dbPTM

RBM14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM14_HUMAN
UniProt AC	Q96PK6
Protein Name	RNA-binding protein 14
Gene Name	RBM14
Organism	Homo sapiens (Human).
Sequence Length	669
Subcellular Localization	Nucleus . Nucleus, nucleolus . Cytoplasm . In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles (PubMed:11790299). Cytoplasmic localization is crucial for its function in suppressing the formation of aber
Protein Description	Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1. [PubMed: 11443112 Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CENPJ complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CENPJ]
Protein Sequence	MKIFVGNVDGADTTPEELAALFAPYGTVMSCAVMKQFAFVHMRENAGALRAIEALHGHELRPGRALVVEMSRPRPLNTWKIFVGNVSAACTSQELRSLFERRGRVIECDVVKDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPGLAVQSGDKTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPPRASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMTAQAASYRAQPSVSLGAPYRGQLASPSSQSAAASSLGPYGGAQPSASALSSYGGQAAAASSLNSYGAQGSSLASYGNQPSSYGAQAASSYGVRAAASSYNTQGAASSLGSYGAQAASYGAQSAASSLAYGAQAASYNAQPSASYNAQSAPYAAQQAASYSSQPAAYVAQPATAAAYASQPAAYAAQATTPMAGSYGAQPVVQTQLNSYGAQASMGLSGSYGAQSAAAATGSYGAAAAYGAQPSATLAAPYRTQSSASLAASYAAQQHPQAAASYRGQPGNAYDGAGQPSAAYLSMSQGAVANANSTPPPYERTRLSPPRASYDDPYKKAVAMSKRYGSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYNDYLRAAQMHSGYQRRM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Sumoylation	------MKIFVGNVD ------CEEEECCCC	44.87	-
13	Phosphorylation	GNVDGADTTPEELAA CCCCCCCCCHHHHHH	43.65	26552605
14	Phosphorylation	NVDGADTTPEELAAL CCCCCCCCHHHHHHH	29.29	26552605
25	Phosphorylation	LAALFAPYGTVMSCA HHHHHCCHHHHHHHH	23.23	26552605
27	Phosphorylation	ALFAPYGTVMSCAVM HHHCCHHHHHHHHHH	13.75	26552605
30	Phosphorylation	APYGTVMSCAVMKQF CCHHHHHHHHHHHHH	8.45	26552605
70	Sulfoxidation	GRALVVEMSRPRPLN CCEEEEECCCCCCCC	2.52	21406390
87	Phosphorylation	KIFVGNVSAACTSQE EEEEECHHHHHCHHH	17.72	27251275
90	Glutathionylation	VGNVSAACTSQELRS EECHHHHHCHHHHHH	3.63	22555962
91	Phosphorylation	GNVSAACTSQELRSL ECHHHHHCHHHHHHH	28.81	30108239
92	Phosphorylation	NVSAACTSQELRSLF CHHHHHCHHHHHHHH	22.88	17525332
112	2-Hydroxyisobutyrylation	VIECDVVKDYAFVHM EEECEEECCEEEEEE	44.89	-
112	Acetylation	VIECDVVKDYAFVHM EEECEEECCEEEEEE	44.89	25825284
112	Ubiquitination	VIECDVVKDYAFVHM EEECEEECCEEEEEE	44.89	22505724
114	Phosphorylation	ECDVVKDYAFVHMEK ECEEECCEEEEEECC	9.02	28796482
121	2-Hydroxyisobutyrylation	YAFVHMEKEADAKAA EEEEEECCHHHHHHH	51.10	-
121	Ubiquitination	YAFVHMEKEADAKAA EEEEEECCHHHHHHH	51.10	22817900
126	Sumoylation	MEKEADAKAAIAQLN ECCHHHHHHHHHHHC	38.61	-
126	2-Hydroxyisobutyrylation	MEKEADAKAAIAQLN ECCHHHHHHHHHHHC	38.61	-
