KI21B_HUMAN - dbPTM
KI21B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KI21B_HUMAN
UniProt AC O75037
Protein Name Kinesin-like protein KIF21B
Gene Name KIF21B
Organism Homo sapiens (Human).
Sequence Length 1637
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, dendrite . Cell projection, growth cone . Cell projection, axon . Cytoplasmic vesicle .
Protein Description Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface..
Protein Sequence MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRDPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVNEAVTGLPDGTPPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQENGYASTDEEISEFSEGSFSQSFTMKGSTSHDDFKFKSEPKLSAQMKAVSAECLGPPLDISTKNITKSLASLVEIKEDGVGFSVRDPYYRDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIISPVGGAKGARTAPLQCVSMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSTSYIKVWDIRDSAKCIRTLTSSGQVISGDACAATSTRAITSAQGEHQINQIALSPSGTMLYAASGNAVRIWELSRFQPVGKLTGHIGPVMCLTVTQTASQHDLVVTGSKDHYVKMFELGECVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAICTNAKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRATTLP
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
205UbiquitinationEELIQCLKQGALSRT
HHHHHHHHHCCCCCC		55.07-
212PhosphorylationKQGALSRTTASTQMN
HHCCCCCCCCCCCCC		24.2821406692
213PhosphorylationQGALSRTTASTQMNV
HCCCCCCCCCCCCCC		19.9424719451
215PhosphorylationALSRTTASTQMNVQS
CCCCCCCCCCCCCCC		19.6521406692
216PhosphorylationLSRTTASTQMNVQSS
CCCCCCCCCCCCCCC		29.4021406692
222PhosphorylationSTQMNVQSSRSHAIF
CCCCCCCCCHHHHEE		24.3629978859
223PhosphorylationTQMNVQSSRSHAIFT
CCCCCCCCHHHHEEE		22.2529978859
326UbiquitinationHVPYRDSKLTRLLQD
EECCCCHHHHHHHHH		59.16-
328PhosphorylationPYRDSKLTRLLQDSL
CCCCHHHHHHHHHHC		24.0220068231
380UbiquitinationKVVVNQDKTSQQISA
CEEECCCCHHHHHHH		40.07-
417PhosphorylationGEDGAEGYSDLFREN
CCCCCCCHHHHHHHH		7.19-
453PhosphorylationDAINNRVTQLMSQEA
HHHHHHHHHHHHHHH		16.8520860994
501PhosphorylationESEAMNESLRRSLSR
HHHHHHHHHHHHHHH		23.36-
510PhosphorylationRRSLSRASARSPYSL
HHHHHHHHCCCCCCC		24.0930377224
510O-linked_GlycosylationRRSLSRASARSPYSL
HHHHHHHHCCCCCCC		24.0928411811
516PhosphorylationASARSPYSLGASPAA
HHCCCCCCCCCCCCC		24.5822210691
532PhosphorylationAFGGSPASSMEDASE
CCCCCCCCCHHHHHH		33.3322210691
562PhosphorylationEVRQRRKSPEKEAFK
HHHHHHCCHHHHHHH		36.1629496963
579PhosphorylationAKLQQENSEETDENE
HHHHHHCCCCCCHHH		35.74-
582PhosphorylationQQENSEETDENEAEE
HHHCCCCCCHHHHHH		44.56-
677AcetylationKLILLQNKIRDTQLE
HHHHHHHHHHCCHHH		26.5921466224
681PhosphorylationLQNKIRDTQLERDRV
HHHHHHCCHHHHHHH		25.7922210691
702AcetylationMECYTEEKANKIKAD
CCCCCHHHHHHHHHH		51.5323749302
739PhosphorylationARLLKNQSRYERELK
HHHHHHHHHHHHHHH		46.3420860994
778PhosphorylationQRRRLVETKRNREIA
HHHHHHHHHHHHHHH		28.0229496963
816PhosphorylationEMVLRRKTQEVSALR
HHHHHHHHHHHHHHH		28.3129083192
820PhosphorylationRRKTQEVSALRRLAK
HHHHHHHHHHHHHHH		22.3429083192
830PhosphorylationRRLAKPMSERVAGRA
HHHHHCHHHHHCCCC		30.6722210691
856PhosphorylationEVSASTTSSEAESGA
EECCCCCCHHHHHCC		26.6922210691
861PhosphorylationTTSSEAESGARSVSS
CCCHHHHHCCCCHHH		44.8122210691
907PhosphorylationQKKGASQSFSKAARL
HHCCCCCCHHHHHHH		29.0626699800
910UbiquitinationGASQSFSKAARLKWQ
CCCCCHHHHHHHHHH		44.02-
932PhosphorylationDIVMQRMTIVNLEAD
HHHHHHCEEEEHHHH		24.7821406692
1044UbiquitinationFLKASIDKGLQVAQK
HHHHHHHHHCHHHHH		60.91-
1051UbiquitinationKGLQVAQKEAQIRLL
HHCHHHHHHHHHHHH		45.33-
1127PhosphorylationQSFTMKGSTSHDDFK
CCEECCCCCCCCCCC		22.6328111955
1128PhosphorylationSFTMKGSTSHDDFKF
CEECCCCCCCCCCCC		38.4628111955
1129PhosphorylationFTMKGSTSHDDFKFK
EECCCCCCCCCCCCC		26.9830108239
1137 (in isoform 2)Phosphorylation-63.3624719451
1137PhosphorylationHDDFKFKSEPKLSAQ
CCCCCCCCCCCCHHH		63.3624719451
1149 (in isoform 2)Phosphorylation-24.1824719451
1149PhosphorylationSAQMKAVSAECLGPP
HHHHHHHHHHHHCCC		24.1830266825
1165PhosphorylationDISTKNITKSLASLV
