dbPTM

SRRT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRRT_HUMAN
UniProt AC	Q9BXP5
Protein Name	Serrate RNA effector molecule homolog
Gene Name	SRRT
Organism	Homo sapiens (Human).
Sequence Length	876
Subcellular Localization	Nucleus, nucleoplasm. Cytoplasm. Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way (By similarity)..
Protein Description	Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity)..
Protein Sequence	MGDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSDPYHSGYEMPYAGGGGGPTYGPPQPWGHPDVHIMQHHVLPIQARLGSIAEIDLGVPPPVMKTFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEVGKRRQEARGALQNRLRVFLSLMETGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLRILEQEEEEEQAGKPGEPSKKEEGRAGAGLGDGERKTNDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEDSEKEAKKSSKKRNRKHSGDDSFDEGSVSESESESESGQAEEEKEEAEEALKEKEKPKEEEWEKPKDAAGLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVTFDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLIHTLDDRTQLWASEPGTPPLPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGAPPEEPPKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPEIKPAQPPGPAQILPPGLTPGLPYPHQTPQGLMPYGQPRPPILGYGAGAVRPAVPTGGPPYPHAPYGAGRGNYDAFRGQGGYPGKPRNRMVRGDPRAIVEYRDLDAPDDVDFF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGDSDDEYD ------CCCCHHHHH	43.03	21406692
4	Phosphorylation	----MGDSDDEYDRR ----CCCCHHHHHHH	41.03	29255136
8	Phosphorylation	MGDSDDEYDRRRRDK CCCCHHHHHHHHHHH	23.03	21955146
21	Phosphorylation	DKFRRERSDYDRSRE HHHHHHHHHHHHHHH	35.45	25849741
23	Phosphorylation	FRRERSDYDRSRERD HHHHHHHHHHHHHHH	17.95	30576142
26	Phosphorylation	ERSDYDRSRERDERR HHHHHHHHHHHHHHH	35.28	30576142
45	Methylation	WNDREWDRGRERRSR CCHHHHHHHCHHHHC	47.33	26494911
47	Methylation	DREWDRGRERRSRGE HHHHHHHCHHHHCCC	34.83	115388471
51	Phosphorylation	DRGRERRSRGEYRDY HHHCHHHHCCCCCCC	51.35	29496963
52	Methylation	RGRERRSRGEYRDYD HHCHHHHCCCCCCCC	39.90	54554487
55	Phosphorylation	ERRSRGEYRDYDRNR HHHHCCCCCCCCCCC	16.17	29523821
58	Phosphorylation	SRGEYRDYDRNRRER HCCCCCCCCCCCCHH	14.06	-
67	Phosphorylation	RNRRERFSPPRHELS CCCCHHCCCCHHHCC	39.97	29255136
71	Ubiquitination	ERFSPPRHELSPPQK HHCCCCHHHCCCCHH	46.23	23000965
74	Phosphorylation	SPPRHELSPPQKRMR CCCHHHCCCCHHHHC	31.39	29255136
74	Ubiquitination	SPPRHELSPPQKRMR CCCHHHCCCCHHHHC	31.39	23000965
92	Phosphorylation	DEHSSDPYHSGYEMP CCCCCCCCCCCCCCC	17.38	22817900
97	Ubiquitination	DPYHSGYEMPYAGGG CCCCCCCCCCCCCCC	36.89	24816145
129	Ubiquitination	IMQHHVLPIQARLGS HHHCCHHHHHHCCCC	18.63	24816145
