dbPTM

TXLNA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TXLNA_HUMAN
UniProt AC	P40222
Protein Name	Alpha-taxilin
Gene Name	TXLNA
Organism	Homo sapiens (Human).
Sequence Length	546
Subcellular Localization
Protein Description	May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells..
Protein Sequence	MKNQDKKNGAAKQSNPKSSPGQPEAGPEGAQERPSQAAPAVEAEGPGSSQAPRKPEGAQARTAQSGALRDVSEELSRQLEDILSTYCVDNNQGGPGEDGAQGEPAEPEDAEKSRTYVARNGEPEPTPVVNGEKEPSKGDPNTEEIRQSDEVGDRDHRRPQEKKKAKGLGKEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSAGGQGSLTDSGPERRPEGPGAQAPSSPRVTEAPCYPGAPSTEASGQTGPQEPTSARA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	KNGAAKQSNPKSSPG CCCCCCCCCCCCCCC	55.16	28464451
18	Phosphorylation	AKQSNPKSSPGQPEA CCCCCCCCCCCCCCC	42.92	25159151
19	Phosphorylation	KQSNPKSSPGQPEAG CCCCCCCCCCCCCCC	38.89	25159151
19	Ubiquitination	KQSNPKSSPGQPEAG CCCCCCCCCCCCCCC	38.89	33845483
33	Ubiquitination	GPEGAQERPSQAAPA CCCCCCCCCCCCCCC	24.88	32015554
35	Phosphorylation	EGAQERPSQAAPAVE CCCCCCCCCCCCCCC	38.38	30278072
48	Phosphorylation	VEAEGPGSSQAPRKP CCCCCCCCCCCCCCC	23.55	23927012
49	Phosphorylation	EAEGPGSSQAPRKPE CCCCCCCCCCCCCCC	35.96	24732914
49	Ubiquitination	EAEGPGSSQAPRKPE CCCCCCCCCCCCCCC	35.96	32015554
54	Ubiquitination	GSSQAPRKPEGAQAR CCCCCCCCCCCCHHH	46.49	29967540
58	Ubiquitination	APRKPEGAQARTAQS CCCCCCCCHHHHHHC	9.74	33845483
65	Phosphorylation	AQARTAQSGALRDVS CHHHHHHCCHHHHHH	24.46	23917254
65	Ubiquitination	AQARTAQSGALRDVS CHHHHHHCCHHHHHH	24.46	23000965
69	Methylation	TAQSGALRDVSEELS HHHCCHHHHHHHHHH	41.57	115919189
72	Phosphorylation	SGALRDVSEELSRQL CCHHHHHHHHHHHHH	29.64	21815630
80	Ubiquitination	EELSRQLEDILSTYC HHHHHHHHHHHHHHC	34.37	23000965
81	Ubiquitination	ELSRQLEDILSTYCV HHHHHHHHHHHHHCC	56.58	33845483
84	Phosphorylation	RQLEDILSTYCVDNN HHHHHHHHHHCCCCC	20.05	29978859
85	Phosphorylation	QLEDILSTYCVDNNQ HHHHHHHHHCCCCCC	19.93	29978859
86	Phosphorylation	LEDILSTYCVDNNQG HHHHHHHHCCCCCCC	6.26	22817900
96	Ubiquitination	DNNQGGPGEDGAQGE CCCCCCCCCCCCCCC	49.23	24816145
113	Phosphorylation	EPEDAEKSRTYVARN CHHHHHHHCCEECCC	22.74	21712546
135	Ubiquitination	VVNGEKEPSKGDPNT CCCCCCCCCCCCCCH	53.03	23000965
136	Ubiquitination	VNGEKEPSKGDPNTE CCCCCCCCCCCCCHH	50.81	23000965
137	Ubiquitination	NGEKEPSKGDPNTEE CCCCCCCCCCCCHHH	77.40	24816145
