dbPTM

UBP14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP14_HUMAN
UniProt AC	P54578
Protein Name	Ubiquitin carboxyl-terminal hydrolase 14
Gene Name	USP14
Organism	Homo sapiens (Human).
Sequence Length	494
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein .
Protein Description	Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation..
Protein Sequence	MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPLYSVTVKWG ----CCCEEEEEEEC	8.67	28152594
5	Phosphorylation	---MPLYSVTVKWGK ---CCCEEEEEEECH	20.99	21406692
7	Phosphorylation	-MPLYSVTVKWGKEK -CCCEEEEEEECHHH	15.49	21406692
9	Ubiquitination	PLYSVTVKWGKEKFE CCEEEEEEECHHHCC	40.64	32015554
14	Acetylation	TVKWGKEKFEGVELN EEEECHHHCCCEECC	52.80	25953088
27	Sulfoxidation	LNTDEPPMVFKAQLF CCCCCCCCEEEEHHH	8.94	21406390
49	Ubiquitination	ARQKVMVKGGTLKDD CCCEEEEECCCCCCC	33.26	21890473
49	2-Hydroxyisobutyrylation	ARQKVMVKGGTLKDD CCCEEEEECCCCCCC	33.26	-
49	Acetylation	ARQKVMVKGGTLKDD CCCEEEEECCCCCCC	33.26	25953088
49	Malonylation	ARQKVMVKGGTLKDD CCCEEEEECCCCCCC	33.26	26320211
49	Ubiquitination	ARQKVMVKGGTLKDD CCCEEEEECCCCCCC	33.26	32015554
52	Phosphorylation	KVMVKGGTLKDDDWG EEEEECCCCCCCCCC	39.02	28450419
54	Acetylation	MVKGGTLKDDDWGNI EEECCCCCCCCCCCE	59.97	25953088
54	Succinylation	MVKGGTLKDDDWGNI EEECCCCCCCCCCCE	59.97	23954790
54	Ubiquitination	MVKGGTLKDDDWGNI EEECCCCCCCCCCCE	59.97	32015554
62	Acetylation	DDDWGNIKIKNGMTL CCCCCCEEEECCEEE	52.18	25953088
62	Malonylation	DDDWGNIKIKNGMTL CCCCCCEEEECCEEE	52.18	26320211
62	Ubiquitination	DDDWGNIKIKNGMTL CCCCCCEEEECCEEE	52.18	27667366
64	Ubiquitination	DWGNIKIKNGMTLLM CCCCEEEECCEEEEE	42.31	23503661
74	Phosphorylation	MTLLMMGSADALPEE EEEEEEECCCCCCCC	12.70	20068231
78 (in isoform 2)	Phosphorylation	-	5.89	22210691
83	Phosphorylation	DALPEEPSAKTVFVE CCCCCCCCCCEEEEC	45.75	27251275
90 (in isoform 2)	Phosphorylation	-	30.51	22210691
95	Ubiquitination	FVEDMTEEQLASAME EECCCCHHHHHHHCC	41.55	27667366
108	Phosphorylation	MELPCGLTNLGNTCY CCCCCCCCCCCCCCH	17.43	32142685
130	Ubiquitination	IRSVPELKDALKRYA HHCCHHHHHHHHHHH	39.01	21890473
130	Ubiquitination	IRSVPELKDALKRYA HHCCHHHHHHHHHHH	39.01	27667366
134	Ubiquitination	PELKDALKRYAGALR HHHHHHHHHHHHHHH	45.12	-
136	Phosphorylation	LKDALKRYAGALRAS HHHHHHHHHHHHHHC	14.06	28176443
143	Phosphorylation	YAGALRASGEMASAQ HHHHHHHCHHHHHHH	28.93	29255136
146	Sulfoxidation	ALRASGEMASAQYIT HHHHCHHHHHHHHHH	3.99	30846556
148	Phosphorylation	RASGEMASAQYITAA HHCHHHHHHHHHHHH	18.00	29255136
151	Phosphorylation	GEMASAQYITAALRD HHHHHHHHHHHHHHH	10.43	29255136
153	Phosphorylation	MASAQYITAALRDLF HHHHHHHHHHHHHHH	10.84	23403867
179	Ubiquitination	PIILLQFLHMAFPQF HHHHHHHHHHHCHHH	1.42	21963094
181	Sulfoxidation	ILLQFLHMAFPQFAE HHHHHHHHHCHHHHH	4.47	28183972
