dbPTM

RSBNL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RSBNL_HUMAN
UniProt AC	Q6PCB5
Protein Name	Round spermatid basic protein 1-like protein
Gene Name	RSBN1L
Organism	Homo sapiens (Human).
Sequence Length	846
Subcellular Localization	Nucleus.
Protein Description
Protein Sequence	MAEPPSPVHCVAAAAPTATVSEKEPFGKLQLSSRDPPGSLSAKKVRTEEKKAPRRVNGEGGSGGNSRQLQPPAAPSPQSYGSPASWSFAPLSAAPSPSSSRSSFSFSAGTAVPSSASASLSQPVPRKLLVPPTLLHAQPHHLLLPAAAAAASANAKSRRPKEKREKERRRHGLGGAREAGGASREENGEVKPLPRDKIKDKIKERDKEKEREKKKHKVMNEIKKENGEVKILLKSGKEKPKTNIEDLQIKKVKKKKKKKHKENEKRKRPKMYSKSIQTICSGLLTDVEDQAAKGILNDNIKDYVGKNLDTKNYDSKIPENSEFPFVSLKEPRVQNNLKRLDTLEFKQLIHIEHQPNGGASVIHAYSNELSHLSPMEMERFAEEFVGLVFSENENSAAFYVMGIVHGAATYLPDFLDYFSFNFPNSPVKMEILGKKDIETTTMSNFHAQVKRTYSHGTYRAGPMRQISLVGAVDEEVGDYFPEFLDMLEESPFLKCTLPWGTLSSLKLQSRKDSDDGPIMWVRPGEQMIPVADMPKSPFKRKRTTNEIKNLQYLPRTSEPREMLFEDRTRAHADHIGQGFERQTTAAVGVLKAVHCGEWPDQPRITKDVICFHAEDFLEVVQRMQLDLHEPPLSQCVQWVDDAKLNQLRREGIRYARIQLYDNDIYFIPRNVVHQFKTVSAVCSLAWHIRLKLYHSEEDTSQNTATHETGTSSDSTSSVLGPHTDNMICAVSKASLDSVFSDKLHSKYELQQIKHEPIASVRIKEEPVNVNIPEKTTALNNMDGKNVKAKLDHVQFAEFKIDMDSKFENSNKDLKEELCPGNLSLVDTRQHSSAHSNQDKKDDDILC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEPPSPVH ------CCCCCCCCC	37.69	19413330
6	Phosphorylation	--MAEPPSPVHCVAA --CCCCCCCCCEEEE	50.71	29255136
17	Phosphorylation	CVAAAAPTATVSEKE EEEECCCCCEECCCC	30.18	20068231
19	Phosphorylation	AAAAPTATVSEKEPF EECCCCCEECCCCCC	27.35	20068231
21	Phosphorylation	AAPTATVSEKEPFGK CCCCCEECCCCCCCC	38.30	20068231
28	Acetylation	SEKEPFGKLQLSSRD CCCCCCCCCCCCCCC	33.18	19608861
32	Phosphorylation	PFGKLQLSSRDPPGS CCCCCCCCCCCCCCC	15.46	25159151
33	Phosphorylation	FGKLQLSSRDPPGSL CCCCCCCCCCCCCCC	49.66	-
39	Phosphorylation	SSRDPPGSLSAKKVR CCCCCCCCCCCCCCC	25.56	21815630
41	Phosphorylation	RDPPGSLSAKKVRTE CCCCCCCCCCCCCCC	39.48	21815630
43	Acetylation	PPGSLSAKKVRTEEK CCCCCCCCCCCCCCC	48.72	25953088
44	Ubiquitination	PGSLSAKKVRTEEKK CCCCCCCCCCCCCCC	36.34	24816145
44	Acetylation	PGSLSAKKVRTEEKK CCCCCCCCCCCCCCC	36.34	11924383
51	Ubiquitination	KVRTEEKKAPRRVNG CCCCCCCCCCCCCCC	67.89	24816145
62	Phosphorylation	RVNGEGGSGGNSRQL CCCCCCCCCCCCCCC	55.15	27174698
76	Phosphorylation	LQPPAAPSPQSYGSP CCCCCCCCCCCCCCC	30.74	22199227
79	Phosphorylation	PAAPSPQSYGSPASW CCCCCCCCCCCCCCC	34.54	22199227
80	Phosphorylation	AAPSPQSYGSPASWS CCCCCCCCCCCCCCC	19.17	22199227
82	Phosphorylation	PSPQSYGSPASWSFA CCCCCCCCCCCCCCC	14.73	22199227
85	Phosphorylation	QSYGSPASWSFAPLS CCCCCCCCCCCCCCC	27.00	22199227
87	Phosphorylation	YGSPASWSFAPLSAA CCCCCCCCCCCCCCC	14.72	22199227
92	Phosphorylation	SWSFAPLSAAPSPSS CCCCCCCCCCCCCCC	22.71	22199227
92	O-linked_Glycosylation	SWSFAPLSAAPSPSS CCCCCCCCCCCCCCC	22.71	23301498
