dbPTM

STRAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STRAP_HUMAN
UniProt AC	Q9Y3F4
Protein Name	Serine-threonine kinase receptor-associated protein
Gene Name	STRAP
Organism	Homo sapiens (Human).
Sequence Length	350
Subcellular Localization	Cytoplasm. Nucleus. Localized predominantly in the cytoplasm but also found in the nucleus.
Protein Description	The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein..
Protein Sequence	MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSEDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLDPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETTEEELEEIASENSDCIFPSAPDVKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Phosphorylation	DLAFSGITPYGYFLI EEEECCCCCCEEEEE	17.62	28985074
28	Phosphorylation	AFSGITPYGYFLISA EECCCCCCEEEEEEE	18.79	28985074
30	Phosphorylation	SGITPYGYFLISACK CCCCCCEEEEEEEEC	6.86	28985074
40	Ubiquitination	ISACKDGKPMLRQGD EEEECCCCCCCCCCC	37.07	-
40	Malonylation	ISACKDGKPMLRQGD EEEECCCCCCCCCCC	37.07	26320211
59	Ubiquitination	IGTFLGHKGAVWGAT HHHHHCCCCCEEEEE	46.93	21906983
69	Ubiquitination	VWGATLNKDATKAAT EEEEECCHHHHHHHH	52.43	-
73	Ubiquitination	TLNKDATKAATAAAD ECCHHHHHHHHHHHH	37.43	21906983
73	2-Hydroxyisobutyrylation	TLNKDATKAATAAAD ECCHHHHHHHHHHHH	37.43	-
82	Phosphorylation	ATAAADFTAKVWDAV HHHHHHHHHHHHHHC	26.56	23403867
82	Ubiquitination	ATAAADFTAKVWDAV HHHHHHHHHHHHHHC	26.56	-
86	Ubiquitination	ADFTAKVWDAVSGDE HHHHHHHHHHCCHHH	6.27	-
90	Phosphorylation	AKVWDAVSGDELMTL HHHHHHCCHHHHHHH	42.10	28348404
100	Ubiquitination	ELMTLAHKHIVKTVD HHHHHHHHCEEEEEE	29.44	21890473
100	Acetylation	ELMTLAHKHIVKTVD HHHHHHHHCEEEEEE	29.44	25953088
104	Acetylation	LAHKHIVKTVDFTQD HHHHCEEEEEECCCC	42.08	23954790
104	Malonylation	LAHKHIVKTVDFTQD HHHHCEEEEEECCCC	42.08	26320211
104	2-Hydroxyisobutyrylation	LAHKHIVKTVDFTQD HHHHCEEEEEECCCC	42.08	-
104	Ubiquitination	LAHKHIVKTVDFTQD HHHHCEEEEEECCCC	42.08	-
109	Phosphorylation	IVKTVDFTQDSNYLL EEEEEECCCCCCCEE	27.31	29449344
112	Phosphorylation	TVDFTQDSNYLLTGG EEECCCCCCCEEECC	19.98	28152594
114	Nitration	DFTQDSNYLLTGGQD ECCCCCCCEEECCCC	13.67	-
114	Phosphorylation	DFTQDSNYLLTGGQD ECCCCCCCEEECCCC	13.67	28152594
117	Ubiquitination	QDSNYLLTGGQDKLL CCCCCEEECCCCEEE	36.35	-
117	Phosphorylation	QDSNYLLTGGQDKLL CCCCCEEECCCCEEE	36.35	28152594
122	2-Hydroxyisobutyrylation	LLTGGQDKLLRIYDL EEECCCCEEEEEEEC	41.35	-
122	Ubiquitination	LLTGGQDKLLRIYDL EEECCCCEEEEEEEC	41.35	21890473
122	Acetylation	LLTGGQDKLLRIYDL EEECCCCEEEEEEEC	41.35	23954790
125	Methylation	GGQDKLLRIYDLNKP CCCCEEEEEEECCCC	35.54	115917973
127	Phosphorylation	QDKLLRIYDLNKPEA CCEEEEEEECCCCCC	14.14	28152594
131	Acetylation	LRIYDLNKPEAEPKE EEEEECCCCCCCCCC	52.08	26051181
131	Ubiquitination	LRIYDLNKPEAEPKE EEEEECCCCCCCCCC	52.08	21906983
135	Ubiquitination	DLNKPEAEPKEISGH ECCCCCCCCCCCCCC	56.07	21890473
137	Ubiquitination	NKPEAEPKEISGHTS CCCCCCCCCCCCCCH	60.22	-
137	Acetylation	NKPEAEPKEISGHTS CCCCCCCCCCCCCCH	60.22	23236377