136	Phosphorylation	PIQARLGSIAEIDLG HHHHCCCCCEEECCC	24.18	28355574
150	Sumoylation	GVPPPVMKTFKEFLL CCCCHHHHHHHHHHH	51.55	28112733
150	Ubiquitination	GVPPPVMKTFKEFLL CCCCHHHHHHHHHHH	51.55	23000965
153	Ubiquitination	PPVMKTFKEFLLSLD CHHHHHHHHHHHCCC	53.43	23000965
157	Ubiquitination	KTFKEFLLSLDDSVD HHHHHHHHCCCCCCC	6.08	23000965
160	Ubiquitination	KEFLLSLDDSVDETE HHHHHCCCCCCCHHH	42.64	23000965
170	Ubiquitination	VDETEAVKRYNDYKL CCHHHHHHHHHCCCC	57.10	33845483
172	Phosphorylation	ETEAVKRYNDYKLDF HHHHHHHHHCCCCHH	13.48	-
175	Phosphorylation	AVKRYNDYKLDFRRQ HHHHHHCCCCHHHHH	15.15	23403867
176	2-Hydroxyisobutyrylation	VKRYNDYKLDFRRQQ HHHHHCCCCHHHHHH	44.43	-
176	Acetylation	VKRYNDYKLDFRRQQ HHHHHCCCCHHHHHH	44.43	25953088
176	Ubiquitination	VKRYNDYKLDFRRQQ HHHHHCCCCHHHHHH	44.43	24816145
183	Ubiquitination	KLDFRRQQMQDFFLA CCHHHHHHHHHHHHH	29.68	24816145
192	Ubiquitination	QDFFLAHKDEEWFRS HHHHHHHCCHHHHHH	62.32	32015554
200	2-Hydroxyisobutyrylation	DEEWFRSKYHPDEVG CHHHHHHCCCHHHHH	43.24	-
200	Acetylation	DEEWFRSKYHPDEVG CHHHHHHCCCHHHHH	43.24	23749302
200	Ubiquitination	DEEWFRSKYHPDEVG CHHHHHHCCCHHHHH	43.24	22817900
208	2-Hydroxyisobutyrylation	YHPDEVGKRRQEARG CCHHHHHHHHHHHHH	49.97	-
208	Acetylation	YHPDEVGKRRQEARG CCHHHHHHHHHHHHH	49.97	25953088
208	Ubiquitination	YHPDEVGKRRQEARG CCHHHHHHHHHHHHH	49.97	24816145
215	Ubiquitination	KRRQEARGALQNRLR HHHHHHHHHHHHHHH	37.37	24816145
248	2-Hydroxyisobutyrylation	DKADAIVKMLDAAVI HHHHHHHHHHHHHHH	27.86	-
256	Ubiquitination	MLDAAVIKMEGGTEN HHHHHHHCCCCCCHH	25.05	32015554
279	Acetylation	EEEEQAGKPGEPSKK HHHHHCCCCCCCCCC	53.52	23236377
279	Ubiquitination	EEEEQAGKPGEPSKK HHHHHCCCCCCCCCC	53.52	21906983
279 (in isoform 1)	Ubiquitination	-	53.52	21890473
279 (in isoform 2)	Ubiquitination	-	53.52	21890473
279 (in isoform 3)	Ubiquitination	-	53.52	21890473
279 (in isoform 4)	Ubiquitination	-	53.52	21890473
285	Ubiquitination	GKPGEPSKKEEGRAG CCCCCCCCCCCCCCC	74.95	32015554
286	Ubiquitination	KPGEPSKKEEGRAGA CCCCCCCCCCCCCCC	66.39	22817900
305	Ubiquitination	GERKTNDKDEKKEDG CCCCCCCCHHHHHCC	70.61	-
313	Acetylation	DEKKEDGKQAENDSS HHHHHCCCCCCCCCC	59.67	26051181
319	Phosphorylation	GKQAENDSSNDDKTK CCCCCCCCCCCHHHC	42.49	28985074
320	Phosphorylation	KQAENDSSNDDKTKK CCCCCCCCCCHHHCC	47.33	21406692
321 (in isoform 5)	Phosphorylation	-	66.51	25137130
324	Acetylation	NDSSNDDKTKKSEGD CCCCCCHHHCCCCCC	66.17	26051181
325 (in isoform 5)	Phosphorylation	-	51.18	25137130
328	Phosphorylation	NDDKTKKSEGDGDKE CCHHHCCCCCCCCHH	48.66	28985074