189	Ubiquitination	AFPQFAEKGEQGQYL HCHHHHHCCCCCCCH	65.40	27667366
203	Glutathionylation	LQQDANECWIQMMRV HHHHHHHHHHHHHHH	3.78	22555962
203	Ubiquitination	LQQDANECWIQMMRV HHHHHHHHHHHHHHH	3.78	27667366
204	Ubiquitination	QQDANECWIQMMRVL HHHHHHHHHHHHHHH	4.25	22505724
205	Ubiquitination	QDANECWIQMMRVLQ HHHHHHHHHHHHHHH	2.58	22505724
214	Ubiquitination	MMRVLQQKLEAIEDD HHHHHHHHHHHHCCC	35.02	21890473
214	2-Hydroxyisobutyrylation	MMRVLQQKLEAIEDD HHHHHHHHHHHHCCC	35.02	-
214	Acetylation	MMRVLQQKLEAIEDD HHHHHHHHHHHHCCC	35.02	26822725
214	Malonylation	MMRVLQQKLEAIEDD HHHHHHHHHHHHCCC	35.02	26320211
214	Ubiquitination	MMRVLQQKLEAIEDD HHHHHHHHHHHHCCC	35.02	21963094
222	O-linked_Glycosylation	LEAIEDDSVKETDSS HHHHCCCCCCCCCCC	47.62	31373491
222	Phosphorylation	LEAIEDDSVKETDSS HHHHCCCCCCCCCCC	47.62	25159151
224	Acetylation	AIEDDSVKETDSSSA HHCCCCCCCCCCCCC	59.87	26051181
224	Ubiquitination	AIEDDSVKETDSSSA HHCCCCCCCCCCCCC	59.87	21906983
226	Phosphorylation	EDDSVKETDSSSASA CCCCCCCCCCCCCCC	35.15	28258704
228	Phosphorylation	DSVKETDSSSASAAT CCCCCCCCCCCCCCC	33.34	25159151
229	Phosphorylation	SVKETDSSSASAATP CCCCCCCCCCCCCCC	32.50	25850435
230	Phosphorylation	VKETDSSSASAATPS CCCCCCCCCCCCCCC	30.14	25850435
232	Phosphorylation	ETDSSSASAATPSKK CCCCCCCCCCCCCHH	22.00	29255136
232	Ubiquitination	ETDSSSASAATPSKK CCCCCCCCCCCCCHH	22.00	22505724
234	Ubiquitination	DSSSASAATPSKKKS CCCCCCCCCCCHHHH	19.97	21963094
235	Phosphorylation	SSSASAATPSKKKSL CCCCCCCCCCHHHHH	28.01	29255136
237	Phosphorylation	SASAATPSKKKSLID CCCCCCCCHHHHHHH	53.40	26462736
238	Acetylation	ASAATPSKKKSLIDQ CCCCCCCHHHHHHHH	66.48	25953088
238	Ubiquitination	ASAATPSKKKSLIDQ CCCCCCCHHHHHHHH	66.48	21906983
239	Ubiquitination	SAATPSKKKSLIDQF CCCCCCHHHHHHHHH	52.51	22505724
240	Ubiquitination	AATPSKKKSLIDQFF CCCCCHHHHHHHHHH	54.98	22505724
249	Ubiquitination	LIDQFFGVEFETTMK HHHHHHCCEEEEEEE	6.86	32015554
256	Acetylation	VEFETTMKCTESEEE CEEEEEEECCCCHHH	35.59	19608861
256	Ubiquitination	VEFETTMKCTESEEE CEEEEEEECCCCHHH	35.59	23000965
260	Phosphorylation	TTMKCTESEEEEVTK EEEECCCCHHHHHHC	31.96	27067055
265	Ubiquitination	TESEEEEVTKGKENQ CCCHHHHHHCCCCCE	8.30	27667366
267	Ubiquitination	SEEEEVTKGKENQLQ CHHHHHHCCCCCEEE	73.49	22505724
269	Ubiquitination	EEEVTKGKENQLQLS HHHHHCCCCCEEEHH	55.86	21963094
276	Phosphorylation	KENQLQLSCFINQEV CCCEEEHHHCCCHHH	8.27	21712546
277	Glutathionylation	ENQLQLSCFINQEVK CCEEEHHHCCCHHHH	5.58	22555962
278	Acetylation	NQLQLSCFINQEVKY CEEEHHHCCCHHHHH	5.44	19608861
278	Ubiquitination	NQLQLSCFINQEVKY CEEEHHHCCCHHHHH	5.44	27667366
281	Ubiquitination	QLSCFINQEVKYLFT EHHHCCCHHHHHHHH	52.63	22505724
284	Acetylation	CFINQEVKYLFTGLK HCCCHHHHHHHHCHH	35.17	30593285