140	Phosphorylation	EAEPKEISGHTSGIK CCCCCCCCCCCHHHH	26.13	20068231
143	Phosphorylation	PKEISGHTSGIKKAL CCCCCCCCHHHHHEE	31.97	20068231
144	Ubiquitination	KEISGHTSGIKKALW CCCCCCCHHHHHEEE	32.61	21890473
144	Phosphorylation	KEISGHTSGIKKALW CCCCCCCHHHHHEEE	32.61	20068231
147	2-Hydroxyisobutyrylation	SGHTSGIKKALWCSE CCCCHHHHHEEEECC	35.20	-
147	Ubiquitination	SGHTSGIKKALWCSE CCCCHHHHHEEEECC	35.20	-
148	Ubiquitination	GHTSGIKKALWCSED CCCHHHHHEEEECCC	46.95	-
152	S-palmitoylation	GIKKALWCSEDKQIL HHHHEEEECCCCEEE	3.12	29575903
156	Ubiquitination	ALWCSEDKQILSADD EEEECCCCEEECCCC	34.88	21890473
156	Acetylation	ALWCSEDKQILSADD EEEECCCCEEECCCC	34.88	26822725
156	2-Hydroxyisobutyrylation	ALWCSEDKQILSADD EEEECCCCEEECCCC	34.88	-
164	Ubiquitination	QILSADDKTVRLWDH EEECCCCCCEEEECC	49.84	-
164	Acetylation	QILSADDKTVRLWDH EEECCCCCCEEEECC	49.84	25953088
164	2-Hydroxyisobutyrylation	QILSADDKTVRLWDH EEECCCCCCEEEECC	49.84	-
165	Phosphorylation	ILSADDKTVRLWDHA EECCCCCCEEEECCC	20.18	24719451
173	Phosphorylation	VRLWDHATMTEVKSL EEEECCCCHHEEEEC	22.62	21406692
175	Phosphorylation	LWDHATMTEVKSLNF EECCCCHHEEEECCC	33.02	21148321
179	Phosphorylation	ATMTEVKSLNFNMSV CCHHEEEECCCCCCE	33.45	21148321
219	Phosphorylation	VSLDPIKSFEAPATI CCCCCCCCCCCCEEE	29.10	22199227
225	Phosphorylation	KSFEAPATINSASLH CCCCCCEEECCCCCC	21.45	21406692
228	Phosphorylation	EAPATINSASLHPEK CCCEEECCCCCCCCC	18.51	-
235	Acetylation	SASLHPEKEFLVAGG CCCCCCCCEEEEECC	59.21	26051181
235	Ubiquitination	SASLHPEKEFLVAGG CCCCCCCCEEEEECC	59.21	21890473
235	2-Hydroxyisobutyrylation	SASLHPEKEFLVAGG CCCCCCCCEEEEECC	59.21	-
246	Sumoylation	VAGGEDFKLYKYDYN EECCCCEEEEEECCC	64.33	-
248	Ubiquitination	GGEDFKLYKYDYNSG CCCCEEEEEECCCCC	14.21	21890473
249	Acetylation	GEDFKLYKYDYNSGE CCCEEEEEECCCCCC	41.92	26822725
249	Ubiquitination	GEDFKLYKYDYNSGE CCCEEEEEECCCCCC	41.92	2190698
250	Phosphorylation	EDFKLYKYDYNSGEE CCEEEEEECCCCCCC	15.31	28152594
252	Phosphorylation	FKLYKYDYNSGEELE EEEEEECCCCCCCHH	14.24	28152594
254	Phosphorylation	LYKYDYNSGEELESY EEEECCCCCCCHHHC	41.16	-
262	Ubiquitination	GEELESYKGHFGPIH CCCHHHCCCCCCCEE	56.01	-
262	Ubiquitination	GEELESYKGHFGPIH CCCHHHCCCCCCCEE	56.01	21890473
262	Malonylation	GEELESYKGHFGPIH CCCHHHCCCCCCCEE	56.01	26320211
262	2-Hydroxyisobutyrylation	GEELESYKGHFGPIH CCCHHHCCCCCCCEE	56.01	-
262	Acetylation	GEELESYKGHFGPIH CCCHHHCCCCCCCEE	56.01	23749302
272	Methylation	FGPIHCVRFSPDGEL CCCEEEEEECCCCCE	31.55	115917977
282	Phosphorylation	PDGELYASGSEDGTL CCCCEEECCCCCCCE	29.33	-
290	Methylation	GSEDGTLRLWQTVVG CCCCCCEEEEEEECC	33.45	115917981
298	Acetylation	LWQTVVGKTYGLWKC EEEEECCCCCEEEEE	27.28	26051181
298	Ubiquitination	LWQTVVGKTYGLWKC EEEEECCCCCEEEEE	27.28	-
300	Phosphorylation	QTVVGKTYGLWKCVL EEECCCCCEEEEEEC	17.44	-
304	Acetylation	GKTYGLWKCVLPEED CCCCEEEEEECCCCC	21.36	26051181
304	Ubiquitination	GKTYGLWKCVLPEED CCCCEEEEEECCCCC	21.36	-
