dbPTM

KTN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KTN1_HUMAN
UniProt AC	Q86UP2
Protein Name	Kinectin
Gene Name	KTN1
Organism	Homo sapiens (Human).
Sequence Length	1357
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type II membrane protein. Vesicle membrane protein anchored to the endoplasmic reticulum.
Protein Description	Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin..
Protein Sequence	MEFYESAYFIVLIPSIVITVIFLFFWLFMKETLYDEVLAKQKREQKLIPTKTDKKKAEKKKNKKKEIQNGNLHESDSESVPRDFKLSDALAVEDDQVAPVPLNVVETSSSVRERKKKEKKQKPVLEEQVIKESDASKIPGKKVEPVPVTKQPTPPSEAAASKKKPGQKKSKNGSDDQDKKVETLMVPSKRQEALPLHQETKQESGSGKKKASSKKQKTENVFVDEPLIHATTYIPLMDNADSSPVVDKREVIDLLKPDQVEGIQKSGTKKLKTETDKENAEVKFKDFLLSLKTMMFSEDEALCVVDLLKEKSGVIQDALKKSSKGELTTLIHQLQEKDKLLAAVKEDAAATKDRCKQLTQEMMTEKERSNVVITRMKDRIGTLEKEHNVFQNKIHVSYQETQQMQMKFQQVREQMEAEIAHLKQENGILRDAVSNTTNQLESKQSAELNKLRQDYARLVNELTEKTGKLQQEEVQKKNAEQAATQLKVQLQEAERRWEEVQSYIRKRTAEHEAAQQDLQSKFVAKENEVQSLHSKLTDTLVSKQQLEQRLMQLMESEQKRVNKEESLQMQVQDILEQNEALKAQIQQFHSQIAAQTSASVLAEELHKVIAEKDKQIKQTEDSLASERDRLTSKEEELKDIQNMNFLLKAEVQKLQALANEQAAAAHELEKMQQSVYVKDDKIRLLEEQLQHEISNKMEEFKILNDQNKALKSEVQKLQTLVSEQPNKDVVEQMEKCIQEKDEKLKTVEELLETGLIQVATKEEELNAIRTENSSLTKEVQDLKAKQNDQVSFASLVEELKKVIHEKDGKIKSVEELLEAELLKVANKEKTVQDLKQEIKALKEEIGNVQLEKAQQLSITSKVQELQNLLKGKEEQMNTMKAVLEEKEKDLANTGKWLQDLQEENESLKAHVQEVAQHNLKEASSASQFEELEIVLKEKENELKRLEAMLKERESDLSSKTQLLQDVQDENKLFKSQIEQLKQQNYQQASSFPPHEELLKVISEREKEISGLWNELDSLKDAVEHQRKKNNDLREKNWEAMEALASTEKMLQDKVNKTSKERQQQVEAVELEAKEVLKKLFPKVSVPSNLSYGEWLHGFEKKAKECMAGTSGSEEVKVLEHKLKEADEMHTLLQLECEKYKSVLAETEGILQKLQRSVEQEENKWKVKVDESHKTIKQMQSSFTSSEQELERLRSENKDIENLRREREHLEMELEKAEMERSTYVTEVRELKDLLTELQKKLDDSYSEAVRQNEELNLLKAQLNETLTKLRTEQNERQKVAGDLHKAQQSLELIQSKIVKAAGDTTVIENSDVSPETESSEKETMSVSLNQTVTQLQQLLQAVNQQLTKEKEHYQVLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	FWLFMKETLYDEVLA HHHHHHHHHHHHHHH	25.71	28796482
34	Phosphorylation	LFMKETLYDEVLAKQ HHHHHHHHHHHHHHH	19.92	28796482
46	Ubiquitination	AKQKREQKLIPTKTD HHHHHHHCCCCCHHC	43.56	-
52	Phosphorylation	QKLIPTKTDKKKAEK HCCCCCHHCHHHHHH	56.37	-
75	Phosphorylation	QNGNLHESDSESVPR CCCCCCCCCCCCCCC	35.37	29255136
75 (in isoform 2)	Phosphorylation	-	35.37	-
75 (in isoform 3)	Phosphorylation	-	35.37	-
77	Phosphorylation	GNLHESDSESVPRDF CCCCCCCCCCCCCCC	40.84	29255136
77 (in isoform 2)	Phosphorylation	-	40.84	-
77 (in isoform 3)	Phosphorylation	-	40.84	-
79	Phosphorylation	LHESDSESVPRDFKL CCCCCCCCCCCCCCH	41.18	29255136
79 (in isoform 2)	Phosphorylation	-	41.18	-
79 (in isoform 3)	Phosphorylation	-	41.18	-
85	Ubiquitination	ESVPRDFKLSDALAV CCCCCCCCHHHHEEC	51.90	-
87	Phosphorylation	VPRDFKLSDALAVED CCCCCCHHHHEECCC	22.79	26074081
107	Phosphorylation	VPLNVVETSSSVRER CCCCHHCCCHHHHHH	23.46	25159151
