SPN1_HUMAN - dbPTM
SPN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPN1_HUMAN
UniProt AC O95149
Protein Name Snurportin-1
Gene Name SNUPN
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Nucleus . Cytoplasm . Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta (PubMed:10209022, PubMed:12095920). It is re-exported to the cytoplasm by the XPO1-dependent nuclear export rece
Protein Description Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs..
Protein Sequence MEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTPESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKPDYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLMEN
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-------MEELSQAL
-------CHHHHHHH
9.0120068231
10PhosphorylationELSQALASSFSVSQD
HHHHHHHHCCCCCCC
32.5328348404
11PhosphorylationLSQALASSFSVSQDL
HHHHHHHCCCCCCCC
18.8828348404
13PhosphorylationQALASSFSVSQDLNS
HHHHHCCCCCCCCCC
23.8628348404
15PhosphorylationLASSFSVSQDLNSTA
HHHCCCCCCCCCCCC
19.4428348404
20PhosphorylationSVSQDLNSTAAPHPR
CCCCCCCCCCCCCCC
27.0728122231
21PhosphorylationVSQDLNSTAAPHPRL
CCCCCCCCCCCCCCH
26.2628122231
29PhosphorylationAAPHPRLSQYKSKYS
CCCCCCHHHHHHHHH
32.5120068231
31PhosphorylationPHPRLSQYKSKYSSL
CCCCHHHHHHHHHHH
17.5420068231
32UbiquitinationHPRLSQYKSKYSSLE
CCCHHHHHHHHHHHH
32.6029967540
34UbiquitinationRLSQYKSKYSSLEQS
CHHHHHHHHHHHHHH
45.03-
34SumoylationRLSQYKSKYSSLEQS
CHHHHHHHHHHHHHH
45.03-
34SumoylationRLSQYKSKYSSLEQS
CHHHHHHHHHHHHHH
45.03-
35PhosphorylationLSQYKSKYSSLEQSE
HHHHHHHHHHHHHHH
15.5828796482
36PhosphorylationSQYKSKYSSLEQSER
HHHHHHHHHHHHHHH
31.98-
37PhosphorylationQYKSKYSSLEQSERR
HHHHHHHHHHHHHHH
32.6028857561
41PhosphorylationKYSSLEQSERRRRLL
HHHHHHHHHHHHHHH
24.5621815630
52UbiquitinationRRLLELQKSKRLDYV
HHHHHHHHHHHHHHH
71.2529967540
71PhosphorylationRLAEDDWTGMESEEE
HHHHCCCCCCCCHHH
33.3830576142
75PhosphorylationDDWTGMESEEENKKD
CCCCCCCCHHHHCCC
41.2225159151
90PhosphorylationDEEMDIDTVKKLPKH
CHHCCHHHHHHHCHH
34.2629978859
92UbiquitinationEMDIDTVKKLPKHYA
HCCHHHHHHHCHHHH
51.1629967540
135PhosphorylationKRALIVASRGSTSAY
CCEEEEEECCCCCCC
26.7030576142
138PhosphorylationLIVASRGSTSAYTKS
EEEEECCCCCCCCCC
20.3422210691
142PhosphorylationSRGSTSAYTKSGYCV
ECCCCCCCCCCCCCC
17.9230576142
144UbiquitinationGSTSAYTKSGYCVNR
CCCCCCCCCCCCCHH
29.2521963094
147PhosphorylationSAYTKSGYCVNRFSS
CCCCCCCCCCHHHHH
10.5830576142
153PhosphorylationGYCVNRFSSLLPGGN
CCCCHHHHHCCCCCC
19.4823879269
154PhosphorylationYCVNRFSSLLPGGNR
CCCHHHHHCCCCCCC
31.0820873877
164PhosphorylationPGGNRRNSTAKDYTI
CCCCCCCCCCCCCCH
28.1223882029
165PhosphorylationGGNRRNSTAKDYTIL
CCCCCCCCCCCCCHH
41.0723882029
182O-linked_GlycosylationIYNEVNQTYYVLDVM
HCCCCCCEEEEEEEE
16.1829351928
199S-nitrosylationRGHPFYDCQTDFRFY
CCCCCCCCCCCCEEE
2.9824105792
221UbiquitinationEEEGLGEKTKLNPFK
CCCCCCCCCCCCCCC
49.5121906983
223UbiquitinationEGLGEKTKLNPFKFV
CCCCCCCCCCCCCCC
58.2829967540
228UbiquitinationKTKLNPFKFVGLKNF
CCCCCCCCCCCCCCC
40.1621890473
228UbiquitinationKTKLNPFKFVGLKNF
CCCCCCCCCCCCCCC
40.1621906983
298SumoylationPAGPLTTKPDYAGHQ
CCCCCCCCCCCHHHH
30.56-
301PhosphorylationPLTTKPDYAGHQLQQ
CCCCCCCCHHHHHHH
24.02-
325PhosphorylationEGMKEKLTHKASENG
HHHHHHHCCHHHHCC
32.1928348404
329PhosphorylationEKLTHKASENGHYEL
HHHCCHHHHCCCEEE
36.0821945579
334PhosphorylationKASENGHYELEHLST
HHHHCCCEEEEECCC
24.4921945579
340PhosphorylationHYELEHLSTPKLKGS
CEEEEECCCCCCCCC
44.5721945579
341PhosphorylationYELEHLSTPKLKGSS
EEEEECCCCCCCCCC
30.7021945579
347PhosphorylationSTPKLKGSSHSPDHP
CCCCCCCCCCCCCCC
24.2423401153
348PhosphorylationTPKLKGSSHSPDHPG
CCCCCCCCCCCCCCC
36.3322115753
350PhosphorylationKLKGSSHSPDHPGCL
CCCCCCCCCCCCCCC
33.6923401153
356S-nitrosylationHSPDHPGCLMEN---
CCCCCCCCCCCC---
3.7324105792

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
-KUbiquitinationE3 ubiquitin ligaseMEX3BQ6ZN04
PMID:24326307

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPN1_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 SPN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNNT3_HUMANTNNT3physical
16169070
ENOG_HUMANENO2physical
16169070
PEX5_HUMANPEX5physical
16169070
SMN_HUMANSMN1physical
12095920
DDX20_HUMANDDX20physical
12095920
RSMB_HUMANSNRPBphysical
12095920
ZPR1_HUMANZPR1physical
12095920
RAN_HUMANRANphysical
10209022
XPO1_HUMANXPO1physical
10209022
IMB1_HUMANKPNB1physical
10209022
DREB_HUMANDBN1physical
21900206
MEX3B_HUMANMEX3Bphysical
21900206
RN126_HUMANRNF126physical
21900206
PDP1_HUMANPDP1physical
26186194
TOE1_HUMANTOE1physical
26186194
EGLN1_HUMANEGLN1physical
26186194
UBP15_HUMANUSP15physical
26186194
SMD1_HUMANSNRPD1physical
26186194
PDP1_HUMANPDP1physical
28514442
TOE1_HUMANTOE1physical
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 SPN1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP