TNPO3_HUMAN - dbPTM
TNPO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNPO3_HUMAN
UniProt AC Q9Y5L0
Protein Name Transportin-3
Gene Name TNPO3
Organism Homo sapiens (Human).
Sequence Length 923
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains..
Protein Sequence MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
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-------MEGAKPTL
-------CCCCCCHH
10.9319413330
5Acetylation---MEGAKPTLQLVY
---CCCCCCHHHHHH
49.7621339330
19PhosphorylationYQAVQALYHDPDPSG
HHHHHHHHCCCCCCC
13.7520068231
59PhosphorylationQIRQDVESCYFAAQT
HHHHHHHHHHHHHHH
17.6127067055
61PhosphorylationRQDVESCYFAAQTMK
HHHHHHHHHHHHHHH
12.9227067055
66PhosphorylationSCYFAAQTMKMKIQT
HHHHHHHHHHHHHEE
17.6527067055
68UbiquitinationYFAAQTMKMKIQTSF
HHHHHHHHHHHEECE
40.19-
73PhosphorylationTMKMKIQTSFYELPT
HHHHHHEECEECCCC
25.0320873877
74PhosphorylationMKMKIQTSFYELPTD
HHHHHEECEECCCCC
14.9520873877
76PhosphorylationMKIQTSFYELPTDSH
HHHEECEECCCCCCC
19.1420873877
80PhosphorylationTSFYELPTDSHASLR
ECEECCCCCCCHHHH
63.8620873877
82PhosphorylationFYELPTDSHASLRDS
EECCCCCCCHHHHHH
24.3520873877
85PhosphorylationLPTDSHASLRDSLLT
CCCCCCHHHHHHHHH
20.6520068231
89PhosphorylationSHASLRDSLLTHIQN
CCHHHHHHHHHHHHH
20.8820873877
92PhosphorylationSLRDSLLTHIQNLKD
HHHHHHHHHHHHHHC
23.4020873877
190UbiquitinationLLMTCVEKAGTDEKM
HHHHHHHHHCCCHHH
31.55-
2912-HydroxyisobutyrylationVAREDLDKVLNYCRI
HHHHHHHHHHHHHHH
56.79-
355UbiquitinationRLGEHLYKTNDEVIH
HHCCHHHHCCHHHHH
47.41-
501 (in isoform 5)Phosphorylation-25.9428348404
513UbiquitinationLMKGLCEKPLASAAA
HHHCCCCCHHHHHHH
44.31-
513AcetylationLMKGLCEKPLASAAA
HHHCCCCCHHHHHHH
44.3125953088
521UbiquitinationPLASAAAKAIHNICS
HHHHHHHHHHHHHHH
43.05-
530UbiquitinationIHNICSVCRDHMAQH
HHHHHHHHHHHHHHH
2.1321890473
554PhosphorylationSLDSFLLSPEAAVGL
HHHHHHCCHHHHHHH
23.88-
594 (in isoform 3)Ubiquitination-56.3521890473
594AcetylationVQVMALKKLLSQEPS
HHHHHHHHHHCCCCC
56.3525953088
594 (in isoform 2)Ubiquitination-56.3521890473
594UbiquitinationVQVMALKKLLSQEPS
HHHHHHHHHHCCCCC
56.352189047
628 (in isoform 1)Ubiquitination-36.6621890473
646PhosphorylationQEIWPVLSETLNKHR
HHHHHHHHHHHHHHC
28.8620873877
648PhosphorylationIWPVLSETLNKHRAD
HHHHHHHHHHHHCCC
32.0520873877
877AcetylationRWLENSLKGLPKETT
HHHHHHCCCCCCCCC
59.2225953088
883PhosphorylationLKGLPKETTVGAVTV
CCCCCCCCCCCEEEE
32.6719690332
891PhosphorylationTVGAVTVTHKQLTDF
CCCEEEEEHHHHHHH
17.6219690332
896 (in isoform 3)Phosphorylation-33.8425599653
896PhosphorylationTVTHKQLTDFHKQVT
EEEHHHHHHHHHHCC
33.8410366588
900AcetylationKQLTDFHKQVTSAEE
HHHHHHHHHCCCHHH
46.5923749302
909AcetylationVTSAEECKQVCWALR
CCCHHHHHHHHHHHH
49.3925953088

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 TNPO3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNPO3_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 TNPO3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE3A_HUMANUBE3Aphysical
22939629
ARP3_HUMANACTR3physical
22863883
ARPC2_HUMANARPC2physical
22863883
FEN1_HUMANFEN1physical
22863883
HNRH1_HUMANHNRNPH1physical
22863883
IPO9_HUMANIPO9physical
22863883
PFD6_HUMANPFDN6physical
22863883
PP2AA_HUMANPPP2CAphysical
22863883
PP2BA_HUMANPPP3CAphysical
22863883
TTL12_HUMANTTLL12physical
22863883
STOM_HUMANSTOMphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608423Limb-girdle muscular dystrophy 1F (LGMD1F)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNPO3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-896, AND MASSSPECTROMETRY.

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