108	Phosphorylation	PLNVVETSSSVRERK CCCHHCCCHHHHHHH	13.70	25159151
109	Phosphorylation	LNVVETSSSVRERKK CCHHCCCHHHHHHHH	40.03	25159151
109 (in isoform 2)	Phosphorylation	-	40.03	-
109 (in isoform 3)	Phosphorylation	-	40.03	-
110	Phosphorylation	NVVETSSSVRERKKK CHHCCCHHHHHHHHH	25.59	25159151
110 (in isoform 2)	Phosphorylation	-	25.59	-
110 (in isoform 3)	Phosphorylation	-	25.59	-
120	Malonylation	ERKKKEKKQKPVLEE HHHHHHHHCCCCHHH	65.72	32601280
122	Ubiquitination	KKKEKKQKPVLEEQV HHHHHHCCCCHHHHH	46.07	-
131	Ubiquitination	VLEEQVIKESDASKI CHHHHHHCCCHHCCC	52.92	-
133	Phosphorylation	EEQVIKESDASKIPG HHHHHCCCHHCCCCC	33.21	21601212
136	Phosphorylation	VIKESDASKIPGKKV HHCCCHHCCCCCCCC	35.79	21601212
137	2-Hydroxyisobutyrylation	IKESDASKIPGKKVE HCCCHHCCCCCCCCC	55.42	-
149	Phosphorylation	KVEPVPVTKQPTPPS CCCCCCCCCCCCCCH	20.21	23927012
153	Phosphorylation	VPVTKQPTPPSEAAA CCCCCCCCCCHHHHH	45.39	29255136
153 (in isoform 2)	Phosphorylation	-	45.39	-
153 (in isoform 3)	Phosphorylation	-	45.39	-
156	Phosphorylation	TKQPTPPSEAAASKK CCCCCCCHHHHHCCC	40.86	30266825
156 (in isoform 2)	Phosphorylation	-	40.86	-
156 (in isoform 3)	Phosphorylation	-	40.86	-
161	Phosphorylation	PPSEAAASKKKPGQK CCHHHHHCCCCCCCC	40.04	23927012
172	N-linked_Glycosylation	PGQKKSKNGSDDQDK CCCCCCCCCCCCCCH	63.39	UniProtKB CARBOHYD
174	Phosphorylation	QKKSKNGSDDQDKKV CCCCCCCCCCCCHHE	47.62	29214152
180	Ubiquitination	GSDDQDKKVETLMVP CCCCCCHHEEEEECC	54.30	-
183	Phosphorylation	DQDKKVETLMVPSKR CCCHHEEEEECCCHH	24.12	28555341
185	Sulfoxidation	DKKVETLMVPSKRQE CHHEEEEECCCHHCC	5.63	21406390
188	O-linked_Glycosylation	VETLMVPSKRQEALP EEEEECCCHHCCCCC	29.12	OGP
189	2-Hydroxyisobutyrylation	ETLMVPSKRQEALPL EEEECCCHHCCCCCC	52.62	-
189	Ubiquitination	ETLMVPSKRQEALPL EEEECCCHHCCCCCC	52.62	-
200	Phosphorylation	ALPLHQETKQESGSG CCCCCHHHHCCCCCC	31.30	28111955
201	Acetylation	LPLHQETKQESGSGK CCCCHHHHCCCCCCC	51.84	26051181
201	Ubiquitination	LPLHQETKQESGSGK CCCCHHHHCCCCCCC	51.84	-
204	Phosphorylation	HQETKQESGSGKKKA CHHHHCCCCCCCCCC	35.45	29396449
206	Phosphorylation	ETKQESGSGKKKASS HHHCCCCCCCCCCCC	57.63	29396449
218	Phosphorylation	ASSKKQKTENVFVDE CCCCCCCCCCEECCC	30.23	22199227
218 (in isoform 2)	Phosphorylation	-	30.23	-
218 (in isoform 3)	Phosphorylation	-	30.23	-
231	Phosphorylation	DEPLIHATTYIPLMD CCCCCCEEECEECCC	13.13	28796482
232	Phosphorylation	EPLIHATTYIPLMDN CCCCCEEECEECCCC	21.90	28796482
233	Phosphorylation	PLIHATTYIPLMDNA CCCCEEECEECCCCC	9.00	28796482
242	Phosphorylation	PLMDNADSSPVVDKR ECCCCCCCCCCCCHH	33.85	25159151
242 (in isoform 2)	Phosphorylation	-	33.85	-
242 (in isoform 3)	Phosphorylation	-	33.85	-
243	Phosphorylation	LMDNADSSPVVDKRE CCCCCCCCCCCCHHH	23.43	25159151
243 (in isoform 2)	Phosphorylation	-	23.43	-
243 (in isoform 3)	Phosphorylation	-	23.43	-