305	Glutathionylation	KTYGLWKCVLPEEDS CCCEEEEEECCCCCC	2.28	22555962
311	Ubiquitination	KCVLPEEDSGELAKP EEECCCCCCCCCCCC	61.35	-
312	Phosphorylation	CVLPEEDSGELAKPK EECCCCCCCCCCCCC	37.13	30266825
317	Ubiquitination	EDSGELAKPKIGFPE CCCCCCCCCCCCCCC	60.51	-
317	Acetylation	EDSGELAKPKIGFPE CCCCCCCCCCCCCCC	60.51	25953088
319	Ubiquitination	SGELAKPKIGFPETT CCCCCCCCCCCCCCC	55.55	-
325	Phosphorylation	PKIGFPETTEEELEE CCCCCCCCCHHHHHH	39.48	18669648
326	Phosphorylation	KIGFPETTEEELEEI CCCCCCCCHHHHHHH	39.47	18669648
330	Ubiquitination	PETTEEELEEIASEN CCCCHHHHHHHHHHC	8.94	-
335	Phosphorylation	EELEEIASENSDCIF HHHHHHHHHCCCCCC	42.86	26503892
338	Phosphorylation	EEIASENSDCIFPSA HHHHHHCCCCCCCCC	29.79	26503892
340	Glutathionylation	IASENSDCIFPSAPD HHHHCCCCCCCCCCC	3.29	22555962
344	Phosphorylation	NSDCIFPSAPDVKA- CCCCCCCCCCCCCC-	41.50	20873877

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
175	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
179	S	Phosphorylation	Kinase	MAP3K5	Q99683	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGFR1_HUMAN	TGFBR1	physical	9856985
TGFR2_HUMAN	TGFBR2	physical	9856985
SMAD7_HUMAN	SMAD7	genetic	10757800
SMAD6_HUMAN	SMAD6	physical	10757800
SMAD7_HUMAN	SMAD7	physical	10757800
STRAP_HUMAN	STRAP	physical	10757800
TGFR1_HUMAN	TGFBR1	physical	10757800
SMAD2_HUMAN	SMAD2	physical	10757800
SMAD3_HUMAN	SMAD3	physical	10757800
NDKA_HUMAN	NME1	physical	17314099
STRAP_HUMAN	STRAP	physical	17314099
SMAD7_HUMAN	SMAD7	physical	17314099
GSK3B_HUMAN	GSK3B	physical	21502811
AXIN1_HUMAN	AXIN1	physical	21502811
NOTC3_HUMAN	NOTCH3	physical	21502811
ACOC_HUMAN	ACO1	physical	22863883
CAZA1_HUMAN	CAPZA1	physical	22863883
CAZA2_HUMAN	CAPZA2	physical	22863883
SMAD3_HUMAN	SMAD3	genetic	10757800
PYRG1_HUMAN	CTPS1	physical	26344197
PLCG1_HUMAN	PLCG1	physical	26344197
UBA6_HUMAN	UBA6	physical	26344197
SMN_HUMAN	SMN1	physical	26496610
CSDE1_HUMAN	CSDE1	physical	26496610
DDX20_HUMAN	DDX20	physical	26496610
LAR4B_HUMAN	LARP4B	physical	26496610
SZRD1_HUMAN	SZRD1	physical	26496610
RAPH1_HUMAN	RAPH1	physical	26496610
GEMI7_HUMAN	GEMIN7	physical	26496610
GEMI6_HUMAN	GEMIN6	physical	26496610
PLBL2_HUMAN	PLBD2	physical	26496610
SP1_HUMAN	SP1	physical	25483064
LARP6_HUMAN	LARP6	physical	28514442
SZRD1_HUMAN	SZRD1	physical	28514442
ZNFX1_HUMAN	ZNFX1	physical	28514442
CSDE1_HUMAN	CSDE1	physical	28514442
GEMI7_HUMAN	GEMIN7	physical	28514442
RPRD2_HUMAN	RPRD2	physical	28514442
CDKA1_HUMAN	CDK2AP1	physical	28514442
PYC_HUMAN	PC	physical	28514442
GEMI5_HUMAN	GEMIN5	physical	28514442
TSN_HUMAN	TSN	physical	28514442
CK068_HUMAN	C11orf68	physical	28514442
GEMI2_HUMAN	GEMIN2	physical	28514442
GEMI4_HUMAN	GEMIN4	physical	28514442
RPR1B_HUMAN	RPRD1B	physical	28514442
LS14A_HUMAN	LSM14A	physical	28514442
SPT6H_HUMAN	SUPT6H	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 STRAP_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-335 AND SER-338, ANDMASS SPECTROMETRY.	18669648 [Abstract]