284	Ubiquitination	CFINQEVKYLFTGLK HCCCHHHHHHHHCHH	35.17	32015554
285	Phosphorylation	FINQEVKYLFTGLKL CCCHHHHHHHHCHHH	16.54	25884760
291	Ubiquitination	KYLFTGLKLRLQEEI HHHHHCHHHHHHHHH	32.67	21890473
291	2-Hydroxyisobutyrylation	KYLFTGLKLRLQEEI HHHHHCHHHHHHHHH	32.67	-
291	Acetylation	KYLFTGLKLRLQEEI HHHHHCHHHHHHHHH	32.67	19608861
291	Ubiquitination	KYLFTGLKLRLQEEI HHHHHCHHHHHHHHH	32.67	23000965
293	Methylation	LFTGLKLRLQEEITK HHHCHHHHHHHHHHH	32.51	115919593
299	Phosphorylation	LRLQEEITKQSPTLQ HHHHHHHHHCCCCHH	26.72	21406692
300	Ubiquitination	RLQEEITKQSPTLQR HHHHHHHHCCCCHHC	55.21	21890473
300	2-Hydroxyisobutyrylation	RLQEEITKQSPTLQR HHHHHHHHCCCCHHC	55.21	-
300	Acetylation	RLQEEITKQSPTLQR HHHHHHHHCCCCHHC	55.21	25953088
300	Malonylation	RLQEEITKQSPTLQR HHHHHHHHCCCCHHC	55.21	26320211
300	Ubiquitination	RLQEEITKQSPTLQR HHHHHHHHCCCCHHC	55.21	27667366
301	Ubiquitination	LQEEITKQSPTLQRN HHHHHHHCCCCHHCC	46.09	33845483
302	O-linked_Glycosylation	QEEITKQSPTLQRNA HHHHHHCCCCHHCCE	22.77	31373491
302	Phosphorylation	QEEITKQSPTLQRNA HHHHHHCCCCHHCCE	22.77	27050516
304	O-linked_Glycosylation	EITKQSPTLQRNALY HHHHCCCCHHCCEEE	40.55	31373491
304	Phosphorylation	EITKQSPTLQRNALY HHHHCCCCHHCCEEE	40.55	23186163
307	Ubiquitination	KQSPTLQRNALYIKS HCCCCHHCCEEEEEC	33.24	27667366
313	2-Hydroxyisobutyrylation	QRNALYIKSSKISRL HCCEEEEECCCCCCC	34.81	-
313	Acetylation	QRNALYIKSSKISRL HCCEEEEECCCCCCC	34.81	19608861
313	Ubiquitination	QRNALYIKSSKISRL HCCEEEEECCCCCCC	34.81	27667366
314	Phosphorylation	RNALYIKSSKISRLP CCEEEEECCCCCCCC	27.57	20044836
315	Phosphorylation	NALYIKSSKISRLPA CEEEEECCCCCCCCH	29.07	20044836
316	Ubiquitination	ALYIKSSKISRLPAY EEEEECCCCCCCCHH	52.36	22505724
334	Ubiquitination	QMVRFFYKEKESVNA HHHHHHHHCCCCCCC	58.09	-
336	Acetylation	VRFFYKEKESVNAKV HHHHHHCCCCCCCHH	51.65	25953088
336	Ubiquitination	VRFFYKEKESVNAKV HHHHHHCCCCCCCHH	51.65	33845483
338	Phosphorylation	FFYKEKESVNAKVLK HHHHCCCCCCCHHHC	31.57	28857561
340	Ubiquitination	YKEKESVNAKVLKDV HHCCCCCCCHHHCCC	43.24	33845483
342	Ubiquitination	EKESVNAKVLKDVKF CCCCCCCHHHCCCCH	42.78	21890473
342	Ubiquitination	EKESVNAKVLKDVKF CCCCCCCHHHCCCCH	42.78	21906983
345	Ubiquitination	SVNAKVLKDVKFPLM CCCCHHHCCCCHHHE	64.56	27667366
346	Ubiquitination	VNAKVLKDVKFPLML CCCHHHCCCCHHHEE	44.68	29967540
348	Acetylation	AKVLKDVKFPLMLDM CHHHCCCCHHHEEEH	51.93	19820141
348	Ubiquitination	AKVLKDVKFPLMLDM CHHHCCCCHHHEEEH	51.93	29967540
356	Ubiquitination	FPLMLDMYELCTPEL HHHEEEHHHHCCHHH	12.86	27667366
359	Glutathionylation	MLDMYELCTPELQEK EEEHHHHCCHHHHHH	3.89	22555962
365	Ubiquitination	LCTPELQEKMVSFRS HCCHHHHHHHHHHHH	56.60	21963094
373	Ubiquitination	KMVSFRSKFKDLEDK HHHHHHHHCCCHHHH	52.78	-
375	Acetylation	VSFRSKFKDLEDKKV HHHHHHCCCHHHHCC	66.20	26051181
