dbPTM

SLAI2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SLAI2_HUMAN
UniProt AC	Q9P270
Protein Name	SLAIN motif-containing protein 2
Gene Name	SLAIN2
Organism	Homo sapiens (Human).
Sequence Length	581
Subcellular Localization	Cytoplasm, cytoskeleton. Colocalizes with microtubules. Detected at the plus end of growing microtubules.
Protein Description	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase..
Protein Sequence	MEDVNSNVNADQEVRKLQELVKKLEKQNEQLRSRSGAVQGAGSLGPGSPVRAGASIPSSGAASPRGFPLGLSAKSGGGPGSGPRRTSSEELRDATSLLAAGEGGLLDEVEPLRPDELERLSGWEEEEESWLYSSPKKKLTPMQKSVSPLVWCRQVLDYPSPDVECAKKSLIHKLDQTMSALKRQNLYNNPFNSMSYTSPYSPNASSPYSSGFNSPSSTPVRPPIVKQLILPGNSGNLKSSDRNPPLSPQSSIDSELSASELDEDSIGSNYKLNDVTDVQILARMQEESLRQEYAATTSRRSSGSSCNSTRRGTFSDQELDAQSLDDEDDNMHHAVYPAVNRFSPSPRNSPRPSPKQSPRNSPRSRSPARGIEYSRVSPQPMISRLQQPRLSLQGHPTDLQTSNVKNEEKLRRSLPNLSRTSNTQVDSVKSSRSDSNFQVPNGGIPRMQPQASAIPSPGKFRSPAAPSPLALRQPVKAFSNHGSGSPGSQEITQLTQTTSSPGPPMVQSTVSANPPSNINSATLTRPAGTTAMRSGLPRPSAPSAGGIPVPRSKLAQPVRRSLPAPKTYGSMKDDSWKDGCY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDVNSNV -------CCCHHHCC	10.02	22814378
33	Phosphorylation	KQNEQLRSRSGAVQG HHHHHHHHCCCCCCC	39.11	25627689
35	Phosphorylation	NEQLRSRSGAVQGAG HHHHHHCCCCCCCCC	32.14	25159151
43	Phosphorylation	GAVQGAGSLGPGSPV CCCCCCCCCCCCCCC	29.62	23927012
48	Phosphorylation	AGSLGPGSPVRAGAS CCCCCCCCCCCCCCC	24.29	22167270
51	Methylation	LGPGSPVRAGASIPS CCCCCCCCCCCCCCC	30.59	115389093
55	Phosphorylation	SPVRAGASIPSSGAA CCCCCCCCCCCCCCC	33.83	23927012
58	Phosphorylation	RAGASIPSSGAASPR CCCCCCCCCCCCCCC	39.47	23927012
59	O-linked_Glycosylation	AGASIPSSGAASPRG CCCCCCCCCCCCCCC	27.39	30379171
59	Phosphorylation	AGASIPSSGAASPRG CCCCCCCCCCCCCCC	27.39	25159151
63	O-linked_Glycosylation	IPSSGAASPRGFPLG CCCCCCCCCCCCCCC	18.00	30379171
63	Phosphorylation	IPSSGAASPRGFPLG CCCCCCCCCCCCCCC	18.00	30266825
65	Methylation	SSGAASPRGFPLGLS CCCCCCCCCCCCCCC	57.81	115389101
72	Phosphorylation	RGFPLGLSAKSGGGP CCCCCCCCCCCCCCC	31.67	25159151
81	Phosphorylation	KSGGGPGSGPRRTSS CCCCCCCCCCCCCCH	49.08	29396449
86	Phosphorylation	PGSGPRRTSSEELRD CCCCCCCCCHHHHHH	37.57	30266825
87	Phosphorylation	GSGPRRTSSEELRDA CCCCCCCCHHHHHHH	33.66	27273156
88	Phosphorylation	SGPRRTSSEELRDAT CCCCCCCHHHHHHHH	34.18	30266825
95	Phosphorylation	SEELRDATSLLAAGE HHHHHHHHHHHHHCC	24.97	30108239
96	Phosphorylation	EELRDATSLLAAGEG HHHHHHHHHHHHCCC	24.09	30108239
132	Phosphorylation	EEEESWLYSSPKKKL HHHHHHCCCCCCCCC	10.80	22199227
133	Phosphorylation	EEESWLYSSPKKKLT HHHHHCCCCCCCCCC	37.68	22199227