96	Phosphorylation	APLSAAPSPSSSRSS CCCCCCCCCCCCCCC	32.46	22199227
96	O-linked_Glycosylation	APLSAAPSPSSSRSS CCCCCCCCCCCCCCC	32.46	23301498
98	O-linked_Glycosylation	LSAAPSPSSSRSSFS CCCCCCCCCCCCCEE	45.33	23301498
98	Phosphorylation	LSAAPSPSSSRSSFS CCCCCCCCCCCCCEE	45.33	22199227
99	Phosphorylation	SAAPSPSSSRSSFSF CCCCCCCCCCCCEEE	32.91	19690332
99	O-linked_Glycosylation	SAAPSPSSSRSSFSF CCCCCCCCCCCCEEE	32.91	23301498
100	O-linked_Glycosylation	AAPSPSSSRSSFSFS CCCCCCCCCCCEEEE	40.28	23301498
100	Phosphorylation	AAPSPSSSRSSFSFS CCCCCCCCCCCEEEE	40.28	22199227
102	Phosphorylation	PSPSSSRSSFSFSAG CCCCCCCCCEEEECC	37.37	25159151
102	O-linked_Glycosylation	PSPSSSRSSFSFSAG CCCCCCCCCEEEECC	37.37	23301498
103	Phosphorylation	SPSSSRSSFSFSAGT CCCCCCCCEEEECCC	24.65	25159151
103	O-linked_Glycosylation	SPSSSRSSFSFSAGT CCCCCCCCEEEECCC	24.65	23301498
105	Phosphorylation	SSSRSSFSFSAGTAV CCCCCCEEEECCCCC	21.90	26434776
107	Phosphorylation	SRSSFSFSAGTAVPS CCCCEEEECCCCCCC	25.29	27080861
110	Phosphorylation	SFSFSAGTAVPSSAS CEEEECCCCCCCCCC	24.97	27080861
115	O-linked_Glycosylation	AGTAVPSSASASLSQ CCCCCCCCCCCCCCC	21.85	23301498
183	Phosphorylation	AREAGGASREENGEV HHHCCCCCHHCCCCC	43.42	26714015
191	Acetylation	REENGEVKPLPRDKI HHCCCCCCCCCHHHH	36.21	23749302
191	Ubiquitination	REENGEVKPLPRDKI HHCCCCCCCCCHHHH	36.21	24816145
201	Ubiquitination	PRDKIKDKIKERDKE CHHHHHHHHHHHHHH	51.15	24816145
223	Sumoylation	HKVMNEIKKENGEVK HHHHHHHHHHCCCEE	48.10	28112733
235	Phosphorylation	EVKILLKSGKEKPKT CEEEEEECCCCCCCC	55.88	24505115
250	Ubiquitination	NIEDLQIKKVKKKKK CHHHHHHHHHHHHHH	38.25	29967540
250	Acetylation	NIEDLQIKKVKKKKK CHHHHHHHHHHHHHH	38.25	25953088
251	Ubiquitination	IEDLQIKKVKKKKKK HHHHHHHHHHHHHHH	62.00	-
273	Phosphorylation	RKRPKMYSKSIQTIC HHCHHHHHHHHHHHH	19.21	24719451
278 (in isoform 2)	Ubiquitination	-	23.45	21890473
278	Phosphorylation	MYSKSIQTICSGLLT HHHHHHHHHHHCCCC	23.45	27690223
278	Ubiquitination	MYSKSIQTICSGLLT HHHHHHHHHHHCCCC	23.45	21890473
281	Phosphorylation	KSIQTICSGLLTDVE HHHHHHHHCCCCCHH	28.73	26552605
285	Phosphorylation	TICSGLLTDVEDQAA HHHHCCCCCHHHHHH	42.94	27422710
301	Ubiquitination	GILNDNIKDYVGKNL HHCCHHHHHHCCCCC	49.62	29967540
303	Phosphorylation	LNDNIKDYVGKNLDT CCHHHHHHCCCCCCC	13.19	30576142
306	Acetylation	NIKDYVGKNLDTKNY HHHHHCCCCCCCCCC	44.27	25953088
306	Ubiquitination	NIKDYVGKNLDTKNY HHHHHCCCCCCCCCC	44.27	29967540
313	Phosphorylation	KNLDTKNYDSKIPEN CCCCCCCCCCCCCCC	24.13	23186163
315	Phosphorylation	LDTKNYDSKIPENSE CCCCCCCCCCCCCCC	23.33	28112733
321	Phosphorylation	DSKIPENSEFPFVSL CCCCCCCCCCCCCCC	38.66	23186163
327	Phosphorylation	NSEFPFVSLKEPRVQ CCCCCCCCCCCHHHH	33.82	28555341
329	Acetylation	EFPFVSLKEPRVQNN CCCCCCCCCHHHHCC	59.16	23236377
