KTN1_MOUSE - dbPTM
KTN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KTN1_MOUSE
UniProt AC Q61595
Protein Name Kinectin
Gene Name Ktn1 {ECO:0000312|MGI:MGI:109153}
Organism Mus musculus (Mouse).
Sequence Length 1327
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Vesicle membrane protein anchored to the endoplasmic reticulum (By similarity). Some isoforms containing the inserts at residues 1007-1035 and 1154-1177 are detected in neurite p
Protein Description Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin (By similarity)..
Protein Sequence MELYESTYFIVLIPSVVITVIFLFFWLFMKETLYDEVLAKQKREQKLISTKTDKKKAEKKKNKKKEIQNGTLRESDSEHVPRDFKLSDASPAEDEQFVPAPLNVAETSSSVRERQKKEKKQKPSLEEQVIKESDASKIPGKKVEPVLVTKQPAPPPPLEAAALKKKAGQKKSKNGSEEQDKKVEMLMAPSKEQDVLLSHQDTKQEGGLGKKKGLSKKQKSENVAVLVDEPLIHATTYMPLDNANSNLMMDKREIIDMIKPDHVEGIQKSGTKKLKIETDKENAEVKFKDFLLSLKTMMFSEDEALCVVDLLKEKSGVIKEALKKSNKGELSGLLHQLQEKERLLSAMKEDAAASKERCKRLTQEMMTEKERSSVVIARMKDRIGTLEKEHNIFQNKMHASYQETQQMQMKFQQVQEQMEAEIAHLKQENGILRDAVSNTTNQLESKQSAELNKLRQDCGRLVSELNEKTGKLQQEGVQKKNAEQAATQLKVQLQEAERRWEEVQSYIRKRTAEHEAAQQDLQSKFVAKENEVQSLHSKLTDTLVSKQQLEQRLMQLMESEQKRASKEESLQIQVQDILEQNEALKAQIQQFHSQIAAQTSASVLAEELHKVIAEKDKQLKQTEDSLANEQDHLASKEEELKDVQNMNFLLKAEVQKWQALANEQAATAHEVEKMQKSIHVKEDEIRLLEEQLQHEVASKMEELKILSEQNKALQSEVRKLQTAVSQQPNKDVVEQMEKCIQEKDEKLRTVEELLETGLIQVATREEELSAIRTENSTLTREVQELKAKQSDQVSFVSLIEDLKRVIHEKDGQIKSVEELLEVELLKVANKEKTVQALKQEIEVLKEEIGNAQLEKAHQLSVTSQVQELQNLLRGKEEQVNSMKAALEDRDRGLTGRGTCAQVCSTPQFEELESVLKEKDNEIKRIEVKLKDTESDVSKMSELLKEVQEENKFLKCQLSHQKHQQASFPSQEELQTVISEKEKEITDLCNELESLKNAVEHQRKKNNDLREKNWEAMEALASTEKMLQDRVNKTSKERRQHVEAIELESKDLLKRLFPTVSVPSNLNYSEWLRGFEKKAKACVAGTSDAEAVKVLEHRLKEASEMHTLLQLECEKYKSVLAETEGILQKLQRSVEQEESKWKIKADESQRMIKQMQSSFTASERELERLRQENKDMENLRREREHLEMELEKAEMERSTYVMEVRELKDLLTELQKKLDDSYSEAVRQNEELNLLKTQLNETHSKLQNEQTERKKVADDLHKAQQSLNSIHSKISLKAAGDTVVIENSDISPEMESPEKETMSVSLNQTVTQLQQLLQEVNQQLTKET
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
40UbiquitinationLYDEVLAKQKREQKL
HHHHHHHHHHHHHHH		52.79-
49PhosphorylationKREQKLISTKTDKKK
HHHHHHHCCHHHHHH		34.0024719451
69N-linked_GlycosylationNKKKEIQNGTLRESD
HHCHHHHCCCCCCCC		51.59-
71PhosphorylationKKEIQNGTLRESDSE
CHHHHCCCCCCCCCC		30.1426824392
75PhosphorylationQNGTLRESDSEHVPR
HCCCCCCCCCCCCCC		39.7527087446
77PhosphorylationGTLRESDSEHVPRDF
CCCCCCCCCCCCCCC		38.5927742792
87PhosphorylationVPRDFKLSDASPAED
CCCCCCCCCCCCCCC		31.5525619855
90PhosphorylationDFKLSDASPAEDEQF
CCCCCCCCCCCCCCC		29.6326239621
107PhosphorylationAPLNVAETSSSVRER
CCCCHHHCCHHHHHH		24.9525619855
108PhosphorylationPLNVAETSSSVRERQ