375	Ubiquitination	VSFRSKFKDLEDKKV HHHHHHCCCHHHHCC	66.20	29901268
380	Ubiquitination	KFKDLEDKKVNQQPN HCCCHHHHCCCCCCC	49.61	27667366
381	Ubiquitination	FKDLEDKKVNQQPNT CCCHHHHCCCCCCCC	59.76	29967540
388	Phosphorylation	KVNQQPNTSDKKSSP CCCCCCCCCCCCCCC	45.01	23403867
389	Phosphorylation	VNQQPNTSDKKSSPQ CCCCCCCCCCCCCCC	54.82	23403867
391	Acetylation	QQPNTSDKKSSPQKE CCCCCCCCCCCCCCC	55.08	23749302
391	Ubiquitination	QQPNTSDKKSSPQKE CCCCCCCCCCCCCCC	55.08	27667366
393	Phosphorylation	PNTSDKKSSPQKEVK CCCCCCCCCCCCCCC	53.65	23401153
394	Phosphorylation	NTSDKKSSPQKEVKY CCCCCCCCCCCCCCC	39.98	26055452
400	Ubiquitination	SSPQKEVKYEPFSFA CCCCCCCCCCCCCCC	45.01	21963094
401	Phosphorylation	SPQKEVKYEPFSFAD CCCCCCCCCCCCCCC	33.73	26074081
405	Phosphorylation	EVKYEPFSFADDIGS CCCCCCCCCCCCCCC	30.18	26074081
406	Ubiquitination	VKYEPFSFADDIGSN CCCCCCCCCCCCCCC	9.88	23000965
408	Ubiquitination	YEPFSFADDIGSNNC CCCCCCCCCCCCCCC	46.15	23000965
412	Phosphorylation	SFADDIGSNNCGYYD CCCCCCCCCCCCEEE	25.79	24043423
414	Acetylation	ADDIGSNNCGYYDLQ CCCCCCCCCCEEEEE	23.45	19608861
414	Neddylation	ADDIGSNNCGYYDLQ CCCCCCCCCCEEEEE	23.45	32015554
414	Ubiquitination	ADDIGSNNCGYYDLQ CCCCCCCCCCEEEEE	23.45	21963094
417	Phosphorylation	IGSNNCGYYDLQAVL CCCCCCCEEEEEEEE	8.94	28464451
418	Phosphorylation	GSNNCGYYDLQAVLT CCCCCCEEEEEEEEE	8.75	24043423
419	Ubiquitination	SNNCGYYDLQAVLTH CCCCCEEEEEEEEEE	24.66	33845483
425	Phosphorylation	YDLQAVLTHQGRSSS EEEEEEEEECCCCCC	12.93	24043423
430	Phosphorylation	VLTHQGRSSSSGHYV EEEECCCCCCCCCCE	41.20	28450419
431	Phosphorylation	LTHQGRSSSSGHYVS EEECCCCCCCCCCEE	27.45	28450419
432	Phosphorylation	THQGRSSSSGHYVSW EECCCCCCCCCCEEE	41.40	28450419
433	Phosphorylation	HQGRSSSSGHYVSWV ECCCCCCCCCCEEEE	31.38	28450419
436	Phosphorylation	RSSSSGHYVSWVKRK CCCCCCCCEEEEEEC	10.33	23186163
441	Ubiquitination	GHYVSWVKRKQDEWI CCCEEEEEECCCCCE	47.85	21890473
441	2-Hydroxyisobutyrylation	GHYVSWVKRKQDEWI CCCEEEEEECCCCCE	47.85	-
441	Ubiquitination	GHYVSWVKRKQDEWI CCCEEEEEECCCCCE	47.85	23000965
443	Ubiquitination	YVSWVKRKQDEWIKF CEEEEEECCCCCEEC	57.28	21890473
443	Ubiquitination	YVSWVKRKQDEWIKF CEEEEEECCCCCEEC	57.28	23000965
449	Ubiquitination	RKQDEWIKFDDDKVS ECCCCCEECCCCCEE	43.76	21890473
449	Acetylation	RKQDEWIKFDDDKVS ECCCCCEECCCCCEE	43.76	19608861
449	Neddylation	RKQDEWIKFDDDKVS ECCCCCEECCCCCEE	43.76	32015554
449	Ubiquitination	RKQDEWIKFDDDKVS ECCCCCEECCCCCEE	43.76	21963094
454	Acetylation	WIKFDDDKVSIVTPE CEECCCCCEEEECHH	44.89	23954790
454	Ubiquitination	WIKFDDDKVSIVTPE CEECCCCCEEEECHH	44.89	33845483
456	Phosphorylation	KFDDDKVSIVTPEDI ECCCCCEEEECHHHH	19.65	27067055
459	Phosphorylation	DDKVSIVTPEDILRL CCCEEEECHHHHHHH	21.20	-
488	Sulfoxidation	GPRRVEIMEEESEQ- CCCEEEECHHHCCC-	3.16	21406390