134	Phosphorylation	EESWLYSSPKKKLTP HHHHCCCCCCCCCCC	27.47	25159151
140	Phosphorylation	SSPKKKLTPMQKSVS CCCCCCCCCCCCCCC	26.12	28985074
144	Acetylation	KKLTPMQKSVSPLVW CCCCCCCCCCCHHHH	46.72	7428257
145	Phosphorylation	KLTPMQKSVSPLVWC CCCCCCCCCCHHHHH	15.78	30266825
147	Phosphorylation	TPMQKSVSPLVWCRQ CCCCCCCCHHHHHHH	21.43	19664994
158	Phosphorylation	WCRQVLDYPSPDVEC HHHHHHCCCCCCHHH	11.05	30266825
160	Phosphorylation	RQVLDYPSPDVECAK HHHHCCCCCCHHHHH	27.74	30266825
177	Phosphorylation	LIHKLDQTMSALKRQ HHHHHHHHHHHHHHC	16.86	25159151
179	Phosphorylation	HKLDQTMSALKRQNL HHHHHHHHHHHHCCC	33.56	25159151
182	Methylation	DQTMSALKRQNLYNN HHHHHHHHHCCCCCC	52.21	115981123
182	Ubiquitination	DQTMSALKRQNLYNN HHHHHHHHHCCCCCC	52.21	-
197	Phosphorylation	PFNSMSYTSPYSPNA CCCCCCCCCCCCCCC	18.87	28348404
198	Phosphorylation	FNSMSYTSPYSPNAS CCCCCCCCCCCCCCC	17.38	28348404
200	Phosphorylation	SMSYTSPYSPNASSP CCCCCCCCCCCCCCC	36.21	28348404
201	Phosphorylation	MSYTSPYSPNASSPY CCCCCCCCCCCCCCC	18.30	23898821
209	Phosphorylation	PNASSPYSSGFNSPS CCCCCCCCCCCCCCC	27.63	28348404
210	Phosphorylation	NASSPYSSGFNSPSS CCCCCCCCCCCCCCC	41.37	28348404
214	Phosphorylation	PYSSGFNSPSSTPVR CCCCCCCCCCCCCCC	24.73	28348404
234	Phosphorylation	QLILPGNSGNLKSSD EEECCCCCCCCCCCC	34.67	25159151
239	Phosphorylation	GNSGNLKSSDRNPPL CCCCCCCCCCCCCCC	40.41	30266825
240	Phosphorylation	NSGNLKSSDRNPPLS CCCCCCCCCCCCCCC	38.72	30266825
247	Phosphorylation	SDRNPPLSPQSSIDS CCCCCCCCCCHHHCC	27.02	30266825
250	Phosphorylation	NPPLSPQSSIDSELS CCCCCCCHHHCCCCC	32.42	30266825
251	Phosphorylation	PPLSPQSSIDSELSA CCCCCCHHHCCCCCH	25.76	30266825
254	Phosphorylation	SPQSSIDSELSASEL CCCHHHCCCCCHHHC	38.47	30266825
257	Phosphorylation	SSIDSELSASELDED HHHCCCCCHHHCCCC	26.20	30266825
259	Phosphorylation	IDSELSASELDEDSI HCCCCCHHHCCCCCC	35.00	30266825
265	Phosphorylation	ASELDEDSIGSNYKL HHHCCCCCCCCCCCC	27.14	30266825
268	Phosphorylation	LDEDSIGSNYKLNDV CCCCCCCCCCCCCCC	35.00	28450419
270	Phosphorylation	EDSIGSNYKLNDVTD CCCCCCCCCCCCCCH	20.67	28450419
276	Phosphorylation	NYKLNDVTDVQILAR CCCCCCCCHHHHHHH	33.06	28555341
288	Phosphorylation	LARMQEESLRQEYAA HHHHHHHHHHHHHHH	28.27	28796482
293	Phosphorylation	EESLRQEYAATTSRR HHHHHHHHHHHHCCC	8.00	28796482
296	Phosphorylation	LRQEYAATTSRRSSG HHHHHHHHHCCCCCC	19.68	28796482
297	Phosphorylation	RQEYAATTSRRSSGS HHHHHHHHCCCCCCC	18.60	28796482
298	Phosphorylation	QEYAATTSRRSSGSS HHHHHHHCCCCCCCC	22.72	28796482
301	Phosphorylation	AATTSRRSSGSSCNS HHHHCCCCCCCCCCC	37.63	-
302	Phosphorylation	ATTSRRSSGSSCNST HHHCCCCCCCCCCCC	40.66	-
304	Phosphorylation	TSRRSSGSSCNSTRR HCCCCCCCCCCCCCC	33.40	30576142
