MAEA_HUMAN - dbPTM
MAEA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAEA_HUMAN
UniProt AC Q7L5Y9
Protein Name Macrophage erythroblast attacher
Gene Name MAEA
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Nucleus matrix . Cell membrane . Cytoplasm, cytoskeleton . Localized as nuclear speckled-like pattern.
Protein Description Plays a role in erythroblast enucleation and in the development of the mature macrophages. Mediates the attachment of erythroid cell to mature macrophages, in correlation with the presence of MAEA at cell surface of mature macrophages; This MAEA-mediated contact inhibits erythroid cells apoptosis. Participates in erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages. May contribute to nuclear architecture and cells division events..
Protein Sequence MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANSRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVVCPRTKEVFHFSQAEKVYIM
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
6Phosphorylation--MAVQESAAQLSMT
--CCHHHHHHHHHCE		16.2922210691
11PhosphorylationQESAAQLSMTLKVQE
HHHHHHHHCEEECHH		9.5322210691
13PhosphorylationSAAQLSMTLKVQEYP
HHHHHHCEEECHHCC		21.7620068231
19PhosphorylationMTLKVQEYPTLKVPY
CEEECHHCCCCCCCH		5.6117360941
21PhosphorylationLKVQEYPTLKVPYET
EECHHCCCCCCCHHH		38.0124043423
23 (in isoform 1)Ubiquitination-43.5821890473
23 (in isoform 2)Ubiquitination-43.5821890473
23 (in isoform 3)Ubiquitination-43.5821890473
23 (in isoform 4)Ubiquitination-43.5821890473
23 (in isoform 5)Ubiquitination-43.5821890473
23UbiquitinationVQEYPTLKVPYETLN
CHHCCCCCCCHHHHH		43.5821890473
28PhosphorylationTLKVPYETLNKRFRA
CCCCCHHHHHHHHHH		29.779763581
31 (in isoform 1)Ubiquitination-56.9021890473
31 (in isoform 2)Ubiquitination-56.9021890473
31 (in isoform 5)Ubiquitination-56.9021890473
31UbiquitinationVPYETLNKRFRAAQK
CCHHHHHHHHHHHHH		56.9021906983
31 (in isoform 3)Ubiquitination-56.9021890473
31 (in isoform 4)Ubiquitination-56.9021890473
38AcetylationKRFRAAQKNIDRETS
HHHHHHHHCCCCCHH		51.6623749302
38UbiquitinationKRFRAAQKNIDRETS
HHHHHHHHCCCCCHH		51.66-
45PhosphorylationKNIDRETSHVTMVVA
HCCCCCHHHHHHHHH		15.94-
61GlutathionylationLEKTLSGCPAVDSVV
HHHHHCCCCHHHHHH		1.4322555962
82UbiquitinationVEKLSVLKRKAVESI
HHHHHHHHHHHHHHH		50.09-
84UbiquitinationKLSVLKRKAVESIQA
HHHHHHHHHHHHHHC		56.0221906983
84 (in isoform 3)Ubiquitination-56.0221890473
84 (in isoform 4)Ubiquitination-56.0221890473
84 (in isoform 1)Ubiquitination-56.0221890473
84 (in isoform 5)Ubiquitination-56.0221890473
84 (in isoform 2)Ubiquitination-56.0221890473
97UbiquitinationQAEDESAKLCKRRIE
HCCHHHHHHHHHHHH		64.79-
107MethylationKRRIEHLKEHSSDQP
HHHHHHHHHCCCCCC		56.1242356881
107 (in isoform 1)Ubiquitination-56.1221890473
107 (in isoform 2)Ubiquitination-56.1221890473
107 (in isoform 3)Ubiquitination-56.1221890473
107 (in isoform 4)Ubiquitination-56.1221890473
107 (in isoform 5)Ubiquitination-56.1221890473