CCCCCHHHHHHHHHH		24.7928464451
1167PhosphorylationSTKNITKSLASLVEI
CCCHHHHHHHHHHEE		22.1030266825
1170PhosphorylationNITKSLASLVEIKED
HHHHHHHHHHEEECC		37.9430266825
1195PhosphorylationYRDRVSRTVSLPTRG
HCCCCCCEEECCCCC		13.6230266825
1197PhosphorylationDRVSRTVSLPTRGST
CCCCCEEECCCCCCC		28.1923401153
1197 (in isoform 2)Phosphorylation-28.1924719451
1200PhosphorylationSRTVSLPTRGSTFPR
CCEEECCCCCCCCCC		53.6126074081
1201MethylationRTVSLPTRGSTFPRQ
CEEECCCCCCCCCCC		34.82115481199
1209PhosphorylationGSTFPRQSRATETSP
CCCCCCCCCCCCCCC		25.7628787133
1212PhosphorylationFPRQSRATETSPLTR
CCCCCCCCCCCCCCC		38.3924043423
1214PhosphorylationRQSRATETSPLTRRK
CCCCCCCCCCCCCCC		31.1524043423
1215 (in isoform 2)Phosphorylation-16.2224719451
1215PhosphorylationQSRATETSPLTRRKS
CCCCCCCCCCCCCCC		16.2223401153
1218PhosphorylationATETSPLTRRKSYDR
CCCCCCCCCCCCCCC		31.6330108239
1222PhosphorylationSPLTRRKSYDRGQPI
CCCCCCCCCCCCCCC		30.3828450419
1223PhosphorylationPLTRRKSYDRGQPIR
CCCCCCCCCCCCCCC		16.8228102081
1231PhosphorylationDRGQPIRSTDVGFTP
CCCCCCCCCCCCCCC		29.6723927012
1232PhosphorylationRGQPIRSTDVGFTPP
CCCCCCCCCCCCCCC		25.5123927012
1237PhosphorylationRSTDVGFTPPSSPPT
CCCCCCCCCCCCCCC		28.5023927012
1237 (in isoform 2)Phosphorylation-28.50-
1240PhosphorylationDVGFTPPSSPPTRPR
CCCCCCCCCCCCCCC		57.5923927012
1241PhosphorylationVGFTPPSSPPTRPRN
CCCCCCCCCCCCCCC		40.4423927012
1241 (in isoform 2)Phosphorylation-40.44-
1244PhosphorylationTPPSSPPTRPRNDRN
CCCCCCCCCCCCCCC		57.6025159151
1244 (in isoform 2)Phosphorylation-57.60-
1257PhosphorylationRNVFSRLTSNQSQGS
CCHHHHHCCCCCCCC		25.2328450419
1258PhosphorylationNVFSRLTSNQSQGSA
CHHHHHCCCCCCCCC		37.1528450419
1258 (in isoform 2)Phosphorylation-37.15-
1261PhosphorylationSRLTSNQSQGSALDK
HHHCCCCCCCCCCCC		40.5328450419
1261 (in isoform 2)Phosphorylation-40.53-
1264 (in isoform 3)Phosphorylation-20.30-
1264 (in isoform 2)Phosphorylation-20.30-
1264PhosphorylationTSNQSQGSALDKSDD
CCCCCCCCCCCCCCC		20.3023663014
1269PhosphorylationQGSALDKSDDSDSSL
CCCCCCCCCCCCCCH		46.4425159151
1272PhosphorylationALDKSDDSDSSLSEV
CCCCCCCCCCCHHHH		44.3725159151
1274PhosphorylationDKSDDSDSSLSEVLR
CCCCCCCCCHHHHHH		36.8123663014
1275PhosphorylationKSDDSDSSLSEVLRG
CCCCCCCCHHHHHHH		40.6923663014
1277PhosphorylationDDSDSSLSEVLRGII
CCCCCCHHHHHHHHH		27.8328450419
1285PhosphorylationEVLRGIISPVGGAKG
HHHHHHHCCCCCCCC		16.1820860994
1421PhosphorylationQINQIALSPSGTMLY
HEEEEEECCCCCEEE		14.16-
1490PhosphorylationFELGECVTGTIGPTH
EECCCCCCCCCCCCC		40.0224275569
1528UbiquitinationSRDNGIKKWDLDQQE
CCCCCCCCCCCCHHH		43.98-
1584UbiquitinationFTPIGEIKGHDSPIN
CEECCEECCCCCCHH		45.98-
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 KI21B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KI21B_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 KI21B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM3_HUMANTRIM3physical
24086586
BTD_HUMANBTDphysical
26496610
CAPG_HUMANCAPGphysical
26496610
CO4A5_HUMANCOL4A5physical
26496610
CSTF2_HUMANCSTF2physical
26496610
TAF5_HUMANTAF5physical
26496610
TAF12_HUMANTAF12physical
26496610
TBX3_HUMANTBX3physical
26496610
BAG6_HUMANBAG6physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
FUBP3_HUMANFUBP3physical
26496610
HNRPQ_HUMANSYNCRIPphysical
26496610
CPSF5_HUMANNUDT21physical
26496610
PRP6_HUMANPRPF6physical
26496610
MED4_HUMANMED4physical
26496610
CPSF1_HUMANCPSF1physical
26496610
CPSF3_HUMANCPSF3physical
26496610
DPOE3_HUMANPOLE3physical
26496610
KI21A_HUMANKIF21Aphysical
26496610
P3H1_HUMANP3H1physical
26496610
WDR75_HUMANWDR75physical
26496610
TCAM1_HUMANTICAM1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KI21B_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 THR-1237 AND SER-1241, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1237 AND THR-1244, ANDMASS SPECTROMETRY.

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