305	Phosphorylation	SRRSSGSSCNSTRRG CCCCCCCCCCCCCCC	22.35	30576142
308	Phosphorylation	SSGSSCNSTRRGTFS CCCCCCCCCCCCCCC	27.84	-
309	Phosphorylation	SGSSCNSTRRGTFSD CCCCCCCCCCCCCCC	15.47	-
313	Phosphorylation	CNSTRRGTFSDQELD CCCCCCCCCCCHHHC	20.39	23401153
315	Phosphorylation	STRRGTFSDQELDAQ CCCCCCCCCHHHCCC	37.92	23927012
323	Phosphorylation	DQELDAQSLDDEDDN CHHHCCCCCCCCCCC	35.17	23927012
336	Phosphorylation	DNMHHAVYPAVNRFS CCHHHHHHHHHHCCC	6.05	23927012
343	Phosphorylation	YPAVNRFSPSPRNSP HHHHHCCCCCCCCCC	22.64	22167270
345	Phosphorylation	AVNRFSPSPRNSPRP HHHCCCCCCCCCCCC	34.98	22167270
349	Phosphorylation	FSPSPRNSPRPSPKQ CCCCCCCCCCCCCCC	24.46	30266825
353	Phosphorylation	PRNSPRPSPKQSPRN CCCCCCCCCCCCCCC	46.11	30266825
357	Phosphorylation	PRPSPKQSPRNSPRS CCCCCCCCCCCCCCC	31.77	22167270
361	Phosphorylation	PKQSPRNSPRSRSPA CCCCCCCCCCCCCCC	23.99	23403867
364	Phosphorylation	SPRNSPRSRSPARGI CCCCCCCCCCCCCCC	40.26	23403867
366	Phosphorylation	RNSPRSRSPARGIEY CCCCCCCCCCCCCCC	24.94	30183078
373	Phosphorylation	SPARGIEYSRVSPQP CCCCCCCCCCCCCCC	10.39	23927012
374	Phosphorylation	PARGIEYSRVSPQPM CCCCCCCCCCCCCCC	17.26	23401153
377	Phosphorylation	GIEYSRVSPQPMISR CCCCCCCCCCCCHHH	19.39	23401153
383	Phosphorylation	VSPQPMISRLQQPRL CCCCCCHHHHCCCCH	22.23	23403867
391	Phosphorylation	RLQQPRLSLQGHPTD HHCCCCHHHCCCCCC	21.67	25159151
397	Phosphorylation	LSLQGHPTDLQTSNV HHHCCCCCCHHCCCC	43.60	23927012
401	Phosphorylation	GHPTDLQTSNVKNEE CCCCCHHCCCCCCHH	29.57	23927012
402	Phosphorylation	HPTDLQTSNVKNEEK CCCCHHCCCCCCHHH	27.02	23927012
413	Phosphorylation	NEEKLRRSLPNLSRT CHHHHHHHCCCCCCC	41.57	22167270
418	Phosphorylation	RRSLPNLSRTSNTQV HHHCCCCCCCCCCCC	39.90	23927012
427	Phosphorylation	TSNTQVDSVKSSRSD CCCCCCCCCCCCCCC	32.37	28857561
430	Phosphorylation	TQVDSVKSSRSDSNF CCCCCCCCCCCCCCC	28.91	23401153
431	Phosphorylation	QVDSVKSSRSDSNFQ CCCCCCCCCCCCCCC	30.04	28450419
433	Phosphorylation	DSVKSSRSDSNFQVP CCCCCCCCCCCCCCC	47.54	30266825
435	Phosphorylation	VKSSRSDSNFQVPNG CCCCCCCCCCCCCCC	40.57	30266825
452	Phosphorylation	PRMQPQASAIPSPGK CCCCCCCCCCCCCCC	22.83	30266825
456	Phosphorylation	PQASAIPSPGKFRSP CCCCCCCCCCCCCCC	39.92	30266825
459	Acetylation	SAIPSPGKFRSPAAP CCCCCCCCCCCCCCC	40.77	25953088
462	Phosphorylation	PSPGKFRSPAAPSPL CCCCCCCCCCCCCCC	23.25	30266825
467	Phosphorylation	FRSPAAPSPLALRQP CCCCCCCCCCHHCCC	28.02	30266825
472	Methylation	APSPLALRQPVKAFS CCCCCHHCCCCHHHC	32.90	54559353
534	Phosphorylation	AGTTAMRSGLPRPSA CCCCHHHCCCCCCCC	31.43	28555341
538	Methylation	AMRSGLPRPSAPSAG HHHCCCCCCCCCCCC	42.73	58859569