492	Phosphorylation	VEIMEEESEQ----- EEECHHHCCC-----	44.57	28450419

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
235	T	Phosphorylation	Kinase	CDK1	P06493	PSP
432	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBP14_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 UBP14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSA6_HUMAN	PSMA6	physical	19615732
PSB5_HUMAN	PSMB5	physical	19615732
PRS4_HUMAN	PSMC1	physical	19615732
PRS7_HUMAN	PSMC2	physical	19615732
PRS6A_HUMAN	PSMC3	physical	19615732
PRS6B_HUMAN	PSMC4	physical	19615732
PRS8_HUMAN	PSMC5	physical	19615732
PRS10_HUMAN	PSMC6	physical	19615732
PSMD1_HUMAN	PSMD1	physical	19615732
PSMD2_HUMAN	PSMD2	physical	19615732
PSMD3_HUMAN	PSMD3	physical	19615732
PSMD4_HUMAN	PSMD4	physical	19615732
PSMD7_HUMAN	PSMD7	physical	19615732
PSD10_HUMAN	PSMD10	physical	19615732
PSD11_HUMAN	PSMD11	physical	19615732
PSD12_HUMAN	PSMD12	physical	19615732
PSD13_HUMAN	PSMD13	physical	19615732
TXNL1_HUMAN	TXNL1	physical	19615732
PSMD6_HUMAN	PSMD6	physical	19615732
PSDE_HUMAN	PSMD14	physical	19615732
ADRM1_HUMAN	ADRM1	physical	19615732
UCHL5_HUMAN	UCHL5	physical	19615732
SRPRB_HUMAN	SRPRB	physical	19615732
RGPD5_HUMAN	RGPD5	physical	19615732
UN45A_HUMAN	UNC45A	physical	22939629
WDR12_HUMAN	WDR12	physical	22939629
VP37B_HUMAN	VPS37B	physical	22939629
XPO1_HUMAN	XPO1	physical	22939629
XPO7_HUMAN	XPO7	physical	22939629
UBC_HUMAN	UBC	physical	23287719
ECHM_HUMAN	ECHS1	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
CG21_YEAST	CLB1	physical	17018280
PSMD2_HUMAN	PSMD2	physical	24951540
ERN1_HUMAN	ERN1	physical	24951540
ARFP1_HUMAN	ARFIP1	physical	26344197
CCD22_HUMAN	CCDC22	physical	26344197
CHMP7_HUMAN	CHMP7	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
PNCB_HUMAN	NAPRT	physical	26344197
NDRG1_HUMAN	NDRG1	physical	26344197
PRS6A_HUMAN	PSMC3	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
XPO7_HUMAN	XPO7	physical	26344197
B2CL1_HUMAN	BCL2L1	physical	25429837
B2CL1_HUMAN	BCL2L1	physical	26710889
UBC_HUMAN	UBC	physical	27066941
CCNB1_HUMAN	CCNB1	physical	27074503
VIME_HUMAN	VIM	physical	27448976
ANDR_HUMAN	AR	physical	28151478
AHNK2_HUMAN	AHNAK2	physical	28514442
CNTN1_HUMAN	CNTN1	physical	28514442
AHNK_HUMAN	AHNAK	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 UBP14_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-291; LYS-313 AND LYS-449,AND MASS SPECTROMETRY.	19608861 [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-143, AND MASSSPECTROMETRY.	19690332 [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-143, AND MASSSPECTROMETRY.	19367720 [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 TYR-136, AND MASSSPECTROMETRY.	18669648 [Abstract]