TNPO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TNPO1_HUMAN
• UniProt AC: Q92973
• Protein Name: Transportin-1
• Gene Name: TNPO1
• Organism: Homo sapiens (Human).
• Sequence Length: 898
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. [PubMed: 24753571 Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19 (By similarity Mediates nuclear import of ADAR/ADAR1 isoform 1 and isoform 5 in a RanGTP-dependent manner]
• Protein Sequence: MVWDRQTKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDDDDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV

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
1	Acetylation	-------MVWDRQTK -------CCCCCCCC	6.58	-
1 (in isoform 2)	Acetylation	-	6.58	19413330
30	Phosphorylation	ILQLLKESQSPDTTI HHHHHHHCCCCCHHH	34.08	29255136
32	Phosphorylation	QLLKESQSPDTTIQR HHHHHCCCCCHHHHH	33.74	29255136
35	Phosphorylation	KESQSPDTTIQRTVQ HHCCCCCHHHHHHHH	29.23	29255136
36	Phosphorylation	ESQSPDTTIQRTVQQ HCCCCCHHHHHHHHH	23.61	29255136
44	Ubiquitination	IQRTVQQKLEQLNQY HHHHHHHHHHHHHCC	36.58	-
67	Phosphorylation	FVLTKLKSEDEPTRS HHHHCCCCCCCCCCC	61.79	21406692
73	Ubiquitination	KSEDEPTRSLSGLIL CCCCCCCCCCCHHHH	46.44	21906983
74	Phosphorylation	SEDEPTRSLSGLILK CCCCCCCCCCHHHHH	29.39	21406692
76	Phosphorylation	DEPTRSLSGLILKNN CCCCCCCCHHHHHCC	32.57	30108239
77 (in isoform 2)	Ubiquitination	-	23.25	21890473
81	Ubiquitination	SLSGLILKNNVKAHF CCCHHHHHCCHHHHH	39.21	21906983
81	Malonylation	SLSGLILKNNVKAHF CCCHHHHHCCHHHHH	39.21	26320211
85 (in isoform 1)	Ubiquitination	-	37.96	21890473
85	Ubiquitination	LILKNNVKAHFQNFP HHHHCCHHHHHHCCC	37.96	21890473
101	Phosphorylation	GVTDFIKSECLNNIG CHHHHHHHHHHHCCC	28.82	21712546
110	Phosphorylation	CLNNIGDSSPLIRAT HHHCCCCCCHHHHHH	28.74	21712546
111	Phosphorylation	LNNIGDSSPLIRATV HHCCCCCCHHHHHHH	28.59	24719451
142 (in isoform 3)	Ubiquitination	-	3.17	21890473
184 (in isoform 2)	Ubiquitination	-	2.73	21890473
192 (in isoform 1)	Ubiquitination	-	43.81	21890473
192	Acetylation	PKFLQFFKHSSPKIR HHHHHHHHCCCHHHH	43.81	25953088
192	Ubiquitination	PKFLQFFKHSSPKIR HHHHHHHHCCCHHHH	43.81	21890473
194	Phosphorylation	FLQFFKHSSPKIRSH HHHHHHCCCHHHHHH	49.26	-
307	Acetylation	VLVRHLPKLIPVLVN HHHHHHHHHHHHHHC	66.46	25953088
307	Ubiquitination	VLVRHLPKLIPVLVN HHHHHHHHHHHHHHC	66.46	-
319	Ubiquitination	LVNGMKYSDIDIILL HHCCCCCCCCEEEEE	23.67	21906983
327	Ubiquitination	DIDIILLKGDVEEDE CCEEEEEECCCCCCC	50.01	21906983
335	Phosphorylation	GDVEEDETIPDSEQD CCCCCCCCCCCCCCC	50.56	20873877
339	Phosphorylation	EDETIPDSEQDIRPR CCCCCCCCCCCCHHH	31.63	28985074
352	Phosphorylation	PRFHRSRTVAQQHDE HHHHHHCHHHHHCCC	22.80	30576142
