PRR11_HUMAN - dbPTM
PRR11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRR11_HUMAN
UniProt AC Q96HE9
Protein Name Proline-rich protein 11
Gene Name PRR11
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Plays a critical role in cell cycle progression..
Protein Sequence MPKFKQRRRKLKAKAERLFKKKEASHFQSKLITPPPPPPSPERVGISSIDISQSRSWLTSSWNFNFPNIRDAIKLWTNRVWSIYSWCQNCITQSLEVLKDTIFPSRICHRELYSVKQQFCILESKLCKLQEALKTISESSSCPSCGQTCHMSGKLTNVPACVLITPGDSKAVLPPTLPQPASHFPPPPPPPPLPPPPPPLAPVLLRKPSLAKALQAGPLKKDGPMQITVKDLLTVKLKKTQSLDEKRKLIPSPKARNPLVTVSDLQHVTLKPNSKVLSTRVTNVLITPGKSQMDLRKLLRKVDVERSPGGTPLTNKENMETGTGLTPVMTQALRRKFQLAHPRSPTPTLPLSTSSFDEQN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
33PhosphorylationHFQSKLITPPPPPPS
HHHCCCCCCCCCCCC
39.9330266825
40PhosphorylationTPPPPPPSPERVGIS
CCCCCCCCCCCCCCE
45.2029255136
47PhosphorylationSPERVGISSIDISQS
CCCCCCCEEEEHHHC
18.4728450419
48PhosphorylationPERVGISSIDISQSR
CCCCCCEEEEHHHCC
23.5128450419
52PhosphorylationGISSIDISQSRSWLT
CCEEEEHHHCCCCHH
20.5321815630
54PhosphorylationSSIDISQSRSWLTSS
EEEEHHHCCCCHHHC
22.8428450419
116UbiquitinationHRELYSVKQQFCILE
HHHHHCHHHHHHHHH
32.23-
125UbiquitinationQFCILESKLCKLQEA
HHHHHHHHHHHHHHH
48.83-
128UbiquitinationILESKLCKLQEALKT
HHHHHHHHHHHHHHH
64.74-
139PhosphorylationALKTISESSSCPSCG
HHHHHHHHCCCCCCC
22.2930576142
140PhosphorylationLKTISESSSCPSCGQ
HHHHHHHCCCCCCCC
31.7230576142
141PhosphorylationKTISESSSCPSCGQT
HHHHHHCCCCCCCCC
39.0530576142
165PhosphorylationVPACVLITPGDSKAV
CCEEEEECCCCCCCC
19.6330266825
169PhosphorylationVLITPGDSKAVLPPT
EEECCCCCCCCCCCC
28.5630266825
209PhosphorylationPVLLRKPSLAKALQA
CCHHCCHHHHHHHHC
43.95-
212MethylationLRKPSLAKALQAGPL
HCCHHHHHHHHCCCC
55.7323644510
220UbiquitinationALQAGPLKKDGPMQI
HHHCCCCCCCCCCEE
52.53-
220MethylationALQAGPLKKDGPMQI
HHHCCCCCCCCCCEE
52.5323644510
221UbiquitinationLQAGPLKKDGPMQIT
HHCCCCCCCCCCEEE
75.50-
240PhosphorylationLTVKLKKTQSLDEKR
EEEEEEECCCHHHHH
23.0828102081
242PhosphorylationVKLKKTQSLDEKRKL
EEEEECCCHHHHHHC
42.9124719451
252PhosphorylationEKRKLIPSPKARNPL
HHHHCCCCCCCCCCC
31.8530266825
254UbiquitinationRKLIPSPKARNPLVT
HHCCCCCCCCCCCEE
65.40-
261PhosphorylationKARNPLVTVSDLQHV
CCCCCCEEHHHCCCE
23.2120068231
269PhosphorylationVSDLQHVTLKPNSKV
HHHCCCEECCCCCCC
27.2620068231
282PhosphorylationKVLSTRVTNVLITPG
CCEEEEEEEEEECCC
19.1330266825
287PhosphorylationRVTNVLITPGKSQMD
EEEEEEECCCCCHHH
23.1030266825
290AcetylationNVLITPGKSQMDLRK
EEEECCCCCHHHHHH
38.4222424773
290UbiquitinationNVLITPGKSQMDLRK
EEEECCCCCHHHHHH
38.42-
291PhosphorylationVLITPGKSQMDLRKL
EEECCCCCHHHHHHH
36.3329978859
307PhosphorylationRKVDVERSPGGTPLT
HHCCCCCCCCCCCCC
17.8730266825
311PhosphorylationVERSPGGTPLTNKEN
CCCCCCCCCCCCHHH
22.5030266825
314PhosphorylationSPGGTPLTNKENMET
CCCCCCCCCHHHCCC
45.5121955146
316UbiquitinationGGTPLTNKENMETGT
CCCCCCCHHHCCCCC
45.2721906983
321PhosphorylationTNKENMETGTGLTPV
CCHHHCCCCCCCHHH
29.3129255136
323PhosphorylationKENMETGTGLTPVMT
HHHCCCCCCCHHHHH
36.1229255136
326PhosphorylationMETGTGLTPVMTQAL
CCCCCCCHHHHHHHH
18.3829255136
330PhosphorylationTGLTPVMTQALRRKF