248	Ubiquitination	DSSPVVDKREVIDLL CCCCCCCHHHHHHHC	38.56	-
248 (in isoform 2)	Ubiquitination	-	38.56	-
256	Ubiquitination	REVIDLLKPDQVEGI HHHHHHCCHHHCCCC	54.57	21890473
256	Acetylation	REVIDLLKPDQVEGI HHHHHHCCHHHCCCC	54.57	26051181
256	Ubiquitination	REVIDLLKPDQVEGI HHHHHHCCHHHCCCC	54.57	21906983
256 (in isoform 1)	Ubiquitination	-	54.57	21890473
256 (in isoform 2)	Ubiquitination	-	54.57	21890473
265	Acetylation	DQVEGIQKSGTKKLK HHCCCCHHHCCCCCC	49.27	20167786
265	Malonylation	DQVEGIQKSGTKKLK HHCCCCHHHCCCCCC	49.27	26320211
265	Ubiquitination	DQVEGIQKSGTKKLK HHCCCCHHHCCCCCC	49.27	-
266	Phosphorylation	QVEGIQKSGTKKLKT HCCCCHHHCCCCCCC	35.01	29496963
266 (in isoform 2)	Phosphorylation	-	35.01	-
266 (in isoform 3)	Phosphorylation	-	35.01	-
268	Phosphorylation	EGIQKSGTKKLKTET CCCHHHCCCCCCCCC	31.90	21712546
269	Acetylation	GIQKSGTKKLKTETD CCHHHCCCCCCCCCC	60.68	20167786
270	Acetylation	IQKSGTKKLKTETDK CHHHCCCCCCCCCCH	55.86	20167786
273	Phosphorylation	SGTKKLKTETDKENA HCCCCCCCCCCHHHC	55.33	30108239
275	Phosphorylation	TKKLKTETDKENAEV CCCCCCCCCHHHCCH	58.57	30108239
285	Ubiquitination	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	21890473
285	Ubiquitination	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	21890473
285	Ubiquitination	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	21890473
285	2-Hydroxyisobutyrylation	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	-
285	Acetylation	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	26051181
285	Ubiquitination	ENAEVKFKDFLLSLK HHCCHHHHHHHHHHH	41.68	21890473
285 (in isoform 1)	Ubiquitination	-	41.68	21890473
285 (in isoform 2)	Ubiquitination	-	41.68	21890473
290	Phosphorylation	KFKDFLLSLKTMMFS HHHHHHHHHHHHCCC	29.93	24719451
292	Phosphoglycerylation	KDFLLSLKTMMFSED HHHHHHHHHHCCCCC	30.88	-
309	Ubiquitination	LCVVDLLKEKSGVIQ HHHHHHHHHCCCHHH	71.09	17370265
311	2-Hydroxyisobutyrylation	VVDLLKEKSGVIQDA HHHHHHHCCCHHHHH	51.42	-
320	Acetylation	GVIQDALKKSSKGEL CHHHHHHHHCCCCHH	52.94	26051181
321	Acetylation	VIQDALKKSSKGELT HHHHHHHHCCCCHHH	61.89	7369601
324	2-Hydroxyisobutyrylation	DALKKSSKGELTTLI HHHHHCCCCHHHHHH	64.59	-
324	Acetylation	DALKKSSKGELTTLI HHHHHCCCCHHHHHH	64.59	7369611
324	Ubiquitination	DALKKSSKGELTTLI HHHHHCCCCHHHHHH	64.59	-
337	2-Hydroxyisobutyrylation	LIHQLQEKDKLLAAV HHHHHHHHHHHHHHH	47.40	-
337	Ubiquitination	LIHQLQEKDKLLAAV HHHHHHHHHHHHHHH	47.40	-
339	2-Hydroxyisobutyrylation	HQLQEKDKLLAAVKE HHHHHHHHHHHHHHH	57.37	-
339	Ubiquitination	HQLQEKDKLLAAVKE HHHHHHHHHHHHHHH	57.37	-
345	2-Hydroxyisobutyrylation	DKLLAAVKEDAAATK HHHHHHHHHHHHHCH	45.19	-
345	Acetylation	DKLLAAVKEDAAATK HHHHHHHHHHHHHCH	45.19	26051181
345	Succinylation	DKLLAAVKEDAAATK HHHHHHHHHHHHHCH	45.19	23954790
351	Phosphorylation	VKEDAAATKDRCKQL HHHHHHHCHHHHHHH	28.84	28348404
