PTN14_HUMAN - dbPTM
PTN14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTN14_HUMAN
UniProt AC Q15678
Protein Name Tyrosine-protein phosphatase non-receptor type 14
Gene Name PTPN14
Organism Homo sapiens (Human).
Sequence Length 1187
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane.
Protein Description Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor..
Protein Sequence MPFGLKLRRTRRYNVLSKNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQDFLREYVLFPMDLALEEAVLEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRLFATRHKFYKQNKICTEQSNSPPPIRRQPTWSRSSLPRQQPYILPPVHVQCGEHYSETHTSQDSIFHGNEEALYCNSHNSLDLNYLNGTVTNGSVCSVHSVNSLNCSQSFIQASPVSSNLSIPGSDIMRADYIPSHRHSAIIVPSYRPTPDYETVMRQMKRGILHTDSQSQSLRNLNIINTHAYNQPEDLVYSQPEMRERHPYTVPYGPQGVYSNKLVSPSDQRNPKNNVVPSKPGASAISHTVSTPELANMQLQGSHNYSTAHMLKNYLFRPPPPYPRPRPATSTPDLASHRHKYVSGSSPDLVTRKVQLSVKTFQEDSSPVVHQSLQEVSEPLTATKHHGTVNKRHSLEVMNSMVRGMEAMTLKSLHLPMARRNTLREQGPPEEGSGSHEVPQLPQYHHKKTFSDATMLIHSSESEEEEEEAPESVPQIPMLREKMEYSAQLQAALARIPNKPPPEYPGPRKSVSNGALRQDQASLPPAMARARVLRHGPAKAISMSRTDPPAVNGASLGPSISEPDLTSVKERVKKEPVKERPVSEMFSLEDSIIEREMMIRNLEKQKMAGLEAQKRPLMLAALNGLSVARVSGREENRVDATRVPMDERFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQNSRLI
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
6Ubiquitination--MPFGLKLRRTRRY
--CCCCCCCHHHHHH
40.08-
13PhosphorylationKLRRTRRYNVLSKNC
CCHHHHHHCCCCCCC
13.3124719451
18UbiquitinationRRYNVLSKNCFVTRI
HHHCCCCCCCEEEEE
54.28-
23PhosphorylationLSKNCFVTRIRLLDS
CCCCCEEEEEEEECC
10.5024719451
265PhosphorylationGNITHNKSTILVELI
CCCCCCCCEEEEEEC
26.4630622161
266PhosphorylationNITHNKSTILVELIN
CCCCCCCEEEEEECC
21.6830622161
274UbiquitinationILVELINKEETALFH
EEEEECCCCHHEEEE
50.35-
289UbiquitinationTDDIENAKYISRLFA
CCCHHHHHHHHHHHH
55.49-
309PhosphorylationYKQNKICTEQSNSPP
HHHCCCCCCCCCCCC
40.3023927012
312PhosphorylationNKICTEQSNSPPPIR
CCCCCCCCCCCCCCC
32.8023927012
314PhosphorylationICTEQSNSPPPIRRQ
CCCCCCCCCCCCCCC
43.9919664994
323PhosphorylationPPIRRQPTWSRSSLP
CCCCCCCCCCCCCCC
27.9523312004
327PhosphorylationRQPTWSRSSLPRQQP
CCCCCCCCCCCCCCC
30.6120363803
328PhosphorylationQPTWSRSSLPRQQPY
CCCCCCCCCCCCCCC
41.0829496963
414PhosphorylationSPVSSNLSIPGSDIM
CCCCCCCCCCCHHHC
30.87-
425PhosphorylationSDIMRADYIPSHRHS
HHHCCCCCCCCCCCC
17.4727642862
428PhosphorylationMRADYIPSHRHSAII
CCCCCCCCCCCCEEE
24.4828857561
432PhosphorylationYIPSHRHSAIIVPSY
CCCCCCCCEEEECCC
22.5627422710
438PhosphorylationHSAIIVPSYRPTPDY
CCEEEECCCCCCCCH
23.9129978859
439PhosphorylationSAIIVPSYRPTPDYE
CEEEECCCCCCCCHH
17.9729978859
442PhosphorylationIVPSYRPTPDYETVM
EECCCCCCCCHHHHH
21.5729978859
445PhosphorylationSYRPTPDYETVMRQM
CCCCCCCHHHHHHHH
18.0729978859
447PhosphorylationRPTPDYETVMRQMKR
CCCCCHHHHHHHHHC
17.2429978859
459PhosphorylationMKRGILHTDSQSQSL
HHCCCCCCCCCCHHH
33.6229255136
461PhosphorylationRGILHTDSQSQSLRN
CCCCCCCCCCHHHHC
32.6529255136
463PhosphorylationILHTDSQSQSLRNLN
CCCCCCCCHHHHCCC
26.2029255136
465PhosphorylationHTDSQSQSLRNLNII
CCCCCCHHHHCCCEE
34.2529255136