142	Phosphorylation	PSKGDPNTEEIRQSD CCCCCCCHHHHHCCC	40.14	21815630
146	Methylation	DPNTEEIRQSDEVGD CCCHHHHHCCCCCCC	32.98	115919181
148	Phosphorylation	NTEEIRQSDEVGDRD CHHHHHCCCCCCCCC	26.37	30576142
150	Ubiquitination	EEIRQSDEVGDRDHR HHHHCCCCCCCCCCC	54.36	23000965
151	Ubiquitination	EIRQSDEVGDRDHRR HHHCCCCCCCCCCCC	13.34	23000965
155	Ubiquitination	SDEVGDRDHRRPQEK CCCCCCCCCCCHHHH	44.37	33845483
165	Ubiquitination	RPQEKKKAKGLGKEI CHHHHHHHCCCHHHH	21.74	32015554
170	Ubiquitination	KKAKGLGKEITLLMQ HHHCCCHHHHHHHHH	51.49	29967540
174	Ubiquitination	GLGKEITLLMQTLNT CCHHHHHHHHHHHHH	4.62	32015554
189	Ubiquitination	LSTPEEKLAALCKKY CCCHHHHHHHHHHHH	3.69	33845483
194	2-Hydroxyisobutyrylation	EKLAALCKKYAELLE HHHHHHHHHHHHHHH	50.06	-
194	Acetylation	EKLAALCKKYAELLE HHHHHHHHHHHHHHH	50.06	25953088
194	Ubiquitination	EKLAALCKKYAELLE HHHHHHHHHHHHHHH	50.06	33845483
195	2-Hydroxyisobutyrylation	KLAALCKKYAELLEE HHHHHHHHHHHHHHH	49.01	-
195	Acetylation	KLAALCKKYAELLEE HHHHHHHHHHHHHHH	49.01	26051181
195	Ubiquitination	KLAALCKKYAELLEE HHHHHHHHHHHHHHH	49.01	-
196	Phosphorylation	LAALCKKYAELLEEH HHHHHHHHHHHHHHH	7.27	25907765
202	Ubiquitination	KYAELLEEHRNSQKQ HHHHHHHHHHCHHHH	48.38	32015554
204	Ubiquitination	AELLEEHRNSQKQMK HHHHHHHHCHHHHHH	48.01	24816145
206	Phosphorylation	LLEEHRNSQKQMKLL HHHHHHCHHHHHHHH	38.42	25907765
211	Acetylation	RNSQKQMKLLQKKQS HCHHHHHHHHHHHHH	43.48	25953088
211	Malonylation	RNSQKQMKLLQKKQS HCHHHHHHHHHHHHH	43.48	30639696
216	Ubiquitination	QMKLLQKKQSQLVQE HHHHHHHHHHHHHHH	42.07	29967540
218	Phosphorylation	KLLQKKQSQLVQEKD HHHHHHHHHHHHHHH	34.07	27282143
218	Ubiquitination	KLLQKKQSQLVQEKD HHHHHHHHHHHHHHH	34.07	32015554
224	Acetylation	QSQLVQEKDHLRGEH HHHHHHHHHHHCCHH	33.10	27452117
224	Ubiquitination	QSQLVQEKDHLRGEH HHHHHHHHHHHCCHH	33.10	32015554
228	Ubiquitination	VQEKDHLRGEHSKAV HHHHHHHCCHHHHHH	45.06	21890473
232	Phosphorylation	DHLRGEHSKAVLARS HHHCCHHHHHHHHHH	20.29	-
233	2-Hydroxyisobutyrylation	HLRGEHSKAVLARSK HHCCHHHHHHHHHHH	44.41	-
233	Ubiquitination	HLRGEHSKAVLARSK HHCCHHHHHHHHHHH	44.41	33845483
237	Ubiquitination	EHSKAVLARSKLESL HHHHHHHHHHHHHHH	13.70	32015554
240	Acetylation	KAVLARSKLESLCRE HHHHHHHHHHHHHHH	51.20	25953088
240	Ubiquitination	KAVLARSKLESLCRE HHHHHHHHHHHHHHH	51.20	23000965
243	Phosphorylation	LARSKLESLCRELQR HHHHHHHHHHHHHHH	43.11	24719451