329	Ubiquitination	EFPFVSLKEPRVQNN CCCCCCCCCHHHHCC	59.16	29967540
338	Acetylation	PRVQNNLKRLDTLEF HHHHCCHHCCCEEEE	53.70	25953088
342	Phosphorylation	NNLKRLDTLEFKQLI CCHHCCCEEEEHHHE	32.55	24247654
440	Phosphorylation	GKKDIETTTMSNFHA CCCCCEECCCCCCHH	14.01	20068231
450	Acetylation	SNFHAQVKRTYSHGT CCCHHEEEECCCCCC	27.26	7710369
457	Phosphorylation	KRTYSHGTYRAGPMR EECCCCCCEECCCCE	12.38	-
458	Phosphorylation	RTYSHGTYRAGPMRQ ECCCCCCEECCCCEE	11.76	-
490	Phosphorylation	FLDMLEESPFLKCTL HHHHHHHCCCCEEEC	16.15	26074081
496	Phosphorylation	ESPFLKCTLPWGTLS HCCCCEEECCCCCHH	33.98	26074081
501	Phosphorylation	KCTLPWGTLSSLKLQ EEECCCCCHHHEEEC	21.43	26074081
503	Phosphorylation	TLPWGTLSSLKLQSR ECCCCCHHHEEECCC	33.20	26074081
504	Phosphorylation	LPWGTLSSLKLQSRK CCCCCHHHEEECCCC	32.41	26699800
506	Ubiquitination	WGTLSSLKLQSRKDS CCCHHHEEECCCCCC	46.56	-
509	Phosphorylation	LSSLKLQSRKDSDDG HHHEEECCCCCCCCC	52.30	26074081
536	Phosphorylation	PVADMPKSPFKRKRT ECCCCCCCCCCCCCC	29.69	25159151
548	Ubiquitination	KRTTNEIKNLQYLPR CCCCHHHCCCCCCCC	45.48	23000965
548 (in isoform 1)	Ubiquitination	-	45.48	21890473
548	Sumoylation	KRTTNEIKNLQYLPR CCCCHHHCCCCCCCC	45.48	28112733
552	Phosphorylation	NEIKNLQYLPRTSEP HHHCCCCCCCCCCCC	23.11	25003641
557	Phosphorylation	LQYLPRTSEPREMLF CCCCCCCCCCHHHHH	47.05	28555341
734	Phosphorylation	ICAVSKASLDSVFSD EEEEEHHHHHHHHHH	36.12	23663014
742	Acetylation	LDSVFSDKLHSKYEL HHHHHHHHHHCCCCH	47.07	25953088
746	Acetylation	FSDKLHSKYELQQIK HHHHHHCCCCHHHCC	31.81	25953088
746	Ubiquitination	FSDKLHSKYELQQIK HHHHHHCCCCHHHCC	31.81	29967540
753	Sumoylation	KYELQQIKHEPIASV CCCHHHCCCCCCEEE	37.26	28112733
753	Sumoylation	KYELQQIKHEPIASV CCCHHHCCCCCCEEE	37.26	-
763	Sumoylation	PIASVRIKEEPVNVN CCEEEEEEECCCCCC	45.52	-
763	Sumoylation	PIASVRIKEEPVNVN CCEEEEEEECCCCCC	45.52	28112733
774	Acetylation	VNVNIPEKTTALNNM CCCCCCCCCCCCCCC	45.91	25953088
784	Acetylation	ALNNMDGKNVKAKLD CCCCCCCCCCEEECC	55.06	25953088
789	Acetylation	DGKNVKAKLDHVQFA CCCCCEEECCEEEEE	49.05	25953088
814	Sumoylation	ENSNKDLKEELCPGN CCCCHHHHHHHCCCC	60.31	-
814	Sumoylation	ENSNKDLKEELCPGN CCCCHHHHHHHCCCC	60.31	28112733
823	Phosphorylation	ELCPGNLSLVDTRQH HHCCCCCEEEECCCC	30.28	21815630
827	Phosphorylation	GNLSLVDTRQHSSAH CCCEEEECCCCCCCC	25.42	20068231

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 RSBNL_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RSBN1_HUMAN	RSBN1	physical	28514442
PININ_HUMAN	PNN	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
NKAP_HUMAN	NKAP	physical	28514442
RNPS1_HUMAN	RNPS1	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 RSBNL_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.	19413330 [Abstract]