474PhosphorylationRNLNIINTHAYNQPE
HCCCEEECCCCCCHH
9.4723403867
477PhosphorylationNIINTHAYNQPEDLV
CEEECCCCCCHHHCC
13.5123403867
485PhosphorylationNQPEDLVYSQPEMRE
CCHHHCCCCCCCHHH
14.6429255136
486PhosphorylationQPEDLVYSQPEMRER
CHHHCCCCCCCHHHC
31.6017525332
496PhosphorylationEMRERHPYTVPYGPQ
CHHHCCCCCCCCCCC
17.7826356563
497PhosphorylationMRERHPYTVPYGPQG
HHHCCCCCCCCCCCC
21.3226356563
500PhosphorylationRHPYTVPYGPQGVYS
CCCCCCCCCCCCCCC
36.7827642862
506PhosphorylationPYGPQGVYSNKLVSP
CCCCCCCCCCCCCCC
17.2226356563
507PhosphorylationYGPQGVYSNKLVSPS
CCCCCCCCCCCCCCH
25.6927642862
509UbiquitinationPQGVYSNKLVSPSDQ
CCCCCCCCCCCCHHC
44.30-
512PhosphorylationVYSNKLVSPSDQRNP
CCCCCCCCCHHCCCC
29.1730266825
514PhosphorylationSNKLVSPSDQRNPKN
CCCCCCCHHCCCCCC
38.5830266825
526PhosphorylationPKNNVVPSKPGASAI
CCCCCCCCCCCCCCE
39.6129978859
527UbiquitinationKNNVVPSKPGASAIS
CCCCCCCCCCCCCEE
41.21-
531PhosphorylationVPSKPGASAISHTVS
CCCCCCCCCEECCCC
31.8622496350
534PhosphorylationKPGASAISHTVSTPE
CCCCCCEECCCCCHH
16.9023927012
536PhosphorylationGASAISHTVSTPELA
CCCCEECCCCCHHHH
14.9023927012
538PhosphorylationSAISHTVSTPELANM
CCEECCCCCHHHHHC
39.1222496350
539PhosphorylationAISHTVSTPELANMQ
CEECCCCCHHHHHCC
19.2223927012
550PhosphorylationANMQLQGSHNYSTAH
HHCCCCCCCCCCHHH
8.8025002506
553PhosphorylationQLQGSHNYSTAHMLK
CCCCCCCCCHHHHHH
11.2825002506
554PhosphorylationLQGSHNYSTAHMLKN
CCCCCCCCHHHHHHH
25.1625002506
555PhosphorylationQGSHNYSTAHMLKNY
CCCCCCCHHHHHHHH
15.3825002506
562PhosphorylationTAHMLKNYLFRPPPP
HHHHHHHHHCCCCCC
12.9627642862
577PhosphorylationYPRPRPATSTPDLAS
CCCCCCCCCCCCHHH
35.5030266825
578PhosphorylationPRPRPATSTPDLASH
CCCCCCCCCCCHHHH
39.8030266825
579PhosphorylationRPRPATSTPDLASHR
CCCCCCCCCCHHHHC
19.2330266825
584PhosphorylationTSTPDLASHRHKYVS
CCCCCHHHHCHHCCC
28.4922617229
588UbiquitinationDLASHRHKYVSGSSP
CHHHHCHHCCCCCCC
47.51-
589PhosphorylationLASHRHKYVSGSSPD
HHHHCHHCCCCCCCC
8.1723927012
591PhosphorylationSHRHKYVSGSSPDLV
HHCHHCCCCCCCCHH
29.8430266825
593PhosphorylationRHKYVSGSSPDLVTR
CHHCCCCCCCCHHHC
31.0629255136
594PhosphorylationHKYVSGSSPDLVTRK
HHCCCCCCCCHHHCE
26.4229255136
599PhosphorylationGSSPDLVTRKVQLSV
CCCCCHHHCEEEEEE
31.8823927012
601UbiquitinationSPDLVTRKVQLSVKT
CCCHHHCEEEEEEEE
25.60-
605PhosphorylationVTRKVQLSVKTFQED
HHCEEEEEEEECCCC
12.4129759185
607UbiquitinationRKVQLSVKTFQEDSS
CEEEEEEEECCCCCC
40.00-
608PhosphorylationKVQLSVKTFQEDSSP
EEEEEEEECCCCCCC
28.5323403867
613PhosphorylationVKTFQEDSSPVVHQS
EEECCCCCCCHHHHH
35.4730243723
614PhosphorylationKTFQEDSSPVVHQSL
EECCCCCCCHHHHHH
33.7530243723
620PhosphorylationSSPVVHQSLQEVSEP
CCCHHHHHHHHHCCC
19.6930266825
625PhosphorylationHQSLQEVSEPLTATK
HHHHHHHCCCCCCCC
32.5130243723
629PhosphorylationQEVSEPLTATKHHGT
HHHCCCCCCCCCCCC
42.8930266825
631PhosphorylationVSEPLTATKHHGTVN
HCCCCCCCCCCCCCC
26.1923403867
642PhosphorylationGTVNKRHSLEVMNSM
CCCCHHHHHHHHHHH
30.2030266825
648PhosphorylationHSLEVMNSMVRGMEA
HHHHHHHHHHCHHHH
10.6829255136
670PhosphorylationLPMARRNTLREQGPP
