PRR14_HUMAN - dbPTM
PRR14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRR14_HUMAN
UniProt AC Q9BWN1
Protein Name Proline-rich protein 14
Gene Name PRR14
Organism Homo sapiens (Human).
Sequence Length 585
Subcellular Localization Chromosome . Nucleus . Nucleus lamina . Nucleus, nucleoplasm . During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associ
Protein Description Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha. [PubMed: 24209742 Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit]
Protein Sequence MDLPGDSSPPGQPRLCRQPLTRALWGARSPKRPRLQLPGAPSPLEKASRRVLAVVLEDVMAVHMVPVVPSKQTSIPQHHSYHQDPVHRQPPASPPRQAGWSSQARPPDPLCLCREPLSRIHRTSSTLRRRSRTTPGPEEGPSQKVDRAPQPTLVVMLEDIASPRPPAEGFIDETPNFIIPAQRAEPMRIVRQPTPPPGDLEPPFQPSALPADPLESPPTAPDPALELPSTPPPSSLLRPRLSPWGLAPLFRSVRSKLESFADIFLTPNKTPQPPPPSPPMKLELKIAISEAEQSGAAEGTASVSPRPPIRQWRTQDHNTPALLPKPSLGRSYSCPDLGPPGPGTCTWPPAPPQPSRPRPRRHTVGGGEMARAPPPPRPCLRKEVFPLGGVGASPSLTTSCSSTASTSFSEPAEPRLGSTKGKEPRASKDQVLSEPETKTMGKVSRFRIRRTPARPQLNLTPMGLPRPIRLNKKEFSLEEIYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRAVEFRDSSLPRSRRPSRGVRAAGGRTVPPNVAPSPDVGPLLQQRLEELDALLLEEETVDREQPHWT
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
1Acetylation-------MDLPGDSS
-------CCCCCCCC		12.3122814378
7Phosphorylation-MDLPGDSSPPGQPR
-CCCCCCCCCCCCCC		51.1422199227
8PhosphorylationMDLPGDSSPPGQPRL
CCCCCCCCCCCCCCC		39.5922199227
29PhosphorylationRALWGARSPKRPRLQ
HHHHCCCCCCCCCCC		33.9527422710
42PhosphorylationLQLPGAPSPLEKASR
CCCCCCCCHHHHHHH		41.4029255136
93PhosphorylationVHRQPPASPPRQAGW
CCCCCCCCCCCCCCC		41.0126657352
131PhosphorylationSSTLRRRSRTTPGPE
HHHHHHHCCCCCCCC		31.9724719451
133PhosphorylationTLRRRSRTTPGPEEG
HHHHHCCCCCCCCCC		38.2922985185
134PhosphorylationLRRRSRTTPGPEEGP
HHHHCCCCCCCCCCC		25.7427794612
162PhosphorylationVMLEDIASPRPPAEG
EEEHHCCCCCCCCCC		23.0625159151
194PhosphorylationMRIVRQPTPPPGDLE
CEEEECCCCCCCCCC		39.8427251275
229PhosphorylationDPALELPSTPPPSSL
CCCCCCCCCCCCHHH		67.1921552520
230PhosphorylationPALELPSTPPPSSLL
CCCCCCCCCCCHHHC		37.5624275569
235PhosphorylationPSTPPPSSLLRPRLS
CCCCCCHHHCCCCCC		36.8824719451
242PhosphorylationSLLRPRLSPWGLAPL
HHCCCCCCHHCHHHH		21.6425106551
256UbiquitinationLFRSVRSKLESFADI
HHHHHHHHHHHHHHE		45.7921890473
259PhosphorylationSVRSKLESFADIFLT
HHHHHHHHHHHEECC		35.8528978645
266PhosphorylationSFADIFLTPNKTPQP
HHHHEECCCCCCCCC		17.6721815630
270PhosphorylationIFLTPNKTPQPPPPS
EECCCCCCCCCCCCC		33.5223186163
277PhosphorylationTPQPPPPSPPMKLEL
CCCCCCCCCCCEEEE		47.6229255136
