IINMP_SCHPO - dbPTM
IINMP_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IINMP_SCHPO
UniProt AC O13681
Protein Name Integral inner nuclear membrane protein ima1
Gene Name IMA1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 615
Subcellular Localization Nucleus inner membrane
Multi-pass membrane protein .
Protein Description Inner nuclear membrane protein that specifically binds to heterochromatic regions and promotes the tethering of centromeric DNA to the SUN-KASH complex. Couples centromeres to the nuclear envelope, thus contributing to their association with the microtubule organizing center attachment site and to the positioning of the nucleus at the cell center by microtubules..
Protein Sequence MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPFYAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDANDYEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLLDGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFLLRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISILNNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSKFSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNRRNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA
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
14PhosphorylationFTLGLGNSDDGLKST
EEECCCCCCCCCHHH
25720772
66PhosphorylationEKGDILDYRPPTPTQ
CCCCCCCCCCCCCCC
21712547
70PhosphorylationILDYRPPTPTQDKGV
CCCCCCCCCCCCCCC
21712547
72PhosphorylationDYRPPTPTQDKGVGP
CCCCCCCCCCCCCCC
24763107
367PhosphorylationPRKKRQESTSSVHRI
CCCCCCCCCCCCHHC
21712547
368PhosphorylationRKKRQESTSSVHRIG
CCCCCCCCCCCHHCC
21712547
369PhosphorylationKKRQESTSSVHRIGK
CCCCCCCCCCHHCCC
24763107
370PhosphorylationKRQESTSSVHRIGKE
CCCCCCCCCHHCCCC
24763107
422PhosphorylationRERAPEESPMTFLQK
HHHCCCCCCCCHHHH
29996109
436PhosphorylationKKMAALPTSSPVRPM
HHHHCCCCCCCCCCC
21712547
437PhosphorylationKMAALPTSSPVRPML
HHHCCCCCCCCCCCC
21712547
438PhosphorylationMAALPTSSPVRPMLK
HHCCCCCCCCCCCCC
24763107
447PhosphorylationVRPMLKPTLQLQNSP
CCCCCCCEEECCCCC
21712547
453PhosphorylationPTLQLQNSPLSKLVP
CEEECCCCCHHHHCC
24763107
456PhosphorylationQLQNSPLSKLVPQEV
ECCCCCHHHHCCHHH
21712547
504PhosphorylationKNLPFSVSTLKSTAK
CCCCCCHHHHHHHCC
25720772
505PhosphorylationNLPFSVSTLKSTAKK
CCCCCHHHHHHHCCC
25720772
539PhosphorylationLESHFSKSLALQNDP
HHHHHCHHHHCCCCC
25720772

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 IINMP_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 IINMP_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUG61_SCHPOman1genetic
21880100
LEM2_SCHPOlem2genetic
21880100
SAD1_SCHPOsad1physical
21880100
IINMP_SCHPOima1physical
21880100
MUG61_SCHPOman1physical
21880100
LEM2_SCHPOlem2physical
21880100
IINMP_SCHPOima1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IINMP_SCHPO

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Related Literatures of Post-Translational Modification

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