243	Ubiquitination	LARSKLESLCRELQR HHHHHHHHHHHHHHH	43.11	21890473
245	Glutathionylation	RSKLESLCRELQRHN HHHHHHHHHHHHHHC	4.41	22555962
246	Ubiquitination	SKLESLCRELQRHNR HHHHHHHHHHHHHCH	53.61	23000965
248	Ubiquitination	LESLCRELQRHNRSL HHHHHHHHHHHCHHH	2.54	23000965
249	Ubiquitination	ESLCRELQRHNRSLK HHHHHHHHHHCHHHH	39.57	23000965
252	Ubiquitination	CRELQRHNRSLKEEG HHHHHHHCHHHHHHH	37.11	23000965
254	Phosphorylation	ELQRHNRSLKEEGVQ HHHHHCHHHHHHHHH	49.46	28857561
256	2-Hydroxyisobutyrylation	QRHNRSLKEEGVQRA HHHCHHHHHHHHHHH	55.77	-
256	Acetylation	QRHNRSLKEEGVQRA HHHCHHHHHHHHHHH	55.77	26051181
256	Ubiquitination	QRHNRSLKEEGVQRA HHHCHHHHHHHHHHH	55.77	24816145
261	Ubiquitination	SLKEEGVQRAREEEE HHHHHHHHHHHHHHH	44.14	23000965
263	Ubiquitination	KEEGVQRAREEEEKR HHHHHHHHHHHHHHH	13.22	23000965
264	Ubiquitination	EEGVQRAREEEEKRK HHHHHHHHHHHHHHH	54.79	23000965
267	Ubiquitination	VQRAREEEEKRKEVT HHHHHHHHHHHHHHH	65.15	23000965
273	Ubiquitination	EEEKRKEVTSHFQVT HHHHHHHHHHHHEEH	8.15	23000965
280	Ubiquitination	VTSHFQVTLNDIQLQ HHHHHEEHHHHHHHH	14.73	24816145
289	Ubiquitination	NDIQLQMEQHNERNS HHHHHHHHHHHHHHH	35.41	24816145
295	Ubiquitination	MEQHNERNSKLRQEN HHHHHHHHHHHHHHH	37.00	24816145
303	Sulfoxidation	SKLRQENMELAERLK HHHHHHHHHHHHHHH	4.37	21406390
308	Methylation	ENMELAERLKKLIEQ HHHHHHHHHHHHHHH	46.32	115919185
310	Ubiquitination	MELAERLKKLIEQYE HHHHHHHHHHHHHHH	52.32	23000965
311	Acetylation	ELAERLKKLIEQYEL HHHHHHHHHHHHHHH	60.33	24885699
311	Ubiquitination	ELAERLKKLIEQYEL HHHHHHHHHHHHHHH	60.33	23000965
325	2-Hydroxyisobutyrylation	LREEHIDKVFKHKDL HHHHHHHHHHCCHHH	49.30	-
325	Acetylation	LREEHIDKVFKHKDL HHHHHHHHHHCCHHH	49.30	23236377
325	Ubiquitination	LREEHIDKVFKHKDL HHHHHHHHHHCCHHH	49.30	-
330	Ubiquitination	IDKVFKHKDLQQQLV HHHHHCCHHHHHHHH	61.80	33845483
340	2-Hydroxyisobutyrylation	QQQLVDAKLQQAQEM HHHHHHHHHHHHHHH	42.22	-
340	Acetylation	QQQLVDAKLQQAQEM HHHHHHHHHHHHHHH	42.22	27452117
340	Phosphorylation	QQQLVDAKLQQAQEM HHHHHHHHHHHHHHH	42.22	33259812
340	Ubiquitination	QQQLVDAKLQQAQEM HHHHHHHHHHHHHHH	42.22	32015554
343	Ubiquitination	LVDAKLQQAQEMLKE HHHHHHHHHHHHHHH	56.29	23000965
344	Ubiquitination	VDAKLQQAQEMLKEA HHHHHHHHHHHHHHH	8.37	23000965
347	Sulfoxidation	KLQQAQEMLKEAEER HHHHHHHHHHHHHHH	4.27	21406390
349	Ubiquitination	QQAQEMLKEAEERHQ HHHHHHHHHHHHHHH	54.27	32015554