294PhosphorylationAISEAEQSGAAEGTA
EEEHHHHCCCCCCCC		23.1624719451
300PhosphorylationQSGAAEGTASVSPRP
HCCCCCCCCCCCCCC		13.7830624053
302PhosphorylationGAAEGTASVSPRPPI
CCCCCCCCCCCCCCC		23.9830624053
304PhosphorylationAEGTASVSPRPPIRQ
CCCCCCCCCCCCCCC		16.8227050516
314PhosphorylationPPIRQWRTQDHNTPA
CCCCCCCCCCCCCCC		35.0827732954
319PhosphorylationWRTQDHNTPALLPKP
CCCCCCCCCCCCCCC		13.4027732954
331PhosphorylationPKPSLGRSYSCPDLG
CCCCCCCCCCCCCCC		21.4324719451
332PhosphorylationKPSLGRSYSCPDLGP
CCCCCCCCCCCCCCC		16.9728152594
333PhosphorylationPSLGRSYSCPDLGPP
CCCCCCCCCCCCCCC		22.0328152594
363PhosphorylationRPRPRRHTVGGGEMA
CCCCCCCCCCCCHHC		21.0226657352
418PhosphorylationPAEPRLGSTKGKEPR
CCCCCCCCCCCCCCC		31.3822210691
419PhosphorylationAEPRLGSTKGKEPRA
CCCCCCCCCCCCCCC		41.8522210691
427PhosphorylationKGKEPRASKDQVLSE
CCCCCCCCHHHCCCC		37.7429457462
433PhosphorylationASKDQVLSEPETKTM
CCHHHCCCCCCCCCC		52.8525159151
451PhosphorylationSRFRIRRTPARPQLN
EEEEEECCCCCCCCC		16.0828555341
460PhosphorylationARPQLNLTPMGLPRP
CCCCCCCCCCCCCCC		15.3428555341
476PhosphorylationRLNKKEFSLEEIYTN
CCCCCEECHHHHHCC		35.64-
481PhosphorylationEFSLEEIYTNKNYQS
EECHHHHHCCCCCCC		13.93-
488PhosphorylationYTNKNYQSPTTRRTF
HCCCCCCCCCCHHHH		17.5425262027
490PhosphorylationNKNYQSPTTRRTFET
CCCCCCCCCHHHHHH		37.8825262027
491PhosphorylationKNYQSPTTRRTFETI
CCCCCCCCHHHHHHH		22.8725262027
508PhosphorylationEPRERNGTLIFTSSR
CHHHHCCEEEECCCH		21.8923663014
512PhosphorylationRNGTLIFTSSRKLRR
HCCEEEECCCHHHHH		20.8523663014
513PhosphorylationNGTLIFTSSRKLRRA
CCEEEECCCHHHHHH		19.8623663014
514PhosphorylationGTLIFTSSRKLRRAV
CEEEECCCHHHHHHH		30.3123663014
526PhosphorylationRAVEFRDSSLPRSRR
HHHHHCCCCCCCCCC		29.5323898821
527PhosphorylationAVEFRDSSLPRSRRP
HHHHCCCCCCCCCCC		46.8323898821
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 PRR14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRR14_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 PRR14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MA2B2_HUMANMAN2B2physical
28514442
2A5D_HUMANPPP2R5Dphysical
28514442
2A5A_HUMANPPP2R5Aphysical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
2A5G_HUMANPPP2R5Cphysical
28514442
CBX5_HUMANCBX5physical
28514442
2AAB_HUMANPPP2R1Bphysical
28514442
PP2AA_HUMANPPP2CAphysical
28514442
2AAA_HUMANPPP2R1Aphysical
28514442
CBX1_HUMANCBX1physical
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 PRR14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-277, AND MASSSPECTROMETRY.

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