352	Acetylation	KEDAAATKDRCKQLT HHHHHHCHHHHHHHH	38.15	26051181
359	Phosphorylation	KDRCKQLTQEMMTEK HHHHHHHHHHHHCHH	21.71	-
364	Phosphorylation	QLTQEMMTEKERSNV HHHHHHHCHHHHCCC	42.46	-
366	2-Hydroxyisobutyrylation	TQEMMTEKERSNVVI HHHHHCHHHHCCCEE	49.62	-
366	Acetylation	TQEMMTEKERSNVVI HHHHHCHHHHCCCEE	49.62	26051181
369	Phosphorylation	MMTEKERSNVVITRM HHCHHHHCCCEEEEC	34.76	23403867
374	Phosphorylation	ERSNVVITRMKDRIG HHCCCEEEECHHHCC	17.07	22210691
382	Phosphorylation	RMKDRIGTLEKEHNV ECHHHCCHHHHHHCC	29.40	21601212
385	Acetylation	DRIGTLEKEHNVFQN HHCCHHHHHHCCCCC	68.34	25953088
385	Malonylation	DRIGTLEKEHNVFQN HHCCHHHHHHCCCCC	68.34	26320211
385	Ubiquitination	DRIGTLEKEHNVFQN HHCCHHHHHHCCCCC	68.34	-
398	Phosphorylation	QNKIHVSYQETQQMQ CCCEEECHHHHHHHH	14.85	27642862
423	2-Hydroxyisobutyrylation	EAEIAHLKQENGILR HHHHHHHHHHCCCHH	45.78	-
423	Acetylation	EAEIAHLKQENGILR HHHHHHHHHHCCCHH	45.78	25953088
423	Ubiquitination	EAEIAHLKQENGILR HHHHHHHHHHCCCHH	45.78	-
435	N-linked_Glycosylation	ILRDAVSNTTNQLES CHHHHHHHHHHHHHH	44.30	UniProtKB CARBOHYD
442	Phosphorylation	NTTNQLESKQSAELN HHHHHHHHHHHHHHH	44.58	21712546
443	2-Hydroxyisobutyrylation	TTNQLESKQSAELNK HHHHHHHHHHHHHHH	38.61	-
443	Ubiquitination	TTNQLESKQSAELNK HHHHHHHHHHHHHHH	38.61	-
463	Phosphorylation	ARLVNELTEKTGKLQ HHHHHHHHHHHCCCC	29.29	29396449
465	2-Hydroxyisobutyrylation	LVNELTEKTGKLQQE HHHHHHHHHCCCCHH	58.29	-
465	Acetylation	LVNELTEKTGKLQQE HHHHHHHHHCCCCHH	58.29	26051181
466	Phosphorylation	VNELTEKTGKLQQEE HHHHHHHHCCCCHHH	33.06	29396449
476	2-Hydroxyisobutyrylation	LQQEEVQKKNAEQAA CCHHHHHHHHHHHHH	53.85	-
487	2-Hydroxyisobutyrylation	EQAATQLKVQLQEAE HHHHHHHHHHHHHHH	20.37	-
487	Ubiquitination	EQAATQLKVQLQEAE HHHHHHHHHHHHHHH	20.37	-
521	2-Hydroxyisobutyrylation	AQQDLQSKFVAKENE HHHHHHHHHHHHHHH	30.78	-
521	Acetylation	AQQDLQSKFVAKENE HHHHHHHHHHHHHHH	30.78	26051181
521	Ubiquitination	AQQDLQSKFVAKENE HHHHHHHHHHHHHHH	30.78	-
525	2-Hydroxyisobutyrylation	LQSKFVAKENEVQSL HHHHHHHHHHHHHHH	56.63	-
525	Acetylation	LQSKFVAKENEVQSL HHHHHHHHHHHHHHH	56.63	26051181
531	Phosphorylation	AKENEVQSLHSKLTD HHHHHHHHHHHHHHH	32.97	20068231
535	2-Hydroxyisobutyrylation	EVQSLHSKLTDTLVS HHHHHHHHHHHHHHC	44.66	-
535	Acetylation	EVQSLHSKLTDTLVS HHHHHHHHHHHHHHC	44.66	25953088
535	Malonylation	EVQSLHSKLTDTLVS HHHHHHHHHHHHHHC	44.66	26320211
535	Ubiquitination	EVQSLHSKLTDTLVS HHHHHHHHHHHHHHC	44.66	-
537	Phosphorylation	QSLHSKLTDTLVSKQ HHHHHHHHHHHHCHH	30.58	22210691
539	Phosphorylation	LHSKLTDTLVSKQQL HHHHHHHHHHCHHHH	24.67	20068231
542	Phosphorylation	KLTDTLVSKQQLEQR HHHHHHHCHHHHHHH	28.05	20068231
543	2-Hydroxyisobutyrylation	LTDTLVSKQQLEQRL HHHHHHCHHHHHHHH	34.29	-
543	Acetylation	LTDTLVSKQQLEQRL HHHHHHCHHHHHHHH	34.29	25953088
543	Malonylation	LTDTLVSKQQLEQRL HHHHHHCHHHHHHHH	34.29	26320211
