63-
1208UbiquitinationMWINQELKQKLGGVN
HHHCHHHHHHHCCCC		44.6322505724
1208TrimethylationMWINQELKQKLGGVN
HHHCHHHHHHHCCCC		44.63-
1210UbiquitinationINQELKQKLGGVNAV
HCHHHHHHHCCCCCC		47.7329967540
1220PhosphorylationGVNAVGHSRGGEKRS
CCCCCCCCCCCCCCC		27.05-
1221MethylationVNAVGHSRGGEKRSL
CCCCCCCCCCCCCCC		52.00115481297
1249UbiquitinationLHLAPELLWLSPLTE
HCCCHHHHHHCCCCC		4.0522505724
1252PhosphorylationAPELLWLSPLTEGAP
CHHHHHHCCCCCCCC		13.28-
1276PhosphorylationVHAPLPLTWKRSSLC
CCCCCCCCCCCHHCC		27.31-
1278UbiquitinationAPLPLTWKRSSLCGE
CCCCCCCCCHHCCCC		36.8521890473
1280PhosphorylationLPLTWKRSSLCGEEQ
CCCCCCCHHCCCCCC		24.7622617229
1281PhosphorylationPLTWKRSSLCGEEQG
CCCCCCHHCCCCCCC		31.5421712546
1289PhosphorylationLCGEEQGSPEELRQR
CCCCCCCCHHHHHHH		28.9119664994
1319UbiquitinationAGLPWNFGPLSKPRR
CCCCCCCCCCCCCHH		21.0121890473
1322PhosphorylationPWNFGPLSKPRRELR
CCCCCCCCCCHHHHH		43.69-
1323UbiquitinationWNFGPLSKPRRELRR
CCCCCCCCCHHHHHH		50.67-
1332PhosphorylationRRELRRASPGMIDVR
HHHHHHCCCCCCCCC		21.8521712546
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KIF7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF7_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KIF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACL6A_HUMANACTL6Aphysical
26496610
APC_HUMANAPCphysical
26496610
BBS4_HUMANBBS4physical
26496610
PGBM_HUMANHSPG2physical
26496610
M3K4_HUMANMAP3K4physical
26496610
NRDC_HUMANNRD1physical
26496610
PCM1_HUMANPCM1physical
26496610
CTIP_HUMANRBBP8physical
26496610
SMTN_HUMANSMTNphysical
26496610
GUAA_HUMANGMPSphysical
26496610
MPZL1_HUMANMPZL1physical
26496610
PIBF1_HUMANPIBF1physical
26496610
STABP_HUMANSTAMBPphysical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
CP131_HUMANCEP131physical
26496610
E41L3_HUMANEPB41L3physical
26496610
N4BP3_HUMANN4BP3physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
CEP72_HUMANCEP72physical
26496610
EMSY_HUMANC11orf30physical
26496610
S39AA_HUMANSLC39A10physical
26496610
DOCK6_HUMANDOCK6physical
26496610
CCD77_HUMANCCDC77physical
26496610
PHLB2_HUMANPHLDB2physical
26496610
TBC31_HUMANTBC1D31physical
26496610
ADIP_HUMANSSX2IPphysical
26496610
TAF8_HUMANTAF8physical
26496610
CCD18_HUMANCCDC18physical
26496610
CCD61_HUMANCCDC61physical
26496610
DLRB2_HUMANDYNLRB2physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Ciliary dysfunction leads to a broad spectrum of disorders, collectively termed ciliopathies. The ciliopathy range of diseases includes Meckel-Gruber syndrome, Bardet-Biedl syndrome, Joubert syndrome, and hydrolethalus syndrome among others. Single-locus allelism is insufficient to explain the variable penetrance and expressivity of such disorders, leading to the suggestion that variations across multiple sites of the ciliary proteome influence the clinical outcome. Primary ciliopathy loci can be modulated by pathogenic lesions in other ciliary genes to either exacerbate overall severity or induce specific endophenotypes. KIF7 may be causally associated with diverse ciliopathies, and also acts as a modifier gene across the ciliopathy spectrum.
209900
614120Hydrolethalus syndrome 2 (HLS2)
200990Acrocallosal syndrome (ACLS)
200990Joubert syndrome 12 (JBTS12)
146510Pallister-Hall syndrome (PHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-895 AND SER-1289, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1332, AND MASSSPECTROMETRY.

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