330 (in isoform 5)	Phosphorylation	-	51.82	25137130
332 (in isoform 5)	Phosphorylation	-	59.76	25137130
334 (in isoform 5)	Phosphorylation	-	73.61	25137130
336 (in isoform 5)	Phosphorylation	-	75.15	25137130
338 (in isoform 5)	Phosphorylation	-	70.77	25137130
340 (in isoform 5)	Phosphorylation	-	71.61	25137130
341	Phosphorylation	KEEKKEDSEKEAKKS HHHHHHHHHHHHHHH	52.22	26657352
346	Acetylation	EDSEKEAKKSSKKRN HHHHHHHHHHHHHHH	55.04	24886907
347	Acetylation	DSEKEAKKSSKKRNR HHHHHHHHHHHHHHH	67.99	24886917
357	Phosphorylation	KKRNRKHSGDDSFDE HHHHHCCCCCCCCCC	47.13	25849741
357 (in isoform 3)	Phosphorylation	-	47.13	25137130
357 (in isoform 4)	Phosphorylation	-	47.13	25137130
361	Phosphorylation	RKHSGDDSFDEGSVS HCCCCCCCCCCCCCC	39.06	25137130
361 (in isoform 3)	Phosphorylation	-	39.06	25137130
361 (in isoform 4)	Phosphorylation	-	39.06	25137130
366	Phosphorylation	DDSFDEGSVSESESE CCCCCCCCCCCCHHC	22.03	25137130
366 (in isoform 3)	Phosphorylation	-	22.03	25137130
366 (in isoform 4)	Phosphorylation	-	22.03	25137130
368	Phosphorylation	SFDEGSVSESESESE CCCCCCCCCCHHCCC	36.78	25137130
368 (in isoform 3)	Phosphorylation	-	36.78	25137130
368 (in isoform 4)	Phosphorylation	-	36.78	25137130
370	Phosphorylation	DEGSVSESESESESG CCCCCCCCHHCCCCC	38.63	20363803
370 (in isoform 3)	Phosphorylation	-	38.63	25137130
370 (in isoform 4)	Phosphorylation	-	38.63	25137130
372	Phosphorylation	GSVSESESESESGQA CCCCCCHHCCCCCCH	56.56	20363803
372 (in isoform 3)	Phosphorylation	-	56.56	25137130
372 (in isoform 4)	Phosphorylation	-	56.56	25137130
374	Phosphorylation	VSESESESESGQAEE CCCCHHCCCCCCHHH	46.47	20363803
374 (in isoform 3)	Phosphorylation	-	46.47	25137130
374 (in isoform 4)	Phosphorylation	-	46.47	25137130
376	Phosphorylation	ESESESESGQAEEEK CCHHCCCCCCHHHHH	45.55	25022875
376 (in isoform 3)	Phosphorylation	-	45.55	25137130
376 (in isoform 4)	Phosphorylation	-	45.55	25137130
396	Ubiquitination	ALKEKEKPKEEEWEK HHHHHCCCCHHHCCC	50.84	22053931
397	Ubiquitination	LKEKEKPKEEEWEKP HHHHCCCCHHHCCCC	84.53	22053931
404	Ubiquitination	KEEEWEKPKDAAGLE CHHHCCCCCCCCCCC	28.39	33845483
405	Ubiquitination	EEEWEKPKDAAGLEC HHHCCCCCCCCCCCC	71.69	33845483
412	Glutathionylation	KDAAGLECKPRPLHK CCCCCCCCCCCCHHH	9.88	22555962
413	Sumoylation	DAAGLECKPRPLHKT CCCCCCCCCCCHHHH	34.39	-
413	Acetylation	DAAGLECKPRPLHKT CCCCCCCCCCCHHHH	34.39	25953088
413	Sumoylation	DAAGLECKPRPLHKT CCCCCCCCCCCHHHH	34.39	-
421	Glutathionylation	PRPLHKTCSLFMRNI CCCHHHHHHHHHHHC	3.87	22555962