540	Phosphorylation	RSGLPRPSAPSAGGI HCCCCCCCCCCCCCC	54.83	27251275
543	Phosphorylation	LPRPSAPSAGGIPVP CCCCCCCCCCCCCCC	38.98	28555341
551	Methylation	AGGIPVPRSKLAQPV CCCCCCCHHHCCCCH	46.81	24129315
553	Methylation	GIPVPRSKLAQPVRR CCCCCHHHCCCCHHH	49.47	24129315
561	Phosphorylation	LAQPVRRSLPAPKTY CCCCHHHCCCCCCCC	28.30	24719451
570	Phosphorylation	PAPKTYGSMKDDSWK CCCCCCCCCCCCCCC	16.55	27251275
581	Phosphorylation	DSWKDGCY------- CCCCCCCC-------	27.41	-

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
48	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SLAI2_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 SLAI2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ARBK1_HUMAN	ADRBK1	physical	26496610
JARD2_HUMAN	JARID2	physical	26496610
P4HA1_HUMAN	P4HA1	physical	26496610
PCM1_HUMAN	PCM1	physical	26496610
TRI27_HUMAN	TRIM27	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
YBOX3_HUMAN	YBX3	physical	26496610
FXR2_HUMAN	FXR2	physical	26496610
CKAP5_HUMAN	CKAP5	physical	26496610
TRIB1_HUMAN	TRIB1	physical	26496610
TACC3_HUMAN	TACC3	physical	26496610
APBP2_HUMAN	APPBP2	physical	26496610
TACC2_HUMAN	TACC2	physical	26496610
SRS10_HUMAN	SRSF10	physical	26496610
CP131_HUMAN	CEP131	physical	26496610
MYCB2_HUMAN	MYCBP2	physical	26496610
NNTM_HUMAN	NNT	physical	26496610
PRDX5_HUMAN	PRDX5	physical	26496610
S18L2_HUMAN	SS18L2	physical	26496610
WAC_HUMAN	WAC	physical	26496610
FOCAD_HUMAN	FOCAD	physical	26496610
BRE1A_HUMAN	RNF20	physical	26496610
CDT1_HUMAN	CDT1	physical	26496610
YTDC1_HUMAN	YTHDC1	physical	26496610
SYTC2_HUMAN	TARSL2	physical	26496610
FOPNL_HUMAN	FOPNL	physical	26496610
LYSM2_HUMAN	LYSMD2	physical	26496610
MZT2A_HUMAN	MZT2A	physical	26496610
CCD61_HUMAN	CCDC61	physical	26496610
CKAP5_HUMAN	CKAP5	physical	28514442
TACC3_HUMAN	TACC3	physical	28514442
TTC19_HUMAN	TTC19	physical	28514442
PCDAA_HUMAN	PCDHA10	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 SLAI2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-48; SER-63 AND SER-433,AND MASS SPECTROMETRY.	19690332 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.	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-43; SER-48; SER-55;SER-63; SER-147; SER-179; SER-247; SER-250; SER-251; SER-254; SER-257;SER-315; SER-323; SER-377; SER-413; SER-456; SER-462 AND SER-467, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-48; SER-63;SER-147; SER-160; SER-234 AND SER-467, AND MASS SPECTROMETRY.	16964243 [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-418, AND MASSSPECTROMETRY.	17081983 [Abstract]