126	Acetylation	MEKEADAKAAIAQLN ECCHHHHHHHHHHHC	38.61	25953088
126	Sumoylation	MEKEADAKAAIAQLN ECCHHHHHHHHHHHC	38.61	28112733
126	Ubiquitination	MEKEADAKAAIAQLN ECCHHHHHHHHHHHC	38.61	21906983
126 (in isoform 1)	Ubiquitination	-	38.61	21906983
126 (in isoform 2)	Ubiquitination	-	38.61	21906983
135	Sumoylation	AIAQLNGKEVKGKRI HHHHHCCCEECCEEE	59.26	-
135	Acetylation	AIAQLNGKEVKGKRI HHHHHCCCEECCEEE	59.26	23954790
135	Sumoylation	AIAQLNGKEVKGKRI HHHHHCCCEECCEEE	59.26	28112733
135	Ubiquitination	AIAQLNGKEVKGKRI HHHHHCCCEECCEEE	59.26	21906983
135 (in isoform 1)	Ubiquitination	-	59.26	21906983
135 (in isoform 2)	Ubiquitination	-	59.26	21906983
138	Sumoylation	QLNGKEVKGKRINVE HHCCCEECCEEEEEE	60.86	28112733
138	Ubiquitination	QLNGKEVKGKRINVE HHCCCEECCEEEEEE	60.86	22817900
140	Sumoylation	NGKEVKGKRINVELS CCCEECCEEEEEEEC	44.37	-
140	Ubiquitination	NGKEVKGKRINVELS CCCEECCEEEEEEEC	44.37	22817900
147	Phosphorylation	KRINVELSTKGQKKG EEEEEEECCCCCCCC	17.99	30108239
148	Phosphorylation	RINVELSTKGQKKGP EEEEEECCCCCCCCC	52.39	30108239
148 (in isoform 5)	Ubiquitination	-	52.39	-
149	Sumoylation	INVELSTKGQKKGPG EEEEECCCCCCCCCC	56.84	-
149	Acetylation	INVELSTKGQKKGPG EEEEECCCCCCCCCC	56.84	25953088
149	Malonylation	INVELSTKGQKKGPG EEEEECCCCCCCCCC	56.84	26320211
149	Sumoylation	INVELSTKGQKKGPG EEEEECCCCCCCCCC	56.84	28112733
149	Ubiquitination	INVELSTKGQKKGPG EEEEECCCCCCCCCC	56.84	27667366
152	Acetylation	ELSTKGQKKGPGLAV EECCCCCCCCCCEEE	69.25	25953088
152	Ubiquitination	ELSTKGQKKGPGLAV EECCCCCCCCCCEEE	69.25	-
153	Sumoylation	LSTKGQKKGPGLAVQ ECCCCCCCCCCEEEE	63.55	-
153	Acetylation	LSTKGQKKGPGLAVQ ECCCCCCCCCCEEEE	63.55	26051181
153	Sumoylation	LSTKGQKKGPGLAVQ ECCCCCCCCCCEEEE	63.55	28112733
153	Ubiquitination	LSTKGQKKGPGLAVQ ECCCCCCCCCCEEEE	63.55	33845483
161	Phosphorylation	GPGLAVQSGDKTKKP CCCEEEECCCCCCCC	42.22	25159151
164	2-Hydroxyisobutyrylation	LAVQSGDKTKKPGAG EEEECCCCCCCCCCC	66.81	-
164	Acetylation	LAVQSGDKTKKPGAG EEEECCCCCCCCCCC	66.81	23749302
164	Sumoylation	LAVQSGDKTKKPGAG EEEECCCCCCCCCCC	66.81	28112733
164	Ubiquitination	LAVQSGDKTKKPGAG EEEECCCCCCCCCCC	66.81	33845483
165	Phosphorylation	AVQSGDKTKKPGAGD EEECCCCCCCCCCCC	49.38	23312004
167	Sumoylation	QSGDKTKKPGAGDTA ECCCCCCCCCCCCCC	54.65	-
167	Ubiquitination	QSGDKTKKPGAGDTA ECCCCCCCCCCCCCC	54.65	-
187	Phosphorylation	GFSATFDYQQAFGNS CCEEEEEHHHHHCCC	9.80	26074081
194	Phosphorylation	YQQAFGNSTGGFDGQ HHHHHCCCCCCCCCC	28.89	26074081
195	Phosphorylation	QQAFGNSTGGFDGQA HHHHCCCCCCCCCCC	45.37	26074081
198 (in isoform 5)	Ubiquitination	-	11.46	-
206	Phosphorylation	DGQARQPTPPFFGRD CCCCCCCCCCCCCCC	34.94	29255136
215	Phosphorylation	PFFGRDRSPLRRSPP CCCCCCCCCCCCCCC	32.35	25463755