CCCHHHCCHHHHHHH		16.4825619855
109PhosphorylationLNVAETSSSVRERQK
CCHHHCCHHHHHHHH		40.0325619855
110PhosphorylationNVAETSSSVRERQKK
CHHHCCHHHHHHHHH		25.5925619855
124PhosphorylationKEKKQKPSLEEQVIK
HHHHCCCCHHHHHHC		56.2927717184
131AcetylationSLEEQVIKESDASKI
CHHHHHHCCCHHCCC		52.927844371
202PhosphorylationVLLSHQDTKQEGGLG
HHHCCCCCCCCCCCC		28.2328464351
219AcetylationKGLSKKQKSENVAVL
CCCCHHCCCCCEEEE		69.497714071
288UbiquitinationENAEVKFKDFLLSLK
HHCCHHHHHHHHHHH		41.68-
331PhosphorylationKSNKGELSGLLHQLQ
HCCHHHHHHHHHHHH		24.0825338131
345PhosphorylationQEKERLLSAMKEDAA
HHHHHHHHHHHHHHH		30.8025338131
367PhosphorylationRLTQEMMTEKERSSV
HHHHHHHCHHHHCHH		42.46-
373PhosphorylationMTEKERSSVVIARMK
HCHHHHCHHHHHHHH		26.99-
448PhosphorylationNQLESKQSAELNKLR
HHHHHHHHHHHHHHH		27.7028059163
540PhosphorylationQSLHSKLTDTLVSKQ
HHHHHHHHHHHHCHH		30.5822802335
559PhosphorylationRLMQLMESEQKRASK
HHHHHHHHHHHHCCH		31.2122802335
788UbiquitinationEVQELKAKQSDQVSF
HHHHHHHCCCCCCCH		49.07-
803UbiquitinationVSLIEDLKRVIHEKD
HHHHHHHHHHHHHCC		57.87-
814UbiquitinationHEKDGQIKSVEELLE
HHCCCCCCCHHHHHH		40.33-
903S-palmitoylationRGTCAQVCSTPQFEE
CCHHHHHCCCCCHHH		2.2028680068
951AcetylationKEVQEENKFLKCQLS
HHHHHHCCCHHHHHH		56.1822826441
951UbiquitinationKEVQEENKFLKCQLS
HHHHHHCCCHHHHHH		56.18-
969PhosphorylationHQQASFPSQEELQTV
HHHCCCCCHHHHHHH		48.4926370283
970 (in isoform 4)Phosphorylation-48.7127841257
970 (in isoform 3)Phosphorylation-48.7127841257
970 (in isoform 2)Phosphorylation-48.7127841257
970 (in isoform 16)Phosphorylation-48.7127841257
970 (in isoform 12)Phosphorylation-48.7127841257
970 (in isoform 10)Phosphorylation-48.7127841257
993 (in isoform 6)Phosphorylation-58.2127841257
993PhosphorylationDLCNELESLKNAVEH
HHHHHHHHHHHHHHH		58.2127841257
993 (in isoform 5)Phosphorylation-58.2127841257
1031N-linked_GlycosylationKMLQDRVNKTSKERR
HHHHHHHHHCHHHHH		42.66-
1058PhosphorylationLLKRLFPTVSVPSNL
HHHHHCCCCCCCCCC		20.3423984901
1060PhosphorylationKRLFPTVSVPSNLNY
HHHCCCCCCCCCCCH		30.6823984901
1063PhosphorylationFPTVSVPSNLNYSEW
CCCCCCCCCCCHHHH		52.3623984901
1066N-linked_GlycosylationVSVPSNLNYSEWLRG
CCCCCCCCHHHHHHH		42.40-
1198PhosphorylationKAEMERSTYVMEVRE
HHHHHHCHHHHHHHH		26.7620469934
1199PhosphorylationAEMERSTYVMEVREL
HHHHHCHHHHHHHHH		10.0720469934
1287PhosphorylationDTVVIENSDISPEME
CEEEEECCCCCCCCC		24.4325619855
1290PhosphorylationVIENSDISPEMESPE
EEECCCCCCCCCCCC		21.5725619855
1295PhosphorylationDISPEMESPEKETMS
CCCCCCCCCCCHHCC		36.7325619855
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 KTN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KTN1_MOUSE !!