107UbiquitinationKRRIEHLKEHSSDQP
HHHHHHHHHCCCCCC		56.1221906983
121 (in isoform 2)Ubiquitination-45.9821890473
121 (in isoform 1)Ubiquitination-45.9821890473
121 (in isoform 3)Ubiquitination-45.9821890473
121 (in isoform 4)Ubiquitination-45.9821890473
121 (in isoform 5)Ubiquitination-45.9821890473
121UbiquitinationPAAASVWKRKRMDRM
CCHHHHHHHHHHHHH		45.9821906983
144UbiquitinationGYYNTAVKLARQSGI
CCHHHHHHHHHHCCC		33.68-
149 (in isoform 5)Phosphorylation-35.8621406692
153 (in isoform 5)Phosphorylation-54.7321406692
162PhosphorylationVNIEMFLTAKEVEES
HCHHHHEEHHHHHHH		25.1527067055
169PhosphorylationTAKEVEESLERRETA
EHHHHHHHHHHHHHH		23.2526091039
182 (in isoform 3)Ubiquitination-2.1021890473
182 (in isoform 2)Ubiquitination-2.1021890473
186AcetylationLAWCHDNKSRLRKMK
HHHHCCCHHHHHHHH		42.9025953088
186UbiquitinationLAWCHDNKSRLRKMK
HHHHCCCHHHHHHHH		42.90-
186MalonylationLAWCHDNKSRLRKMK
HHHHCCCHHHHHHHH		42.9026320211
223 (in isoform 1)Ubiquitination-50.1921890473
223UbiquitinationDAVRHARKHFSQAEG
HHHHHHHHHHHHHCC		50.192190698
252PhosphorylationFPPDTHISPYKDLLD
CCCCCCCCCCHHHCC		17.9926091039
299PhosphorylationAGLSAIKTPQCYKED
CCHHHCCCCCCCCCC		16.6928165663
304UbiquitinationIKTPQCYKEDGSSKS
CCCCCCCCCCCCCCC		57.88-
308PhosphorylationQCYKEDGSSKSPDCP
CCCCCCCCCCCCCCC		47.0929255136
309PhosphorylationCYKEDGSSKSPDCPV
CCCCCCCCCCCCCCC		42.5629255136
310UbiquitinationYKEDGSSKSPDCPVC
CCCCCCCCCCCCCCC		68.64-
311PhosphorylationKEDGSSKSPDCPVCS
CCCCCCCCCCCCCCC		28.1121815630
323SumoylationVCSRSLNKLAQPLPM
CCCCHHHHHCCCCCC		50.95-
323UbiquitinationVCSRSLNKLAQPLPM
CCCCHHHHHCCCCCC		50.95-
323SumoylationVCSRSLNKLAQPLPM
CCCCHHHHHCCCCCC		50.95-
360PhosphorylationPMMLPNGYVYGYNSL
CCCCCCCEEECCCCC		9.3524275569
362PhosphorylationMLPNGYVYGYNSLLS
CCCCCEEECCCCCEE		12.8624275569
369PhosphorylationYGYNSLLSIRQDDKV
ECCCCCEEEECCCEE		22.4824275569
375AcetylationLSIRQDDKVVCPRTK
EEEECCCEEECCCCC		44.8725953088
375UbiquitinationLSIRQDDKVVCPRTK
EEEECCCEEECCCCC		44.87-
382UbiquitinationKVVCPRTKEVFHFSQ
EEECCCCCCEEECCC		53.83-
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 MAEA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAEA_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 MAEA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RMD5A_HUMANRMND5Aphysical
17467196
CLIP1_HUMANCLIP1physical
22863883
RANB9_HUMANRANBP9physical
26344197
MKLN1_HUMANMKLN1physical
27173435
RBP10_HUMANRANBP10physical
27173435
RANB9_HUMANRANBP9physical
27173435
ARMC8_HUMANARMC8physical
27173435
WDR26_HUMANWDR26physical
27173435
HTRA2_HUMANHTRA2physical
27173435
DDX5_HUMANDDX5physical
27173435
CCD51_HUMANCCDC51physical
27173435
YPEL5_HUMANYPEL5physical
27173435
RAB8A_HUMANRAB8Aphysical
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
DB05389WF10
Regulatory Network of MAEA_HUMAN

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Related Literatures of Post-Translational Modification

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