220	Phosphorylation	DRSPLRRSPPRASYV CCCCCCCCCCCCCCC	32.59	25159151
225	O-linked_Glycosylation	RRSPPRASYVAPLTA CCCCCCCCCCCCCCC	22.78	32574038
225	Phosphorylation	RRSPPRASYVAPLTA CCCCCCCCCCCCCCC	22.78	21945579
226	Phosphorylation	RSPPRASYVAPLTAQ CCCCCCCCCCCCCCC	10.31	21945579
231	O-linked_Glycosylation	ASYVAPLTAQPATYR CCCCCCCCCCCCEEC	23.37	32574038
231	Phosphorylation	ASYVAPLTAQPATYR CCCCCCCCCCCCEEC	23.37	21945579
236	Phosphorylation	PLTAQPATYRAQPSV CCCCCCCEECCCCCC	21.89	21945579
237	Phosphorylation	LTAQPATYRAQPSVS CCCCCCEECCCCCCC	13.17	21945579
238	Methylation	TAQPATYRAQPSVSL CCCCCEECCCCCCCC	23.53	115490595
242	O-linked_Glycosylation	ATYRAQPSVSLGAAY CEECCCCCCCCCCEE	16.56	32574038
242	Phosphorylation	ATYRAQPSVSLGAAY CEECCCCCCCCCCEE	16.56	21945579
244	O-linked_Glycosylation	YRAQPSVSLGAAYRA ECCCCCCCCCCEEEC	25.98	32574038
244	O-linked_Glycosylation	YRAQPSVSLGAAYRA ECCCCCCCCCCEEEC	25.98	20068230
244	Phosphorylation	YRAQPSVSLGAAYRA ECCCCCCCCCCEEEC	25.98	21945579
249	Phosphorylation	SVSLGAAYRAQPSAS CCCCCCEEECCCCCC	13.12	21945579
250	Methylation	VSLGAAYRAQPSASL CCCCCEEECCCCCCC	23.24	115490587
254	O-linked_Glycosylation	AAYRAQPSASLGVGY CEEECCCCCCCCCCC	20.57	32574038
254	O-linked_Glycosylation	AAYRAQPSASLGVGY CEEECCCCCCCCCCC	20.57	20068230
254	Phosphorylation	AAYRAQPSASLGVGY CEEECCCCCCCCCCC	20.57	30266825
256	O-linked_Glycosylation	YRAQPSASLGVGYRT EECCCCCCCCCCCCC	29.96	32574038
256	O-linked_Glycosylation	YRAQPSASLGVGYRT EECCCCCCCCCCCCC	29.96	18212344
256	Phosphorylation	YRAQPSASLGVGYRT EECCCCCCCCCCCCC	29.96	30266825
261	Phosphorylation	SASLGVGYRTQPMTA CCCCCCCCCCCCCCH	14.21	23312004
263	Phosphorylation	SLGVGYRTQPMTAQA CCCCCCCCCCCCHHH	28.65	22461510
266	Sulfoxidation	VGYRTQPMTAQAASY CCCCCCCCCHHHHHH	3.31	28183972
267	Phosphorylation	GYRTQPMTAQAASYR CCCCCCCCHHHHHHH	23.46	21945579
272	Phosphorylation	PMTAQAASYRAQPSV CCCHHHHHHHCCCCC	20.40	21945579
273	Nitration	MTAQAASYRAQPSVS CCHHHHHHHCCCCCC	12.77	-
273	Phosphorylation	MTAQAASYRAQPSVS CCHHHHHHHCCCCCC	12.77	21945579
274	Methylation	TAQAASYRAQPSVSL CHHHHHHHCCCCCCC	25.01	24381683
278	O-linked_Glycosylation	ASYRAQPSVSLGAPY HHHHCCCCCCCCCCC	16.56	32574038
278	Phosphorylation	ASYRAQPSVSLGAPY HHHHCCCCCCCCCCC	16.56	30266825
280	O-linked_Glycosylation	YRAQPSVSLGAPYRG HHCCCCCCCCCCCCC	25.98	32574038
280	O-linked_Glycosylation	YRAQPSVSLGAPYRG HHCCCCCCCCCCCCC	25.98	18212344
280	Phosphorylation	YRAQPSVSLGAPYRG HHCCCCCCCCCCCCC	25.98	30266825
285	Phosphorylation	SVSLGAPYRGQLASP CCCCCCCCCCCCCCC	27.17	20090780
286	Methylation	VSLGAPYRGQLASPS CCCCCCCCCCCCCCC	25.89	115388161
291	Phosphorylation	PYRGQLASPSSQSAA CCCCCCCCCCCCHHH	33.63	26074081
293	Phosphorylation	RGQLASPSSQSAAAS CCCCCCCCCCHHHHH	38.22	26074081