385	Ubiquitination	ISDWNLRKCSAAALD CCHHHHHHHHHHHHH	35.39	-
473	Phosphorylation	TCWTLSRYAHWVVSQ HHHHHHHHCHHHHCC	10.23	-
495	Ubiquitination	PLMTELLKRILDSNK HHHHHHHHHHHHCCH	50.44	21890473
502	2-Hydroxyisobutyrylation	KRILDSNKRVQEAAC HHHHHCCHHHHHHHH	58.88	-
569	Phosphorylation	HHLNKPEYIQMLMPP HHCCCHHHHHHHCHH	12.65	-
585	Ubiquitination	IQKWNMLKDEDKDLF HHHHHCCCCCCCCHH	48.59	-
632	Sulfoxidation	QKTLAQAMLNNAQPD HHHHHHHHHHCCCCC	2.47	28183972
683	Glutathionylation	ILTLMYQCMQDKMPE HHHHHHHHHHHCCHH	1.14	22555962
694	Phosphorylation	KMPEVRQSSFALLGD CCHHHHHHHHHHHHH	19.50	21712546
695	Phosphorylation	MPEVRQSSFALLGDL CHHHHHHHHHHHHHH	13.24	21712546
774	Phosphorylation	NRPNTPKTLLENTAI CCCCCCCHHHHCCCE	37.47	20068231
779	Phosphorylation	PKTLLENTAITIGRL CCHHHHCCCEEECCC	15.29	20068231
782	Phosphorylation	LLENTAITIGRLGYV HHHCCCEEECCCCCC	18.21	20068231
813 (in isoform 3)	Ubiquitination	-	44.22	21890473
818	Ubiquitination	NIRDNEEKDSAFRGI CCCCCCCCCCCCCCC	51.29	-
855 (in isoform 2)	Ubiquitination	-	62.53	21890473
863	Ubiquitination	DLRDMFCKILHGFKN HHHHHHHHHHHHHHC	36.72	21890473
863 (in isoform 1)	Ubiquitination	-	36.72	21890473
863	Acetylation	DLRDMFCKILHGFKN HHHHHHHHHHHHHHC	36.72	25953088
869	Acetylation	CKILHGFKNQVGDEN HHHHHHHHCCCCCCC	51.57	25953088
869	Ubiquitination	CKILHGFKNQVGDEN HHHHHHHHCCCCCCC	51.57	-
881	Phosphorylation	DENWRRFSDQFPLPL CCCHHHHCCCCCCCH	28.79	25159151
889	2-Hydroxyisobutyrylation	DQFPLPLKERLAAFY CCCCCCHHHHHHHHH	38.56	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TNPO1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TNPO1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TNPO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUP98_HUMAN	NUP98	physical	9144189
NXF1_HUMAN	NXF1	physical	21965294
VPS16_HUMAN	VPS16	physical	22939629
TNPO3_HUMAN	TNPO3	physical	22939629
WAP53_HUMAN	WRAP53	physical	22939629
NAB2_YEAST	NAB2	physical	23535894
IPO4_HUMAN	IPO4	physical	22863883
IPO7_HUMAN	IPO7	physical	22863883
IREB2_HUMAN	IREB2	physical	22863883
PP2AA_HUMAN	PPP2CA	physical	22863883
TRXR1_HUMAN	TXNRD1	physical	22863883
IPO7_HUMAN	IPO7	physical	26344197
IPO8_HUMAN	IPO8	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
RAN_HUMAN	RAN	physical	26344197
RNBP6_HUMAN	RANBP6	physical	26344197
TBA4A_HUMAN	TUBA4A	physical	26344197
TBB3_HUMAN	TUBB3	physical	26344197
STOM_HUMAN	STOM	physical	27173435

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.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 19413330

Phosphorylation

"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-32, AND MASSSPECTROMETRY.
PubMed: 18691976