543	Ubiquitination	LTDTLVSKQQLEQRL HHHHHHCHHHHHHHH	34.29	-
551	Sulfoxidation	QQLEQRLMQLMESEQ HHHHHHHHHHHHHHH	2.91	21406390
556	Phosphorylation	RLMQLMESEQKRVNK HHHHHHHHHHHHCCH	31.21	27732954
612	2-Hydroxyisobutyrylation	LHKVIAEKDKQIKQT HHHHHHHHHHHHHHC	62.29	-
617	2-Hydroxyisobutyrylation	AEKDKQIKQTEDSLA HHHHHHHHHCHHHHH	48.99	-
619	Phosphorylation	KDKQIKQTEDSLASE HHHHHHHCHHHHHHH	36.44	-
622	Phosphorylation	QIKQTEDSLASERDR HHHHCHHHHHHHHHH	21.43	21815630
625	Phosphorylation	QTEDSLASERDRLTS HCHHHHHHHHHHCCC	38.16	24719451
633	2-Hydroxyisobutyrylation	ERDRLTSKEEELKDI HHHHCCCCHHHHHHH	65.00	-
633	Acetylation	ERDRLTSKEEELKDI HHHHCCCCHHHHHHH	65.00	26051181
643	Sulfoxidation	ELKDIQNMNFLLKAE HHHHHHHHHHHHHHH	1.84	28183972
653	2-Hydroxyisobutyrylation	LLKAEVQKLQALANE HHHHHHHHHHHHHHH	47.98	-
653	Acetylation	LLKAEVQKLQALANE HHHHHHHHHHHHHHH	47.98	26051181
653	Ubiquitination	LLKAEVQKLQALANE HHHHHHHHHHHHHHH	47.98	-
670	Acetylation	AAAHELEKMQQSVYV HHHHHHHHHHHHEEC	55.42	25953088
670	Ubiquitination	AAAHELEKMQQSVYV HHHHHHHHHHHHEEC	55.42	-
678	2-Hydroxyisobutyrylation	MQQSVYVKDDKIRLL HHHHEECCHHHHHHH	42.39	-
678	Acetylation	MQQSVYVKDDKIRLL HHHHEECCHHHHHHH	42.39	26051181
678	Malonylation	MQQSVYVKDDKIRLL HHHHEECCHHHHHHH	42.39	32601280
696	2-Hydroxyisobutyrylation	LQHEISNKMEEFKIL HHHHHHHHHHHHHHH	40.68	-
696	Acetylation	LQHEISNKMEEFKIL HHHHHHHHHHHHHHH	40.68	26051181
708	Malonylation	KILNDQNKALKSEVQ HHHHHHHHHHHHHHH	49.84	26320211
711	Acetylation	NDQNKALKSEVQKLQ HHHHHHHHHHHHHHH	49.80	25953088
716	Ubiquitination	ALKSEVQKLQTLVSE HHHHHHHHHHHHHHC	47.97	-
722	Phosphorylation	QKLQTLVSEQPNKDV HHHHHHHHCCCCHHH	33.36	24505115
727	Acetylation	LVSEQPNKDVVEQME HHHCCCCHHHHHHHH	59.59	26051181
733	Sulfoxidation	NKDVVEQMEKCIQEK CHHHHHHHHHHHHHH	3.17	21406390
735	Ubiquitination	DVVEQMEKCIQEKDE HHHHHHHHHHHHHHH	31.15	-
740	Acetylation	MEKCIQEKDEKLKTV HHHHHHHHHHHHHHH	55.61	25953088
745	2-Hydroxyisobutyrylation	QEKDEKLKTVEELLE HHHHHHHHHHHHHHH	62.69	-
745	Ubiquitination	QEKDEKLKTVEELLE HHHHHHHHHHHHHHH	62.69	-
746	Phosphorylation	EKDEKLKTVEELLET HHHHHHHHHHHHHHC	43.52	-
761	Ubiquitination	GLIQVATKEEELNAI CCCCCCCCHHHHHHH	54.08	-
772	N-linked_Glycosylation	LNAIRTENSSLTKEV HHHHHCCCCHHHHHH	35.96	UniProtKB CARBOHYD
777	Ubiquitination	TENSSLTKEVQDLKA CCCCHHHHHHHHHHH	62.27	-
783	2-Hydroxyisobutyrylation	TKEVQDLKAKQNDQV HHHHHHHHHHHCCCC	62.92	-
785	Ubiquitination	EVQDLKAKQNDQVSF HHHHHHHHHCCCCCH	48.31	-
791	Phosphorylation	AKQNDQVSFASLVEE HHHCCCCCHHHHHHH	14.95	22817900
800	Acetylation	ASLVEELKKVIHEKD HHHHHHHHHHHHHCC	48.55	26051181
800	Ubiquitination	ASLVEELKKVIHEKD HHHHHHHHHHHHHCC	48.55	-
800 (in isoform 2)	Ubiquitination	-	48.55	-
806	2-Hydroxyisobutyrylation	LKKVIHEKDGKIKSV HHHHHHHCCCCCCCH	58.58	-
811	Ubiquitination	HEKDGKIKSVEELLE HHCCCCCCCHHHHHH	52.51	-