294	Phosphorylation	GQLASPSSQSAAASS CCCCCCCCCHHHHHH	31.38	26074081
296	Phosphorylation	LASPSSQSAAASSLG CCCCCCCHHHHHHCC	23.09	26074081
301	O-linked_Glycosylation	SQSAAASSLGPYGGA CCHHHHHHCCCCCCC	32.39	32574038
306	Phosphorylation	ASSLGPYGGAQPSAS HHHCCCCCCCCCCHH	28.26	24719451
316	Phosphorylation	QPSASALSSYGGQAA CCCHHHHHHCCCHHH	22.64	29496963
318	Phosphorylation	SASALSSYGGQAAAA CHHHHHHCCCHHHHH	23.15	24719451
341	Phosphorylation	QGSSLASYGNQPSSY CCCCHHHCCCCCCHH	17.94	28464451
363	O-linked_Glycosylation	YGVRAAASSYNTQGA HCCHHHHCCCCCCCH	28.73	32574038
364	O-linked_Glycosylation	GVRAAASSYNTQGAA CCHHHHCCCCCCCHH	20.06	32574038
365	Phosphorylation	VRAAASSYNTQGAAS CHHHHCCCCCCCHHH	21.53	-
367	O-linked_Glycosylation	AAASSYNTQGAASSL HHHCCCCCCCHHHHH	21.83	32574038
372	O-linked_Glycosylation	YNTQGAASSLGSYGA CCCCCHHHHHHHHHH	26.09	32574038
391	O-linked_Glycosylation	YGAQSAASSLAYGAQ HCCHHHHHHHHHHHH	26.12	32574038
392	O-linked_Glycosylation	GAQSAASSLAYGAQA CCHHHHHHHHHHHHH	16.58	32574038
438	O-linked_Glycosylation	AYVAQPATAAAYASQ EECCCCHHHHHHHCC	24.42	32574038
444	O-linked_Glycosylation	ATAAAYASQPAAYAA HHHHHHHCCHHHHHH	24.83	32574038
518	O-linked_Glycosylation	TLAAPYRTQSSASLA EECCCCCCCCHHHHH	27.28	32574038
518	Phosphorylation	TLAAPYRTQSSASLA EECCCCCCCCHHHHH	27.28	21945579
520	Phosphorylation	AAPYRTQSSASLAAS CCCCCCCCHHHHHHH	27.53	21945579
521	Phosphorylation	APYRTQSSASLAASY CCCCCCCHHHHHHHH	16.44	21945579
523	Phosphorylation	YRTQSSASLAASYAA CCCCCHHHHHHHHHH	22.08	21945579
527	O-linked_Glycosylation	SSASLAASYAAQQHP CHHHHHHHHHHHHCH	15.08	32574038
527	Phosphorylation	SSASLAASYAAQQHP CHHHHHHHHHHHHCH	15.08	21945579
528	Phosphorylation	SASLAASYAAQQHPQ HHHHHHHHHHHHCHH	10.96	21945579
539	Phosphorylation	QHPQAAASYRGQPGN HCHHHHHHHCCCCCC	15.61	21945579
540	Phosphorylation	HPQAAASYRGQPGNA CHHHHHHHCCCCCCC	17.65	21945579
548	Phosphorylation	RGQPGNAYDGAGQPS CCCCCCCCCCCCCCC	20.93	21945579
555	Phosphorylation	YDGAGQPSAAYLSMS CCCCCCCCCCCHHHC	20.04	21945579
558	Phosphorylation	AGQPSAAYLSMSQGA CCCCCCCCHHHCCCC	10.06	21945579
560	Phosphorylation	QPSAAYLSMSQGAVA CCCCCCHHHCCCCHH	12.05	21945579
562	Phosphorylation	SAAYLSMSQGAVANA CCCCHHHCCCCHHCC	23.30	21945579
571	Phosphorylation	GAVANANSTPPPYER CCHHCCCCCCCCCCC	39.62	25159151
572	Phosphorylation	AVANANSTPPPYERT CHHCCCCCCCCCCCC	39.35	25159151
576	Phosphorylation	ANSTPPPYERTRLSP CCCCCCCCCCCCCCC	24.66	21945579
579	Phosphorylation	TPPPYERTRLSPPRA CCCCCCCCCCCCCCC	24.83	30266825
582	Phosphorylation	PYERTRLSPPRASYD CCCCCCCCCCCCCCC	29.57	22167270
587	Phosphorylation	RLSPPRASYDDPYKK CCCCCCCCCCCHHHH	30.30	22617229
588	Phosphorylation	LSPPRASYDDPYKKA CCCCCCCCCCHHHHH	24.31	23898821