CCCHHHHHHHHHHHC
15.7829255136
336UbiquitinationMTQALRRKFQLAHPR
HHHHHHHHCCCCCCC
30.91-
344PhosphorylationFQLAHPRSPTPTLPL
CCCCCCCCCCCCCCC
37.2630266825
346PhosphorylationLAHPRSPTPTLPLST
CCCCCCCCCCCCCCC
30.1030266825
348PhosphorylationHPRSPTPTLPLSTSS
CCCCCCCCCCCCCCC
43.4130266825
352PhosphorylationPTPTLPLSTSSFDEQ
CCCCCCCCCCCCCCC
25.0521712546
353PhosphorylationTPTLPLSTSSFDEQN
CCCCCCCCCCCCCCC
35.7521712546
354PhosphorylationPTLPLSTSSFDEQN-
CCCCCCCCCCCCCC-
26.1525159151
355PhosphorylationTLPLSTSSFDEQN--
CCCCCCCCCCCCC--
36.4825159151

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 PRR11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRR11_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 PRR11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NIP7_HUMANNIP7physical
26186194
KNOP1_HUMANKNOP1physical
26186194
RBM28_HUMANRBM28physical
26186194
SF3B1_HUMANSF3B1physical
26186194
POP1_HUMANPOP1physical
26186194
DDX24_HUMANDDX24physical
26186194
SPB1_HUMANFTSJ3physical
26186194
SF3B2_HUMANSF3B2physical
26186194
ZN668_HUMANZNF668physical
26186194
RL3_HUMANRPL3physical
26186194
RENT1_HUMANUPF1physical
26186194
ZN512_HUMANZNF512physical
26186194
RL10A_HUMANRPL10Aphysical
26186194
DKC1_HUMANDKC1physical
26186194
PABP4_HUMANPABPC4physical
26186194
DHX30_HUMANDHX30physical
26186194
ELAV2_HUMANELAVL2physical
26186194
DDX27_HUMANDDX27physical
26186194
H11_HUMANHIST1H1Aphysical
26186194
GLYR1_HUMANGLYR1physical
26186194
DHSO_HUMANSORDphysical
26186194
HP1B3_HUMANHP1BP3physical
26186194
REXO4_HUMANREXO4physical
26186194
DDX31_HUMANDDX31physical
26186194
MBB1A_HUMANMYBBP1Aphysical
26186194
NOP16_HUMANNOP16physical
26186194
RL26L_HUMANRPL26L1physical
26186194
RS3A_HUMANRPS3Aphysical
26186194
KRI1_HUMANKRI1physical
26186194
NSD2_HUMANWHSC1physical
26186194
CG050_HUMANC7orf50physical
26186194
ZCRB1_HUMANZCRB1physical
26186194
EBP2_HUMANEBNA1BP2physical
26186194
UTP23_HUMANUTP23physical
26186194
ZCHC3_HUMANZCCHC3physical
26186194
RRP12_HUMANRRP12physical
26186194
RSBN1_HUMANRSBN1physical
26186194
TTF1_HUMANTTF1physical
26186194
SURF6_HUMANSURF6physical
26186194
LARP1_HUMANLARP1physical
26186194
LYAR_HUMANLYARphysical
26186194
RRP8_HUMANRRP8physical
26186194
STAU2_HUMANSTAU2physical
26186194
STAU1_HUMANSTAU1physical
26186194
CTCF_HUMANCTCFphysical
26186194
NVL_HUMANNVLphysical
26186194
NOP53_HUMANGLTSCR2physical
26186194
LLPH_HUMANLLPHphysical
26186194
RS15_HUMANRPS15physical
26186194
CCD86_HUMANCCDC86physical
26186194
RBM34_HUMANRBM34physical
26186194
LN28B_HUMANLIN28Bphysical
26186194
NOC4L_HUMANNOC4Lphysical
26186194
NOC3L_HUMANNOC3Lphysical
26186194
BRX1_HUMANBRIX1physical
26186194
NOP2_HUMANNOP2physical
26186194
RLP24_HUMANRSL24D1physical
26186194
TSR1_HUMANTSR1physical
26186194
MOV10_HUMANMOV10physical
26186194
PWP1_HUMANPWP1physical
26186194
RRS1_HUMANRRS1physical
26186194
KRR1_HUMANKRR1physical
26186194
RL15_HUMANRPL15physical
26186194
PUM3_HUMANKIAA0020physical
26186194
PK1IP_HUMANPAK1IP1physical
26186194
RL23A_HUMANRPL23Aphysical
26186194
NOG2_HUMANGNL2physical