CCHHHHCCHHHHCCC
25.9427251275
681PhosphorylationQGPPEEGSGSHEVPQ
HCCCCCCCCCCCCCC
40.16-
683PhosphorylationPPEEGSGSHEVPQLP
CCCCCCCCCCCCCCC
20.40-
697PhosphorylationPQYHHKKTFSDATML
CCCCCCCCCCCCEEE
32.9229514088
699PhosphorylationYHHKKTFSDATMLIH
CCCCCCCCCCEEEEC
31.4129514088
702PhosphorylationKKTFSDATMLIHSSE
CCCCCCCEEEECCCC
19.9429514088
707PhosphorylationDATMLIHSSESEEEE
CCEEEECCCCCHHHH
28.8927422710
708PhosphorylationATMLIHSSESEEEEE
CEEEECCCCCHHHHH
30.8627422710
710PhosphorylationMLIHSSESEEEEEEA
EEECCCCCHHHHHHC
52.8627422710
720PhosphorylationEEEEAPESVPQIPML
HHHHCCCCCCCCHHH
37.7329514088
733PhosphorylationMLREKMEYSAQLQAA
HHHHHHHHHHHHHHH
13.0522817900
747UbiquitinationALARIPNKPPPEYPG
HHHCCCCCCCCCCCC
54.25-
757UbiquitinationPEYPGPRKSVSNGAL
CCCCCCCCCCCCCCC
59.34-
758PhosphorylationEYPGPRKSVSNGALR
CCCCCCCCCCCCCCC
31.8630266825
760PhosphorylationPGPRKSVSNGALRQD
CCCCCCCCCCCCCCC
36.3230266825
787UbiquitinationVLRHGPAKAISMSRT
HHHHCCCCEEEECCC
49.76-
790PhosphorylationHGPAKAISMSRTDPP
HCCCCEEEECCCCCC
18.6322199227
792PhosphorylationPAKAISMSRTDPPAV
CCCEEEECCCCCCCC
25.8223090842
794PhosphorylationKAISMSRTDPPAVNG
CEEEECCCCCCCCCC
45.6222199227
803PhosphorylationPPAVNGASLGPSISE
CCCCCCCCCCCCCCC
34.9523403867
807PhosphorylationNGASLGPSISEPDLT
CCCCCCCCCCCCCCH
36.6330266825
809PhosphorylationASLGPSISEPDLTSV
CCCCCCCCCCCCHHH
47.6230266825
814PhosphorylationSISEPDLTSVKERVK
CCCCCCCHHHHHHHH
38.5630266825
815PhosphorylationISEPDLTSVKERVKK
CCCCCCHHHHHHHHC
38.1930278072
817UbiquitinationEPDLTSVKERVKKEP
CCCCHHHHHHHHCCC
39.30-
831PhosphorylationPVKERPVSEMFSLED
CCCCCCHHHCCCHHH
26.4830266825
835PhosphorylationRPVSEMFSLEDSIIE
CCHHHCCCHHHHHHH
29.5523403867
839PhosphorylationEMFSLEDSIIEREMM
HCCCHHHHHHHHHHH
18.9824719451
874PhosphorylationLAALNGLSVARVSGR
HHHHCCCEEEEECCC
18.3523403867
911PhosphorylationLEEGMVFTEYEQIPK
HHHCCCCEEHHHCCH
26.6729978859
913PhosphorylationEGMVFTEYEQIPKKK
HCCCCEEHHHCCHHH
15.2929978859
920UbiquitinationYEQIPKKKANGIFST
HHHCCHHHCCCCCCC
53.89-
956UbiquitinationRVELIPTKENNTGYI
CEEEEECCCCCCCCE
53.76-
1009PhosphorylationVNVIAMVTAEEEGGR
CCEEEEEECCCCCCC
18.44-
1029UbiquitinationYWPKLGSKHSSATYG
CCCCCCCCCCCCCCC
45.79-
1037UbiquitinationHSSATYGKFKVTTKF
CCCCCCCEEEEEEEE
31.43-
1042PhosphorylationYGKFKVTTKFRTDSV
CCEEEEEEEECCCCE
31.0424719451
1048PhosphorylationTTKFRTDSVCYATTG
EEEECCCCEEEECCC
17.3024719451
1059UbiquitinationATTGLKVKHLLSGQE
ECCCCEEEEECCCCC
27.27-
1128PhosphorylationCSAGVGRTGVLILSE
CCCCCCHHHHHHHHH
26.22-
1170PhosphorylationMIQTIAQYKFVYQVL
HHHHHHHHHHHHHHH
9.4330576142
1171AcetylationIQTIAQYKFVYQVLI
HHHHHHHHHHHHHHH
19.1020167786

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 PTN14_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTN14_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 PTN14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
12808048
CTNA1_HUMANCTNNA1physical
12808048
ZO1_HUMANTJP1physical
12808048
PLAK_HUMANJUPphysical
12808048
AMOT_HUMANAMOTphysical
22948661
1433E_HUMANYWHAEphysical