592	Phosphorylation	RASYDDPYKKAVAMS CCCCCCHHHHHHHHH	31.92	28102081
593	Acetylation	ASYDDPYKKAVAMSK CCCCCHHHHHHHHHH	39.38	25953088
593	Ubiquitination	ASYDDPYKKAVAMSK CCCCCHHHHHHHHHH	39.38	33845483
594	Sumoylation	SYDDPYKKAVAMSKR CCCCHHHHHHHHHHH	42.10	-
594	Acetylation	SYDDPYKKAVAMSKR CCCCHHHHHHHHHHH	42.10	26051181
594	Sumoylation	SYDDPYKKAVAMSKR CCCCHHHHHHHHHHH	42.10	-
594	Ubiquitination	SYDDPYKKAVAMSKR CCCCHHHHHHHHHHH	42.10	29967540
599	O-linked_Glycosylation	YKKAVAMSKRYGSDR HHHHHHHHHHHCCCH	12.30	32574038
600	Sumoylation	KKAVAMSKRYGSDRR HHHHHHHHHHCCCHH	36.23	-
600	2-Hydroxyisobutyrylation	KKAVAMSKRYGSDRR HHHHHHHHHHCCCHH	36.23	-
600	Acetylation	KKAVAMSKRYGSDRR HHHHHHHHHHCCCHH	36.23	25953088
600	Sumoylation	KKAVAMSKRYGSDRR HHHHHHHHHHCCCHH	36.23	28112733
600	Ubiquitination	KKAVAMSKRYGSDRR HHHHHHHHHHCCCHH	36.23	29967540
612	Phosphorylation	DRRLAELSDYRRLSE CHHHHHHHHHHHHCH	24.89	21815630
614	Phosphorylation	RLAELSDYRRLSESQ HHHHHHHHHHHCHHH	8.34	28152594
615	Methylation	LAELSDYRRLSESQL HHHHHHHHHHCHHHH	37.75	115490603
618	Phosphorylation	LSDYRRLSESQLSFR HHHHHHHCHHHHCCC	33.13	29255136
620	Phosphorylation	DYRRLSESQLSFRRS HHHHHCHHHHCCCCC	32.80	29255136
623	Phosphorylation	RLSESQLSFRRSPTK HHCHHHHCCCCCCCC	14.74	29255136
627	Phosphorylation	SQLSFRRSPTKSSLD HHHCCCCCCCCCCCC	32.44	25159151
629	Phosphorylation	LSFRRSPTKSSLDYR HCCCCCCCCCCCCHH	44.82	23927012
631	Phosphorylation	FRRSPTKSSLDYRRL CCCCCCCCCCCHHCC	38.31	23927012
632	Phosphorylation	RRSPTKSSLDYRRLP CCCCCCCCCCHHCCC	27.15	23927012
635	Phosphorylation	PTKSSLDYRRLPDAH CCCCCCCHHCCCCCC	11.70	23927012
643	Phosphorylation	RRLPDAHSDYARYSG HCCCCCCHHHHHHCC	33.75	30266825
645	Phosphorylation	LPDAHSDYARYSGSY CCCCCHHHHHHCCCH	8.94	30266825
647	Methylation	DAHSDYARYSGSYND CCCHHHHHHCCCHHH	21.66	115388169
648	Phosphorylation	AHSDYARYSGSYNDY CCHHHHHHCCCHHHH	14.82	22617229
649	Phosphorylation	HSDYARYSGSYNDYL CHHHHHHCCCHHHHH	18.73	23401153
651	Phosphorylation	DYARYSGSYNDYLRA HHHHHCCCHHHHHHH	18.15	23401153
652	Phosphorylation	YARYSGSYNDYLRAA HHHHCCCHHHHHHHH	18.64	20090780
655	Phosphorylation	YSGSYNDYLRAAQMH HCCCHHHHHHHHHHH	8.41	28152594
657	Methylation	GSYNDYLRAAQMHSG CCHHHHHHHHHHHHC	22.96	82954953
661	Sulfoxidation	DYLRAAQMHSGYQRR HHHHHHHHHHCCCCC	2.02	30846556
663	Phosphorylation	LRAAQMHSGYQRRM- HHHHHHHHCCCCCC-	33.58	23401153
665	Phosphorylation	AAQMHSGYQRRM--- HHHHHHCCCCCC---	11.23	25003641

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
618	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
618	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
627	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
629	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