364	Ubiquitination	REKDFLLKEAVESQR HHHHHHHHHHHHHHH	45.86	32015554
377	Acetylation	QRMCELMKQQETHLK HHHHHHHHHHHHHHH	62.55	25953088
377	Ubiquitination	QRMCELMKQQETHLK HHHHHHHHHHHHHHH	62.55	32015554
393	Acetylation	QLALYTEKFEEFQNT HHHHHHHHHHHHHHH	50.72	26051181
393	Ubiquitination	QLALYTEKFEEFQNT HHHHHHHHHHHHHHH	50.72	32015554
397	Ubiquitination	YTEKFEEFQNTLSKS HHHHHHHHHHHHHHC	5.52	24816145
403	Ubiquitination	EFQNTLSKSSEVFTT HHHHHHHHCHHHHHH	62.20	21906983
412	Acetylation	SEVFTTFKQEMEKMT HHHHHHHHHHHHHHH	43.17	26822725
412	Ubiquitination	SEVFTTFKQEMEKMT HHHHHHHHHHHHHHH	43.17	32015554
419	Phosphorylation	KQEMEKMTKKIKKLE HHHHHHHHHHHHHHH	40.01	22817900
421	Acetylation	EMEKMTKKIKKLEKE HHHHHHHHHHHHHHH	51.06	12436313
421	Ubiquitination	EMEKMTKKIKKLEKE HHHHHHHHHHHHHHH	51.06	23000965
423	Ubiquitination	EKMTKKIKKLEKETT HHHHHHHHHHHHHHH	61.25	23000965
424	Ubiquitination	KMTKKIKKLEKETTM HHHHHHHHHHHHHHH	66.41	23000965
427	Acetylation	KKIKKLEKETTMYRS HHHHHHHHHHHHHHH	71.45	25953088
427	Ubiquitination	KKIKKLEKETTMYRS HHHHHHHHHHHHHHH	71.45	23000965
436	Ubiquitination	TTMYRSRWESSNKAL HHHHHHHHHHHHHHH	15.86	21890473
441	Ubiquitination	SRWESSNKALLEMAE HHHHHHHHHHHHHHH	42.21	29967540
451	Phosphorylation	LEMAEEKTVRDKELE HHHHHHHCCCHHHHH	24.85	27135362
454	Ubiquitination	AEEKTVRDKELEGLQ HHHHCCCHHHHHHHH	44.43	23000965
455	2-Hydroxyisobutyrylation	EEKTVRDKELEGLQV HHHCCCHHHHHHHHH	54.34	-
455	Acetylation	EEKTVRDKELEGLQV HHHCCCHHHHHHHHH	54.34	25953088
455	Ubiquitination	EEKTVRDKELEGLQV HHHCCCHHHHHHHHH	54.34	24816145
456	Ubiquitination	EKTVRDKELEGLQVK HHCCCHHHHHHHHHH	57.24	23000965
457	Ubiquitination	KTVRDKELEGLQVKI HCCCHHHHHHHHHHH	8.56	23000965
460	Ubiquitination	RDKELEGLQVKIQRL CHHHHHHHHHHHHHH	3.75	23000965
463	2-Hydroxyisobutyrylation	ELEGLQVKIQRLEKL HHHHHHHHHHHHHHH	21.84	-
463	Acetylation	ELEGLQVKIQRLEKL HHHHHHHHHHHHHHH	21.84	25953088
463	Ubiquitination	ELEGLQVKIQRLEKL HHHHHHHHHHHHHHH	21.84	29967540
469	Acetylation	VKIQRLEKLCRALQT HHHHHHHHHHHHHHH	58.44	26051181
488	Ubiquitination	LNKRVQDLSAGGQGS HHHHHHHHHCCCCCC	1.80	24816145
489	Phosphorylation	NKRVQDLSAGGQGSL HHHHHHHHCCCCCCC	32.91	28152594
495	Phosphorylation	LSAGGQGSLTDSGPE HHCCCCCCCCCCCCC	21.87	25159151
497	Phosphorylation	AGGQGSLTDSGPERR CCCCCCCCCCCCCCC	29.80	25159151