22948661
CUL2_HUMANCUL2physical
22948661
YAP1_HUMANYAP1physical
22948661
PLK1_HUMANPLK1physical
22948661
DDB1_HUMANDDB1physical
22948661
2AAA_HUMANPPP2R1Aphysical
22948661
2ABA_HUMANPPP2R2Aphysical
22948661
KIBRA_HUMANWWC1physical
22948661
1433Z_HUMANYWHAZphysical
22948661
1433B_HUMANYWHABphysical
22948661
WWC2_HUMANWWC2physical
22948661
UBC_HUMANUBCphysical
22948661
CSN4_HUMANCOPS4physical
22948661
STK3_HUMANSTK3physical
22948661
LLR1_HUMANLRR1physical
22948661
WWP1_HUMANWWP1physical
22948661
WWP2_HUMANWWP2physical
22948661
KC1D_HUMANCSNK1Dphysical
22948661
VHL_HUMANVHLphysical
22948661
KIBRA_HUMANWWC1physical
25023289
LATS1_HUMANLATS1physical
25023289
CRLF3_HUMANCRLF3physical
27880917
PDLI7_HUMANPDLIM7physical
27880917
MAGI1_HUMANMAGI1physical
28514442
MAGI3_HUMANMAGI3physical
28514442
YAP1_HUMANYAP1physical
28514442
STXB4_HUMANSTXBP4physical
28514442
ACD11_HUMANACAD11physical
28514442
PTN14_HUMANPTPN14physical
27432908
STXB4_HUMANSTXBP4physical
27432908
LLR1_HUMANLRR1physical
27432908
CUL2_HUMANCUL2physical
27432908
YAP1_HUMANYAP1physical
27432908
AMOT_HUMANAMOTphysical
27432908
ACD11_HUMANACAD11physical
27432908
KIBRA_HUMANWWC1physical
27432908
WWC2_HUMANWWC2physical
27432908
ANR50_HUMANANKRD50physical
27432908
RMD5A_HUMANRMND5Aphysical
27432908
BAG3_HUMANBAG3physical
27432908
HECW2_HUMANHECW2physical
27432908
MAEA_HUMANMAEAphysical
27432908
PLK1_HUMANPLK1physical
27432908
WDR26_HUMANWDR26physical
27432908
ARMC8_HUMANARMC8physical
27432908
1433F_HUMANYWHAHphysical
27432908
CSN1_HUMANGPS1physical
27432908
PDLI7_HUMANPDLIM7physical
27432908
STK3_HUMANSTK3physical
27432908
AMERL_HUMANAMMECR1Lphysical
27432908
NDEL1_HUMANNDEL1physical
27432908
CSN4_HUMANCOPS4physical
27432908
ACAD8_HUMANACAD8physical
27432908
BPIB1_HUMANBPIFB1physical
27432908
ATE1_HUMANATE1physical
27432908
RBP10_HUMANRANBP10physical
27432908
1433G_HUMANYWHAGphysical
27432908
USP9X_HUMANUSP9Xphysical
27432908
KIF2A_HUMANKIF2Aphysical
27432908
1433B_HUMANYWHABphysical
27432908
WWP1_HUMANWWP1physical
27432908
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CING_HUMANCGNphysical
27173435
LRFN1_HUMANLRFN1physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
RTKN_HUMANRTKNphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
MAST3_HUMANMAST3physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
PPM1H_HUMANPPM1Hphysical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
INP5E_HUMANINPP5Ephysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613611Choanal atresia and lymphedema (CHATLY)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTN14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578 AND SER-594, ANDMASS SPECTROMETRY.
"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-593 AND SER-594, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND MASSSPECTROMETRY.
"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-584, AND MASSSPECTROMETRY.

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