812	Phosphorylation	EKDGKIKSVEELLEA HCCCCCCCHHHHHHH	37.93	21712546
823	Acetylation	LLEAELLKVANKEKT HHHHHHHHHHCCHHH	52.50	26051181
823	Ubiquitination	LLEAELLKVANKEKT HHHHHHHHHHCCHHH	52.50	-
829	2-Hydroxyisobutyrylation	LKVANKEKTVQDLKQ HHHHCCHHHHHHHHH	56.45	-
830	Phosphorylation	KVANKEKTVQDLKQE HHHCCHHHHHHHHHH	25.21	22817900
835	Acetylation	EKTVQDLKQEIKALK HHHHHHHHHHHHHHH	54.92	23954790
835	Malonylation	EKTVQDLKQEIKALK HHHHHHHHHHHHHHH	54.92	26320211
835	Succinylation	EKTVQDLKQEIKALK HHHHHHHHHHHHHHH	54.92	23954790
835	Ubiquitination	EKTVQDLKQEIKALK HHHHHHHHHHHHHHH	54.92	-
842	2-Hydroxyisobutyrylation	KQEIKALKEEIGNVQ HHHHHHHHHHHCCCH	59.15	-
842	Acetylation	KQEIKALKEEIGNVQ HHHHHHHHHHHCCCH	59.15	23236377
842	Malonylation	KQEIKALKEEIGNVQ HHHHHHHHHHHCCCH	59.15	26320211
842	Ubiquitination	KQEIKALKEEIGNVQ HHHHHHHHHHHCCCH	59.15	-
842 (in isoform 2)	Ubiquitination	-	59.15	-
852	Ubiquitination	IGNVQLEKAQQLSIT HCCCHHHHHHHHCCH	61.15	-
870	Ubiquitination	QELQNLLKGKEEQMN HHHHHHHCCHHHHHH	71.72	-
872	2-Hydroxyisobutyrylation	LQNLLKGKEEQMNTM HHHHHCCHHHHHHHH	57.39	-
883 (in isoform 3)	Phosphorylation	-	9.33	-
886	2-Hydroxyisobutyrylation	MKAVLEEKEKDLANT HHHHHHHHHHHHHHC	61.77	-
895	Ubiquitination	KDLANTGKWLQDLQE HHHHHCCHHHHHHHH	42.57	-
904	N-linked_Glycosylation	LQDLQEENESLKAHV HHHHHHHHHHHHHHH	43.32	UniProtKB CARBOHYD
906	Phosphorylation	DLQEENESLKAHVQE HHHHHHHHHHHHHHH	46.91	22199227
906 (in isoform 2)	Phosphorylation	-	46.91	-
908	Ubiquitination	QEENESLKAHVQEVA HHHHHHHHHHHHHHH	45.80	-
923	Phosphorylation	QHNLKEASSASQFEE HHCHHHCCCCHHHHH	27.77	22199227
924	Phosphorylation	HNLKEASSASQFEEL HCHHHCCCCHHHHHH	38.70	28348404
926	Phosphorylation	LKEASSASQFEELEI HHHCCCCHHHHHHHH	37.03	27251275
943	2-Hydroxyisobutyrylation	KEKENELKRLEAMLK HHHHHHHHHHHHHHH	49.08	-
959	2-Hydroxyisobutyrylation	RESDLSSKTQLLQDV HHCHHHHHHHHHHHH	36.59	-
959	Ubiquitination	RESDLSSKTQLLQDV HHCHHHHHHHHHHHH	36.59	-
971	2-Hydroxyisobutyrylation	QDVQDENKLFKSQIE HHHHHHHHHHHHHHH	53.93	-
971	Acetylation	QDVQDENKLFKSQIE HHHHHHHHHHHHHHH	53.93	26051181
971	Ubiquitination	QDVQDENKLFKSQIE HHHHHHHHHHHHHHH	53.93	-
974	2-Hydroxyisobutyrylation	QDENKLFKSQIEQLK HHHHHHHHHHHHHHH	52.46	-
974	Acetylation	QDENKLFKSQIEQLK HHHHHHHHHHHHHHH	52.46	27452117
974	Ubiquitination	QDENKLFKSQIEQLK HHHHHHHHHHHHHHH	52.46	-
985	Phosphorylation	EQLKQQNYQQASSFP HHHHHHCHHHHHCCC	9.54	27642862
1006	Ubiquitination	KVISEREKEISGLWN HHHHHHHHHHHHHHH	67.57	-
1009	Phosphorylation	SEREKEISGLWNELD HHHHHHHHHHHHHHH	29.00	22199227
1019	2-Hydroxyisobutyrylation	WNELDSLKDAVEHQR HHHHHHHHHHHHHHH	47.82	-
1019	Ubiquitination	WNELDSLKDAVEHQR HHHHHHHHHHHHHHH	47.82	-
1053	2-Hydroxyisobutyrylation	TEKMLQDKVNKTSKE HHHHHHHHHHHCHHH	34.44	-
1055	N-linked_Glycosylation	KMLQDKVNKTSKERQ HHHHHHHHHCHHHHH	47.86	UniProtKB CARBOHYD