422	Phosphorylation	RPLHKTCSLFMRNIA CCHHHHHHHHHHHCC	29.85	28857561
439	Phosphorylation	ISRAEIISLCKRYPG CCHHHHHHHHHHCCC	33.12	23312004
441	Glutathionylation	RAEIISLCKRYPGFM HHHHHHHHHHCCCCE	1.56	22555962
441	Ubiquitination	RAEIISLCKRYPGFM HHHHHHHHHHCCCCE	1.56	33845483
442	Acetylation	AEIISLCKRYPGFMR HHHHHHHHHCCCCEE	61.33	25953088
442	Malonylation	AEIISLCKRYPGFMR HHHHHHHHHCCCCEE	61.33	26320211
442	Ubiquitination	AEIISLCKRYPGFMR HHHHHHHHHCCCCEE	61.33	33845483
443	Ubiquitination	EIISLCKRYPGFMRV HHHHHHHHCCCCEEE	41.71	22817900
444	Phosphorylation	IISLCKRYPGFMRVA HHHHHHHCCCCEEEE	8.00	26307563
446	Ubiquitination	SLCKRYPGFMRVALS HHHHHCCCCEEEECC	21.76	21890473
447	Ubiquitination	LCKRYPGFMRVALSE HHHHCCCCEEEECCC	2.15	21890473
448	Sulfoxidation	CKRYPGFMRVALSEP HHHCCCCEEEECCCC	4.11	28183972
453	Phosphorylation	GFMRVALSEPQPERR CCEEEECCCCCCCCC	37.18	22210691
471	Methylation	RGWVTFDRSVNIKEI CCCEEECCCCCHHHH	38.01	115917829
475	Ubiquitination	TFDRSVNIKEICWNL EECCCCCHHHHHHCC	3.87	22053931
476	Acetylation	FDRSVNIKEICWNLQ ECCCCCHHHHHHCCC	35.50	26051181
476	Ubiquitination	FDRSVNIKEICWNLQ ECCCCCHHHHHHCCC	35.50	22053931
476 (in isoform 2)	Ubiquitination	-	35.50	21890473
479	Glutathionylation	SVNIKEICWNLQNIR CCCHHHHHHCCCCCC	1.75	22555962
482	Ubiquitination	IKEICWNLQNIRLRE HHHHHHCCCCCCCEE	1.46	22053931
483	Ubiquitination	KEICWNLQNIRLREC HHHHHCCCCCCCEEC	39.84	22053931
489 (in isoform 5)	Ubiquitination	-	36.61	21890473
490	Glutathionylation	QNIRLRECELSPGVN CCCCCEECCCCCCCC	5.29	22555962
493	Phosphorylation	RLRECELSPGVNRDL CCEECCCCCCCCHHH	9.41	29255136
511	Phosphorylation	VRNINGITQHKQIVR HHCCCCHHHCHHHHH	26.47	30622161
513	Ubiquitination	NINGITQHKQIVRND CCCCHHHCHHHHHHH	18.48	29967540
514	Ubiquitination	INGITQHKQIVRNDI CCCHHHCHHHHHHHH	31.72	29967540
521	Ubiquitination	KQIVRNDIKLAAKLI HHHHHHHHHHHHHHH	4.50	22817900
522	Acetylation	QIVRNDIKLAAKLIH HHHHHHHHHHHHHHH	34.63	25953088
522	Ubiquitination	QIVRNDIKLAAKLIH HHHHHHHHHHHHHHH	34.63	22817900
525	Ubiquitination	RNDIKLAAKLIHTLD HHHHHHHHHHHHHCC	20.02	21890473
525 (in isoform 3)	Ubiquitination	-	20.02	21890473
525 (in isoform 4)	Ubiquitination	-	20.02	21890473
526	Acetylation	NDIKLAAKLIHTLDD HHHHHHHHHHHHCCC	42.22	23954790
526	Ubiquitination	NDIKLAAKLIHTLDD HHHHHHHHHHHHCCC	42.22	21890473
526 (in isoform 1)	Ubiquitination	-	42.22	21890473
526 (in isoform 2)	Ubiquitination	-	42.22	21890473
528	Ubiquitination	IKLAAKLIHTLDDRT HHHHHHHHHHCCCCC	1.99	22817900
529	Ubiquitination	KLAAKLIHTLDDRTQ HHHHHHHHHCCCCCC	30.71	22817900
