EFC4B_HUMAN - dbPTM
EFC4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFC4B_HUMAN
UniProt AC Q9BSW2
Protein Name EF-hand calcium-binding domain-containing protein 4B
Gene Name CRACR2A
Organism Homo sapiens (Human).
Sequence Length 395
Subcellular Localization Cytoplasm .
Protein Description Ca(2+)-binding protein that plays a key role in store-operated Ca(2+) entry (SOCE) in T-cells by regulating CRAC channel activation. Acts as a cytoplasmic calcium-sensor that facilitates the clustering of ORAI1 and STIM1 at the junctional regions between the plasma membrane and the endoplasmic reticulum upon low Ca(2+) concentration. It thereby regulates CRAC channel activation, including translocation and clustering of ORAI1 and STIM1. Upon increase of cytoplasmic Ca(2+) resulting from opening of CRAC channels, dissociates from ORAI1 and STIM1, thereby destabilizing the ORAI1-STIM1 complex..
Protein Sequence MAAPDGRVVSRPQRLGQGSGQGPKGSGACLHPLDSLEQKETQEQTSGQLVMLRKAQEFFQTCDAEGKGFIARKDMQRLHKELPLSLEELEDVFDALDADGNGYLTPQEFTTGFSHFFFSQNNPSQEDAGEQVAQRHEEKVYLSRGDEDLGDMGEDEEAQFRMLMDRLGAQKVLEDESDVKQLWLQLKKEEPHLLSNFEDFLTRIISQLQEAHEEKNELECALKRKIAAYDEEIQHLYEEMEQQIKSEKEQFLLKDTERFQARSQELEQKLLCKEQELEQLTQKQKRLEGQCTALHHDKHETKAENTKLKLTNQELARELERTSWELQDAQQQLESLQQEACKLHQEKEMEVYRVTESLQREKAGLLKQLDFLRCVGGHWPVLRAPPRSLGSEGPV
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
10PhosphorylationAPDGRVVSRPQRLGQ
CCCCCEECCCCCCCC
35.0726074081
19PhosphorylationPQRLGQGSGQGPKGS
CCCCCCCCCCCCCCC
21.7626074081
26PhosphorylationSGQGPKGSGACLHPL
CCCCCCCCCCCCCCC
29.3726657352
35PhosphorylationACLHPLDSLEQKETQ
CCCCCCCHHCCHHHH
41.3026657352
41PhosphorylationDSLEQKETQEQTSGQ
CHHCCHHHHCCCCHH
44.4328348404
51SulfoxidationQTSGQLVMLRKAQEF
CCCHHEEHHHHHHHH
3.9921406390
54UbiquitinationGQLVMLRKAQEFFQT
HHEEHHHHHHHHHHH
50.9229967540
67UbiquitinationQTCDAEGKGFIARKD
HHCCCCCCCEEEHHH
42.0029967540
141PhosphorylationQRHEEKVYLSRGDED
HHHHHHHHCCCCCCC
15.2729978859
143PhosphorylationHEEKVYLSRGDEDLG
HHHHHHCCCCCCCCC
19.2729978859
152SulfoxidationGDEDLGDMGEDEEAQ
CCCCCCCCCCCHHHH
6.3421406390
171UbiquitinationMDRLGAQKVLEDESD
HHHHCCHHHHCCHHH
48.5329967540
237PhosphorylationDEEIQHLYEEMEQQI
HHHHHHHHHHHHHHH
14.0228796482
263PhosphorylationTERFQARSQELEQKL
HHHHHHHHHHHHHHH
30.9029255136
269UbiquitinationRSQELEQKLLCKEQE
HHHHHHHHHHCCHHH
33.7729967540
292PhosphorylationKRLEGQCTALHHDKH
HHHHHHHHHHCCCCC
25.11-
301PhosphorylationLHHDKHETKAENTKL
HCCCCCCHHHCCCHH
34.96-
309UbiquitinationKAENTKLKLTNQELA
HHCCCHHHCCHHHHH
55.6229967540
311PhosphorylationENTKLKLTNQELARE
CCCHHHCCHHHHHHH
33.01-
322PhosphorylationLARELERTSWELQDA
HHHHHHHHHHHHHHH
28.9027690223
323PhosphorylationARELERTSWELQDAQ
HHHHHHHHHHHHHHH
25.4427690223
342UbiquitinationSLQQEACKLHQEKEM
HHHHHHHHHHHHHHH
56.9329967540
355PhosphorylationEMEVYRVTESLQREK
HHHHHHHHHHHHHHH
15.7424719451
357PhosphorylationEVYRVTESLQREKAG
HHHHHHHHHHHHHCH
22.0423403867
388O-linked_GlycosylationVLRAPPRSLGSEGPV
HHCCCCCCCCCCCCC
42.7430379171
391O-linked_GlycosylationAPPRSLGSEGPV---
CCCCCCCCCCCC---
44.6830379171
391PhosphorylationAPPRSLGSEGPV---
CCCCCCCCCCCC---
44.6822210691
397 (in isoform 2)Phosphorylation-29978859
400 (in isoform 2)Phosphorylation-28634120
403 (in isoform 2)Phosphorylation-29978859
408 (in isoform 2)Phosphorylation-28102081
410 (in isoform 2)Phosphorylation-26853621
414Ubiquitination--------------------------
--------------------------
29967540
415 (in isoform 2)Phosphorylation--
424 (in isoform 2)Phosphorylation-30266825
426 (in isoform 2)Phosphorylation-30266825
439 (in isoform 2)Phosphorylation-25849741
440 (in isoform 2)Phosphorylation-25849741
444 (in isoform 2)Phosphorylation-28450419
446 (in isoform 2)Phosphorylation-28450419
449 (in isoform 2)Phosphorylation-28450419
455 (in isoform 2)Phosphorylation-28634298
464 (in isoform 2)Phosphorylation-28634298
473 (in isoform 2)Phosphorylation-30266825
492 (in isoform 2)Phosphorylation-22210691
495 (in isoform 2)Phosphorylation-26657352
501 (in isoform 2)Phosphorylation-25072903
518 (in isoform 2)Phosphorylation-26657352
520 (in isoform 2)Phosphorylation-24719451
521 (in isoform 2)Phosphorylation-30266825
529 (in isoform 2)Ubiquitination--
537 (in isoform 2)Phosphorylation-30108239
538 (in isoform 2)Phosphorylation-30108239
540 (in isoform 2)Phosphorylation-30108239
571 (in isoform 2)Phosphorylation--
601 (in isoform 2)Phosphorylation--
607 (in isoform 2)Phosphorylation--
729Geranylgeranylation-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
27016526

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 EFC4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFC4B_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 EFC4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NT2NL_HUMANNOTCH2NLphysical
25416956
IF1AX_HUMANEIF1AXphysical
26186194
MCPH1_HUMANMCPH1physical
26186194
MCPH1_HUMANMCPH1physical
28514442
PLSI_HUMANPLS1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFC4B_HUMAN

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Related Literatures of Post-Translational Modification

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