1084	Phosphorylation	KKLFPKVSVPSNLSY HHHCCCCCCCCCCCC	34.14	26657352
1087	Phosphorylation	FPKVSVPSNLSYGEW CCCCCCCCCCCCHHH	48.52	27251275
1088	N-linked_Glycosylation	PKVSVPSNLSYGEWL CCCCCCCCCCCHHHH	27.26	UniProtKB CARBOHYD
1090	Phosphorylation	VSVPSNLSYGEWLHG CCCCCCCCCHHHHHH	35.03	26471730
1100	2-Hydroxyisobutyrylation	EWLHGFEKKAKECMA HHHHHHHHHHHHHHC	56.63	-
1100	Acetylation	EWLHGFEKKAKECMA HHHHHHHHHHHHHHC	56.63	25953088
1100	Ubiquitination	EWLHGFEKKAKECMA HHHHHHHHHHHHHHC	56.63	-
1116	2-Hydroxyisobutyrylation	TSGSEEVKVLEHKLK CCCCHHHHHHHHHCC	44.36	-
1116	Acetylation	TSGSEEVKVLEHKLK CCCCHHHHHHHHHCC	44.36	26051181
1121	Ubiquitination	EVKVLEHKLKEADEM HHHHHHHHCCHHHHH	52.45	-
1123	2-Hydroxyisobutyrylation	KVLEHKLKEADEMHT HHHHHHCCHHHHHHH	56.51	-
1123	Acetylation	KVLEHKLKEADEMHT HHHHHHCCHHHHHHH	56.51	26051181
1138	2-Hydroxyisobutyrylation	LLQLECEKYKSVLAE HHHHHHHHHHHHHHH	70.41	-
1138	Acetylation	LLQLECEKYKSVLAE HHHHHHHHHHHHHHH	70.41	26051181
1140	Acetylation	QLECEKYKSVLAETE HHHHHHHHHHHHHHH	45.19	26051181
1152	Acetylation	ETEGILQKLQRSVEQ HHHHHHHHHHHHHHH	43.04	25953088
1152	Ubiquitination	ETEGILQKLQRSVEQ HHHHHHHHHHHHHHH	43.04	-
1163	Acetylation	SVEQEENKWKVKVDE HHHHHHHCCEEEECH	52.23	26051181
1171	Phosphorylation	WKVKVDESHKTIKQM CEEEECHHHHHHHHH	26.31	27251275
1176	Ubiquitination	DESHKTIKQMQSSFT CHHHHHHHHHHHCCC	44.97	-
1178	Sulfoxidation	SHKTIKQMQSSFTSS HHHHHHHHHHCCCCC	3.38	21406390
1180	Phosphorylation	KTIKQMQSSFTSSEQ HHHHHHHHCCCCCHH	23.29	28555341
1181	Phosphorylation	TIKQMQSSFTSSEQE HHHHHHHCCCCCHHH	18.69	21815630
1183	Phosphorylation	KQMQSSFTSSEQELE HHHHHCCCCCHHHHH	33.04	27251275
1184	Phosphorylation	QMQSSFTSSEQELER HHHHCCCCCHHHHHH	29.84	27251275
1185	Phosphorylation	MQSSFTSSEQELERL HHHCCCCCHHHHHHH	40.00	27251275
1194	Phosphorylation	QELERLRSENKDIEN HHHHHHHHCCCHHHH	50.54	29214152
1211	Sulfoxidation	REREHLEMELEKAEM HHHHHHHHHHHHHHH	10.04	21406390
1221	Phosphorylation	EKAEMERSTYVTEVR HHHHHHHHHHHHHHH	15.70	28555341
1223	Phosphorylation	AEMERSTYVTEVREL HHHHHHHHHHHHHHH	13.46	27642862
1231	2-Hydroxyisobutyrylation	VTEVRELKDLLTELQ HHHHHHHHHHHHHHH	41.39	-
1239	2-Hydroxyisobutyrylation	DLLTELQKKLDDSYS HHHHHHHHHCCCHHH	68.85	-
1239 (in isoform 2)	Ubiquitination	-	68.85	21890473
1244	Phosphorylation	LQKKLDDSYSEAVRQ HHHHCCCHHHHHHHH	30.17	25159151
1245	Ubiquitination	QKKLDDSYSEAVRQN HHHCCCHHHHHHHHH	19.95	21890473
1245	Phosphorylation	QKKLDDSYSEAVRQN HHHCCCHHHHHHHHH	19.95	-
1246	Phosphorylation	KKLDDSYSEAVRQNE HHCCCHHHHHHHHHH	24.03	-
1259 (in isoform 2)	Phosphorylation	-	36.93	-
1263	N-linked_Glycosylation	NLLKAQLNETLTKLR HHHHHHHHHHHHHHH	28.29	UniProtKB CARBOHYD
1265	Phosphorylation	LKAQLNETLTKLRTE HHHHHHHHHHHHHHH	38.36	23917254
1265 (in isoform 3)	Phosphorylation	-	38.36	-