530	Phosphorylation	LAAKLIHTLDDRTQL HHHHHHHHCCCCCCH	25.53	24732914
532	Ubiquitination	AKLIHTLDDRTQLWA HHHHHHCCCCCCHHC	44.49	21890473
533	Ubiquitination	KLIHTLDDRTQLWAS HHHHHCCCCCCHHCC	59.65	21890473
534	Methylation	LIHTLDDRTQLWASE HHHHCCCCCCHHCCC	24.84	115917833
535	Phosphorylation	IHTLDDRTQLWASEP HHHCCCCCCHHCCCC	34.70	25463755
539	Phosphorylation	DDRTQLWASEPGTPP CCCCCHHCCCCCCCC	16.77	32142685
540	Phosphorylation	DRTQLWASEPGTPPL CCCCHHCCCCCCCCC	32.51	23927012
543	Phosphorylation	QLWASEPGTPPLPTS CHHCCCCCCCCCCCC	46.96	32645325
544	Phosphorylation	LWASEPGTPPLPTSL HHCCCCCCCCCCCCC	32.23	25159151
549	Phosphorylation	PGTPPLPTSLPSQNP CCCCCCCCCCCCCCH	51.05	23927012
550	Phosphorylation	GTPPLPTSLPSQNPI CCCCCCCCCCCCCHH	36.02	30278072
553	Phosphorylation	PLPTSLPSQNPILKN CCCCCCCCCCHHHHH	48.13	23927012
570	Phosphorylation	DYLIEEVSAEEEELL HHHHHHCCHHHHHHH	32.99	25159151
579	Phosphorylation	EEEELLGSSGGAPPE HHHHHHCCCCCCCCC	26.27	28464451
580	Phosphorylation	EEELLGSSGGAPPEE HHHHHCCCCCCCCCC	39.17	28387310
603	Ubiquitination	EINVERDEKLIKVLD CCCCCCHHHHHHHHH	56.85	29967540
604	Ubiquitination	INVERDEKLIKVLDK CCCCCHHHHHHHHHH	60.86	29967540
607	2-Hydroxyisobutyrylation	ERDEKLIKVLDKLLL CCHHHHHHHHHHHHH	47.37	-
607	Acetylation	ERDEKLIKVLDKLLL CCHHHHHHHHHHHHH	47.37	26051181
607	Malonylation	ERDEKLIKVLDKLLL CCHHHHHHHHHHHHH	47.37	26320211
607	Ubiquitination	ERDEKLIKVLDKLLL CCHHHHHHHHHHHHH	47.37	24816145
608	Ubiquitination	RDEKLIKVLDKLLLY CHHHHHHHHHHHHHH	7.10	24816145
611	Acetylation	KLIKVLDKLLLYLRI HHHHHHHHHHHHHHH	36.55	26051181
611	Ubiquitination	KLIKVLDKLLLYLRI HHHHHHHHHHHHHHH	36.55	-
615	Phosphorylation	VLDKLLLYLRIVHSL HHHHHHHHHHHHHHC	8.23	-
624	Phosphorylation	RIVHSLDYYNTCEYP HHHHHCCCCCCCCCC	12.15	17053785
625	Phosphorylation	IVHSLDYYNTCEYPN HHHHCCCCCCCCCCC	12.03	17053785
628	Glutathionylation	SLDYYNTCEYPNEDE HCCCCCCCCCCCCCC	4.14	22555962
630	Phosphorylation	DYYNTCEYPNEDEMP CCCCCCCCCCCCCCC	17.32	22817900
640	S-nitrosocysteine	EDEMPNRCGIIHVRG CCCCCCCCEEEEECC	6.12	-
640	Glutathionylation	EDEMPNRCGIIHVRG CCCCCCCCEEEEECC	6.12	22555962
640	S-nitrosylation	EDEMPNRCGIIHVRG CCCCCCCCEEEEECC	6.12	19483679
665	Phosphorylation	EVLEWQKTFEEKLTP HHHHHHHHHHHHHHH	22.60	23186163
668	Ubiquitination	EWQKTFEEKLTPLLS HHHHHHHHHHHHHHH	49.53	29967540
669	Sumoylation	WQKTFEEKLTPLLSV HHHHHHHHHHHHHHH	50.92	-
669	2-Hydroxyisobutyrylation	WQKTFEEKLTPLLSV HHHHHHHHHHHHHHH	50.92	-
669	Acetylation	WQKTFEEKLTPLLSV HHHHHHHHHHHHHHH	50.92	25953088