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 KTN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC42_HUMANCDC42physical
9535835
RHOA_HUMANRHOAphysical
9535835
AT2A2_HUMANATP2A2physical
26496610
CATC_HUMANCTSCphysical
26496610
CLCN7_HUMANCLCN7physical
26496610
SYDC_HUMANDARSphysical
26496610
OST48_HUMANDDOSTphysical
26496610
DECR_HUMANDECR1physical
26496610
EF1B_HUMANEEF1B2physical
26496610
EF1D_HUMANEEF1Dphysical
26496610
EF1G_HUMANEEF1Gphysical
26496610
EMD_HUMANEMDphysical
26496610
SYEP_HUMANEPRSphysical
26496610
TF3C2_HUMANGTF3C2physical
26496610
H15_HUMANHIST1H1Bphysical
26496610
SYIC_HUMANIARSphysical
26496610
IF16_HUMANIFI16physical
26496610
STT3A_HUMANSTT3Aphysical
26496610
ITPR3_HUMANITPR3physical
26496610
SYK_HUMANKARSphysical
26496610
SYMC_HUMANMARSphysical
26496610
NOP2_HUMANNOP2physical
26496610
NPM_HUMANNPM1physical
26496610
DPOLB_HUMANPOLBphysical
26496610
PON2_HUMANPON2physical
26496610
ABCD3_HUMANABCD3physical
26496610
SYRC_HUMANRARSphysical
26496610
RL7A_HUMANRPL7Aphysical
26496610
RL18A_HUMANRPL18Aphysical
26496610
RL21_HUMANRPL21physical
26496610
RL22_HUMANRPL22physical
26496610
RL27A_HUMANRPL27Aphysical
26496610
RS16_HUMANRPS16physical
26496610
RS17_HUMANRPS17physical
26496610
RS24_HUMANRPS24physical
26496610
RRBP1_HUMANRRBP1physical
26496610
SOAT1_HUMANSOAT1physical
26496610
SYVC_HUMANVARSphysical
26496610
VRK2_HUMANVRK2physical
26496610
H2B1N_HUMANHIST1H2BNphysical
26496610
H2B1M_HUMANHIST1H2BMphysical
26496610
H1X_HUMANH1FXphysical
26496610
VAPB_HUMANVAPBphysical
26496610
TRIPC_HUMANTRIP12physical
26496610
PTSS1_HUMANPTDSS1physical
26496610
PUM3_HUMANKIAA0020physical
26496610
MBB1A_HUMANMYBBP1Aphysical
26496610
TBL3_HUMANTBL3physical
26496610
ERLN1_HUMANERLIN1physical
26496610
PLPL6_HUMANPNPLA6physical
26496610
CKAP4_HUMANCKAP4physical
26496610
ERLN2_HUMANERLIN2physical
26496610
RRP12_HUMANRRP12physical
26496610
RL13A_HUMANRPL13Aphysical
26496610
OSBL3_HUMANOSBPL3physical
26496610
RL1D1_HUMANRSL1D1physical
26496610
RS27L_HUMANRPS27Lphysical
26496610
SYLC_HUMANLARSphysical
26496610
TMCO1_HUMANTMCO1physical
26496610
T161A_HUMANTMEM161Aphysical
26496610
CC186_HUMANCCDC186physical
26496610
MACOI_HUMANTMEM57physical
26496610
BRX1_HUMANBRIX1physical
26496610
DDX27_HUMANDDX27physical
26496610
ESYT2_HUMANESYT2physical
26496610
ELOV5_HUMANELOVL5physical
26496610
VKOR1_HUMANVKORC1physical
26496610
TMM43_HUMANTMEM43physical
26496610
GT251_HUMANCOLGALT1physical
26496610
ERMP1_HUMANERMP1physical
26496610
MMGT1_HUMANMMGT1physical
26496610
LEMD2_HUMANLEMD2physical
26496610
RABL3_HUMANRABL3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KTN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.

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