ALP4_SCHPO - dbPTM
ALP4_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALP4_SCHPO
UniProt AC Q9Y705
Protein Name Spindle pole body component alp4
Gene Name alp4
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 784
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Localizes to the SPB and also to the equatorial MTOC.
Protein Description Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles. Required for correct septation..
Protein Sequence MVRSISSVLAKEESENGSPIPALEEGSVYHVSLKSEGVSPFSDRIQLNYLYDGKTFSDPSNLNIHQQEACLINELLNAFMGMEGVFVHLQDMKASSEFETIIMPPSFYILPGFDLGIKDIASEMLEMGSHYLSITAFIESRSHFEYGFVNHALCAALRKFVMDYVVLIMQCENQSRIDPNFSLQTLRLYTLPTSRSLRQVYLILRDLLLSMEKNASSSDDLGLSNIDDLLEQLNEGNDISHVVNATRSKKKVCKGGQVISFLTESLTKYAGDPVARKILTYLLREASRPYTKMLNEWIHLGLVNDPYDEFMIKIHKGITSMQLDEDYTDEYWEKRYVIREDQVPPQLLDLQNKVLFAGKYLNVVLECRKGVNNLASLNAKDDTQNQLLWPSTFDDDNFTLNIMNAYVYANESLLQLLQSSQSLYAHLYSLKHYFFLDQSDFFTTFLDNAQHELRKPAKYISITKLQSQLDLALRQPGTITATDPHKEYVTVEVNQTSLIDWLMHIVSISGLEEGTSSQGNEVWNESITKQADVGNETRNFESEHNRSTQGTSKVGSDKDINGFETMQLCYKVPFPLSLILSRKAIIRYQLLFRYFLLLRHVEMQLENSWVQHSKNSAWRLNSSNAKIEQWKRNSWLLRTRMLSFVQKIIYYTTSEVIETHWGKFMGELENARTVDNLMQEHIDFLDTCLKECMLTNSRLLKVQSKLLNTCAMFASYTSTFTRSLYLLENSEESFDEGRMDKMEEILRRYEDSFSRHLKSLVNACNYFASTETAALLSLVMKLTG
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
4Phosphorylation----MVRSISSVLAK
----CCCCHHHHHHH
18.5324763107
6Phosphorylation--MVRSISSVLAKEE
--CCCCHHHHHHHHH
18.6824763107
7Phosphorylation-MVRSISSVLAKEES
-CCCCHHHHHHHHHC
21.3424763107
14PhosphorylationSVLAKEESENGSPIP
HHHHHHHCCCCCCCC
37.1429996109
18PhosphorylationKEESENGSPIPALEE
HHHCCCCCCCCCCCC
31.1025720772
35PhosphorylationVYHVSLKSEGVSPFS
EEEEEEECCCCCCCC
44.8921712547
39PhosphorylationSLKSEGVSPFSDRIQ
EEECCCCCCCCCEEE
30.9628889911
42PhosphorylationSEGVSPFSDRIQLNY
CCCCCCCCCEEEEEE
29.3929996109
216PhosphorylationLSMEKNASSSDDLGL
HHHHHCCCCCCCCCC
39.5129996109
224PhosphorylationSSDDLGLSNIDDLLE
CCCCCCCCCHHHHHH
29.9121712547
240PhosphorylationLNEGNDISHVVNATR
HHCCCCHHHHHHHCC
17.0621712547

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 ALP4_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALP4_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 ALP4_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAD2_SCHPOmad2genetic
11080156
TBG_SCHPOgtb1genetic
15280226
MAD2_SCHPOmad2physical
16855399
ALP6_SCHPOalp6physical
16855399
TBG_SCHPOgtb1physical
16855399
TBG_SCHPOgtb1physical
11080156
ALP16_SCHPOalp16physical
15004232
TBG_SCHPOgtb1physical
15004232
MBO1_SCHPOmto1physical
15004232
GFH1_SCHPOgfh1physical
15004232
PCP1_SCHPOpcp1physical
15004232
ALP6_SCHPOalp6physical
15004232
MBO1_SCHPOmto1physical
15120067
TBG_SCHPOgtb1physical
12134075
ALP16_SCHPOalp16physical
17021256
GFH1_SCHPOgfh1physical
17021256
MOD21_SCHPOmod21physical
17021256
ALP16_SCHPOalp16genetic
12134075
ALP6_SCHPOalp6physical
23886939
GCP3_HUMANTUBGCP3physical
23886939
GCP2_HUMANTUBGCP2physical
23886939

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALP4_SCHPO

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Related Literatures of Post-Translational Modification

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