26186194
RS13_HUMANRPS13physical
26186194
ZBT24_HUMANZBTB24physical
26186194
ZN771_HUMANZNF771physical
26186194
ZBT11_HUMANZBTB11physical
26186194
RL13A_HUMANRPL13Aphysical
26186194
PRD15_HUMANPRDM15physical
26186194
RL7L_HUMANRPL7L1physical
26186194
RPF2_HUMANRPF2physical
26186194
ZN800_HUMANZNF800physical
26186194
PESC_HUMANPES1physical
26186194
CASC3_HUMANCASC3physical
26186194
PURA_HUMANPURAphysical
26186194
NSA2_HUMANNSA2physical
26186194
ZNF22_HUMANZNF22physical
26186194
NOL12_HUMANNOL12physical
26186194
ZN189_HUMANZNF189physical
26186194
RM38_HUMANMRPL38physical
26186194
ZN689_HUMANZNF689physical
26186194
DUS11_HUMANDUSP11physical
26186194
H11_HUMANHIST1H1Aphysical
28514442
ZN800_HUMANZNF800physical
28514442
RL26L_HUMANRPL26L1physical
28514442
NOG2_HUMANGNL2physical
28514442
BRX1_HUMANBRIX1physical
28514442
ZCRB1_HUMANZCRB1physical
28514442
RS15_HUMANRPS15physical
28514442
RENT1_HUMANUPF1physical
28514442
DDX31_HUMANDDX31physical
28514442
RRP12_HUMANRRP12physical
28514442
ZN689_HUMANZNF689physical
28514442
RRP8_HUMANRRP8physical
28514442
REXO4_HUMANREXO4physical
28514442
TTF1_HUMANTTF1physical
28514442
DHSO_HUMANSORDphysical
28514442
PRD15_HUMANPRDM15physical
28514442
ZBT24_HUMANZBTB24physical
28514442
ZN668_HUMANZNF668physical
28514442
SF3B2_HUMANSF3B2physical
28514442
LARP1_HUMANLARP1physical
28514442
MOV10_HUMANMOV10physical
28514442
GLYR1_HUMANGLYR1physical
28514442
RL3_HUMANRPL3physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
RLP24_HUMANRSL24D1physical
28514442
NVL_HUMANNVLphysical
28514442
SPB1_HUMANFTSJ3physical
28514442
RBM28_HUMANRBM28physical
28514442
DKC1_HUMANDKC1physical
28514442
DDX24_HUMANDDX24physical
28514442
SF3B1_HUMANSF3B1physical
28514442
NSD2_HUMANWHSC1physical
28514442
ZN189_HUMANZNF189physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
DUS11_HUMANDUSP11physical
28514442
NOP2_HUMANNOP2physical
28514442
POP1_HUMANPOP1physical
28514442
UTP23_HUMANUTP23physical
28514442
PUM3_HUMANKIAA0020physical
28514442
DHX30_HUMANDHX30physical
28514442
RL7L_HUMANRPL7L1physical
28514442
EBP2_HUMANEBNA1BP2physical
28514442
ZN771_HUMANZNF771physical
28514442
NSA2_HUMANNSA2physical
28514442
RS3_HUMANRPS3physical
28514442
DDX27_HUMANDDX27physical
28514442
RBM34_HUMANRBM34physical
28514442
PK1IP_HUMANPAK1IP1physical
28514442
CTCF_HUMANCTCFphysical
28514442
RS13_HUMANRPS13physical
28514442
STAU2_HUMANSTAU2physical
28514442
RL4_HUMANRPL4physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
RPF2_HUMANRPF2physical
28514442
ZN512_HUMANZNF512physical
28514442
BOP1_HUMANBOP1physical
28514442
STAU1_HUMANSTAU1physical
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 PRR11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-33; SER-40; THR-287;SER-344; THR-346 AND THR-348, AND MASS SPECTROMETRY.
"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 SER-307 AND THR-314, ANDMASS SPECTROMETRY.
"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-40, AND MASSSPECTROMETRY.

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