669	Sumoylation	WQKTFEEKLTPLLSV HHHHHHHHHHHHHHH	50.92	-
669	Ubiquitination	WQKTFEEKLTPLLSV HHHHHHHHHHHHHHH	50.92	29967540
671	Phosphorylation	KTFEEKLTPLLSVRE HHHHHHHHHHHHHHH	23.98	23312004
675	Phosphorylation	EKLTPLLSVRESLSE HHHHHHHHHHHHCCH	27.15	20068231
678	Ubiquitination	TPLLSVRESLSEEEA HHHHHHHHHCCHHHH	54.60	21890473
679	Phosphorylation	PLLSVRESLSEEEAQ HHHHHHHHCCHHHHH	26.99	21815630
679	Ubiquitination	PLLSVRESLSEEEAQ HHHHHHHHCCHHHHH	26.99	21890473
681	Phosphorylation	LSVRESLSEEEAQKM HHHHHHCCHHHHHHC	52.84	21815630
686	Ubiquitination	SLSEEEAQKMGRKDP HCCHHHHHHCCCCCH	39.28	33845483
687	Acetylation	LSEEEAQKMGRKDPE CCHHHHHHCCCCCHH	50.82	23236377
687	Ubiquitination	LSEEEAQKMGRKDPE CCHHHHHHCCCCCHH	50.82	24816145
691	Acetylation	EAQKMGRKDPEQEVE HHHHCCCCCHHHHHH	72.42	26051181
693	Ubiquitination	QKMGRKDPEQEVEKF HHCCCCCHHHHHHHH	48.48	24816145
694	Ubiquitination	KMGRKDPEQEVEKFV HCCCCCHHHHHHHHH	70.30	24816145
709	Ubiquitination	TSNTQELGKDKWLCP HCCHHHHCCCCEEEC	35.05	33845483
710	Acetylation	SNTQELGKDKWLCPL CCHHHHCCCCEEECC	69.62	23954790
710	Ubiquitination	SNTQELGKDKWLCPL CCHHHHCCCCEEECC	69.62	33845483
712	Acetylation	TQELGKDKWLCPLSG HHHHCCCCEEECCCC	45.62	23954790
718	Phosphorylation	DKWLCPLSGKKFKGP CCEEECCCCCCCCCH	33.44	25159151
720	Acetylation	WLCPLSGKKFKGPEF EEECCCCCCCCCHHH	52.22	25953088
721 (in isoform 5)	Ubiquitination	-	56.70	21890473
723	Acetylation	PLSGKKFKGPEFVRK CCCCCCCCCHHHHHH	80.55	26051181
723	Malonylation	PLSGKKFKGPEFVRK CCCCCCCCCHHHHHH	80.55	26320211
739	Acetylation	IFNKHAEKIEEVKKE HHHHHHHHHHHHHHH	57.09	23749302
744	Ubiquitination	AEKIEEVKKEVAFFN HHHHHHHHHHHHHHH	46.63	29967540
745	Ubiquitination	EKIEEVKKEVAFFNN HHHHHHHHHHHHHHH	63.70	29967540
757	Ubiquitination	FNNFLTDAKRPALPE HHHHCCCCCCCCCCC	12.43	21890473
757 (in isoform 3)	Ubiquitination	-	12.43	21890473
757 (in isoform 4)	Ubiquitination	-	12.43	21890473
758	Acetylation	NNFLTDAKRPALPEI HHHCCCCCCCCCCCC	62.82	24469679
758	Ubiquitination	NNFLTDAKRPALPEI HHHCCCCCCCCCCCC	62.82	22817900
758 (in isoform 1)	Ubiquitination	-	62.82	21890473
758 (in isoform 2)	Ubiquitination	-	62.82	21890473
764	Ubiquitination	AKRPALPEIKPAQPP CCCCCCCCCCCCCCC	65.58	21890473
765	Ubiquitination	KRPALPEIKPAQPPG CCCCCCCCCCCCCCC	6.47	21890473
782	Phosphorylation	QILPPGLTPGLPYPH CCCCCCCCCCCCCCC	22.64	-
787	Phosphorylation	GLTPGLPYPHQTPQG CCCCCCCCCCCCCCC	20.56	-
791	Phosphorylation	GLPYPHQTPQGLMPY CCCCCCCCCCCCCCC	17.97	-
798	Phosphorylation	TPQGLMPYGQPRPPI CCCCCCCCCCCCCCC	17.90	22817900