649	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM14_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 RBM14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRBP2_HUMAN	TARBP2	physical	11443112
EP300_HUMAN	EP300	physical	11443112
XRCC5_HUMAN	XRCC5	physical	11443112
PARP1_HUMAN	PARP1	physical	11443112
SYT1_HUMAN	SYT1	physical	15919756
SSXT_HUMAN	SS18	physical	16227627
TR150_HUMAN	THRAP3	physical	22939629
RNPS1_HUMAN	RNPS1	physical	22939629
TOP2B_HUMAN	TOP2B	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
SRS11_HUMAN	SRSF11	physical	22939629
RFC1_HUMAN	RFC1	physical	22939629
SMC1A_HUMAN	SMC1A	physical	22939629
TOP1_HUMAN	TOP1	physical	22939629
STAG2_HUMAN	STAG2	physical	22939629
TR112_HUMAN	TRMT112	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
RBM25_HUMAN	RBM25	physical	22939629
TPBG_HUMAN	TPBG	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
RBM39_HUMAN	RBM39	physical	22939629
SAP18_HUMAN	SAP18	physical	22939629
RBM8A_HUMAN	RBM8A	physical	22939629
RCC1_HUMAN	RCC1	physical	22939629
SMRC2_HUMAN	SMARCC2	physical	22939629
SRRM1_HUMAN	SRRM1	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
SRS10_HUMAN	SRSF10	physical	22939629
RED_HUMAN	IK	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
SSRP1_HUMAN	SSRP1	physical	22939629
RL1D1_HUMAN	RSL1D1	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
EAF1_HUMAN	EAF1	physical	27173435
NAF1_HUMAN	NAF1	physical	27173435
MFAP1_HUMAN	MFAP1	physical	27173435
DPOD1_HUMAN	POLD1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RBM14_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-280 AND THR-572, ANDMASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206; SER-571 ANDTHR-572, 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 THR-206; SER-256 ANDSER-618, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND MASSSPECTROMETRY.	19367720 [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 THR-572; SER-582; SER-618AND SER-649, AND MASS SPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.	16565220 [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-161; THR-206; SER-215;SER-220; SER-582 AND SER-618, AND MASS SPECTROMETRY.	17081983 [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 THR-206, AND MASSSPECTROMETRY.	19369195 [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-206, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND MASSSPECTROMETRY.	18187866 [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-572, AND MASSSPECTROMETRY.	19007248 [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 THR-206, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND MASSSPECTROMETRY.	15144186 [Abstract]