499	Phosphorylation	GQGSLTDSGPERRPE CCCCCCCCCCCCCCC	51.52	21082442
514	Phosphorylation	GPGAQAPSSPRVTEA CCCCCCCCCCCCCCC	56.86	29255136
515	Phosphorylation	PGAQAPSSPRVTEAP CCCCCCCCCCCCCCC	18.70	29255136
519	O-linked_Glycosylation	APSSPRVTEAPCYPG CCCCCCCCCCCCCCC	27.92	23301498
519	Phosphorylation	APSSPRVTEAPCYPG CCCCCCCCCCCCCCC	27.92	25159151
523	Glutathionylation	PRVTEAPCYPGAPST CCCCCCCCCCCCCCC	9.14	22555962
524	Phosphorylation	RVTEAPCYPGAPSTE CCCCCCCCCCCCCCC	12.02	28464451
529	Phosphorylation	PCYPGAPSTEASGQT CCCCCCCCCCCCCCC	38.04	26074081
530	Phosphorylation	CYPGAPSTEASGQTG CCCCCCCCCCCCCCC	34.21	28464451
533	Phosphorylation	GAPSTEASGQTGPQE CCCCCCCCCCCCCCC	25.79	26074081
536	Phosphorylation	STEASGQTGPQEPTS CCCCCCCCCCCCCCC	55.12	26074081
542	Phosphorylation	QTGPQEPTSARA--- CCCCCCCCCCCC---	33.98	23186163
543	Phosphorylation	TGPQEPTSARA---- CCCCCCCCCCC----	26.86	29978859

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 TXLNA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NACAM_HUMAN	NACA	physical	21903422
NACA_HUMAN	NACA	physical	21903422
TXLNB_HUMAN	TXLNB	physical	21903422
TBK1_HUMAN	TBK1	physical	21903422
TXLNG_HUMAN	TXLNG	physical	21903422
XRN2_HUMAN	XRN2	physical	22939629
UFD1_HUMAN	UFD1L	physical	22939629
WIPI2_HUMAN	WIPI2	physical	22939629
TXLNG_HUMAN	TXLNG	physical	22939629
TXLNA_HUMAN	TXLNA	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
NSE2_HUMAN	NSMCE2	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
CUL3_HUMAN	CUL3	physical	26344197
DDX17_HUMAN	DDX17	physical	26344197
DHX15_HUMAN	DHX15	physical	26344197
FUS_HUMAN	FUS	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
TXLNG_HUMAN	TXLNG	physical	28514442
TBK1_HUMAN	TBK1	physical	28514442
CA122_HUMAN	C1orf122	physical	28514442
GFOD2_HUMAN	GFOD2	physical	28514442
IFT74_HUMAN	IFT74	physical	28514442

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 TXLNA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-515, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASSSPECTROMETRY.	19369195 [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 SER-19 AND SER-515, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-515, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-18 AND SER-19, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-515, AND MASSSPECTROMETRY.	17287340 [Abstract]