833	Dimethylation	HAPYGAGRGNYDAFR CCCCCCCCCCCHHCC	29.65	-
833	Methylation	HAPYGAGRGNYDAFR CCCCCCCCCCCHHCC	29.65	24129315
836	Phosphorylation	YGAGRGNYDAFRGQG CCCCCCCCHHCCCCC	16.09	22817900
840	Dimethylation	RGNYDAFRGQGGYPG CCCCHHCCCCCCCCC	37.94	-
840	Methylation	RGNYDAFRGQGGYPG CCCCHHCCCCCCCCC	37.94	24129315
848	Acetylation	GQGGYPGKPRNRMVR CCCCCCCCCCCCCCC	35.98	25953088
850	Methylation	GGYPGKPRNRMVRGD CCCCCCCCCCCCCCC	47.04	24129315
855	Methylation	KPRNRMVRGDPRAIV CCCCCCCCCCCCEEE	34.16	115917837
859	Methylation	RMVRGDPRAIVEYRD CCCCCCCCEEEEECC	41.51	115917841
864	Phosphorylation	DPRAIVEYRDLDAPD CCCEEEEECCCCCCC	9.87	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
92	Y	Phosphorylation	Kinase	SRC	P12931	PSP
175	Y	Phosphorylation	Kinase	SRC	P12931	PSP
798	Y	Phosphorylation	Kinase	SRC	P12931	PSP
836	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MIC60_HUMAN	IMMT	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
GIT1_HUMAN	GIT1	physical	16169070
VIME_HUMAN	VIM	physical	16169070
A4_HUMAN	APP	physical	21832049
TSSK2_HUMAN	TSSK2	physical	22939629
SYN1_HUMAN	SYN1	physical	22939629
RUXF_HUMAN	SNRPF	physical	22365833
HSP7C_HUMAN	HSPA8	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
STAT3_HUMAN	STAT3	physical	21988832
ACLY_HUMAN	ACLY	physical	22863883
CSN8_HUMAN	COPS8	physical	22863883
MAGD2_HUMAN	MAGED2	physical	22863883
PPP6_HUMAN	PPP6C	physical	22863883
PP6R3_HUMAN	PPP6R3	physical	22863883
EF1D_HUMAN	EEF1D	physical	26344197
OGFD1_HUMAN	OGFOD1	physical	26344197
GLU2B_HUMAN	PRKCSH	physical	26344197
PSME3_HUMAN	PSME3	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
TIF1B_HUMAN	TRIM28	physical	26344197
ZCH18_HUMAN	ZC3H18	physical	26344197

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 SRRT_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-136; SER-540 ANDTHR-544, AND MASS SPECTROMETRY.	19690332 [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-136; SER-493; SER-540AND THR-544, AND MASS SPECTROMETRY.	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-493, AND MASSSPECTROMETRY.	18220336 [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-540, AND MASSSPECTROMETRY.	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 TYR-8; SER-67; SER-74;SER-493 AND THR-544, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND MASSSPECTROMETRY.	17693683 [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 THR-544, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-624 AND TYR-625, ANDMASS SPECTROMETRY.	17053785 [Abstract]