1268	Ubiquitination	QLNETLTKLRTEQNE HHHHHHHHHHHHHHH	38.80	21890473
1268	2-Hydroxyisobutyrylation	QLNETLTKLRTEQNE HHHHHHHHHHHHHHH	38.80	-
1268	Acetylation	QLNETLTKLRTEQNE HHHHHHHHHHHHHHH	38.80	25953088
1268	Malonylation	QLNETLTKLRTEQNE HHHHHHHHHHHHHHH	38.80	26320211
1270 (in isoform 2)	Phosphorylation	-	37.46	-
1276 (in isoform 3)	Phosphorylation	-	49.52	-
1285	Ubiquitination	KVAGDLHKAQQSLEL HHHHHHHHHHHHHHH	56.01	-
1289	Phosphorylation	DLHKAQQSLELIQSK HHHHHHHHHHHHHHH	16.25	28258704
1296	Ubiquitination	SLELIQSKIVKAAGD HHHHHHHHHHHHHCC	34.83	21890473
1296	Ubiquitination	SLELIQSKIVKAAGD HHHHHHHHHHHHHCC	34.83	21890473
1296 (in isoform 1)	Ubiquitination	-	34.83	21890473
1304	Phosphorylation	IVKAAGDTTVIENSD HHHHHCCCEEEECCC	23.26	23403867
1305	Phosphorylation	VKAAGDTTVIENSDV HHHHCCCEEEECCCC	24.99	23403867
1310	Phosphorylation	DTTVIENSDVSPETE CCEEEECCCCCCCCC	26.97	21955146
1313	Phosphorylation	VIENSDVSPETESSE EEECCCCCCCCCCCC	23.24	29255136
1316	Phosphorylation	NSDVSPETESSEKET CCCCCCCCCCCCCHH	44.55	29255136
1318	Phosphorylation	DVSPETESSEKETMS CCCCCCCCCCCHHCC	51.74	29255136
1319	Phosphorylation	VSPETESSEKETMSV CCCCCCCCCCHHCCC	46.59	29255136
1323	Phosphorylation	TESSEKETMSVSLNQ CCCCCCHHCCCHHHH	26.30	20068231
1325	Phosphorylation	SSEKETMSVSLNQTV CCCCHHCCCHHHHHH	18.90	20068231
1327	Phosphorylation	EKETMSVSLNQTVTQ CCHHCCCHHHHHHHH	17.81	20068231
1329	N-linked_Glycosylation	ETMSVSLNQTVTQLQ HHCCCHHHHHHHHHH	28.15	UniProtKB CARBOHYD
1331	Phosphorylation	MSVSLNQTVTQLQQL CCCHHHHHHHHHHHH	25.17	20068231
1333	Phosphorylation	VSLNQTVTQLQQLLQ CHHHHHHHHHHHHHH	27.27	20068231
1350	2-Hydroxyisobutyrylation	NQQLTKEKEHYQVLE HHHHHHHHHHHHHCC	51.88	-
1353	Phosphorylation	LTKEKEHYQVLE--- HHHHHHHHHHCC---	11.04	28796482

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
75	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KTN1_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 KTN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1D_HUMAN	EEF1D	physical	12773547
RHOG_HUMAN	RHOG	physical	11689693
PYRG2_HUMAN	CTPS2	physical	22863883
SYWC_HUMAN	WARS	physical	22863883
MEOX2_HUMAN	MEOX2	physical	25416956
SGTA_HUMAN	SGTA	physical	25416956
CLC7A_HUMAN	CLEC7A	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956
CDR2_HUMAN	CDR2	physical	27173435

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 KTN1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-75; THR-153 AND SER-156,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77 AND THR-153,AND MASS SPECTROMETRY.	17081983 [Abstract]
"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 THR-153, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASSSPECTROMETRY.	19007248 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-309, AND MASSSPECTROMETRY.	17370265 [Abstract]