Protein detail

MPP9

M-phase phosphoprotein 9

Entry name
MPP9
UniProt ID
EVMP confidence score
0.50
Supporting publications (n)
1
Transmembrane count
Protein classification
Predicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
M-phase phosphoprotein 9
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
MPP9
Gene Description
M-phase phosphoprotein 9
Chromosome
12
Position
123152320-123244014
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization6
Tissue SpecifictestisCell SpecificAdrenal medulla cellsBlood Cell Specificintermediate monocyteBlood Lineage Specificdendritic cellsSecretome LocationIntracellular and membraneSecretome FunctionReceptor
Function & Pathway5
Relations & Evidence6

Ligand-Receptor Signaling (4)

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network (1)

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
TTBK2Q6IQ55MPP9Q99550YesNoYesSIGNORSIGNOR:30375385

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationR Sequencing23873186837922300
Sequence, Structure & Domains8

Sequences

Length
1,183
Mass
133,024
Sequence
MEEFDLVKTLHKTSSSVGSDENSLHSLGLNLNTDRSSPHLSTNGVSSFSGKTRPSVIQGTVEVLTSLMQELQNSGKTDSELWKNCETRWLQLFNLVEKQCQEQIVAQQEQFHNQIQHIQEEIKNLVKLQTSSASLASCEGNSSNKQVSSESQMGFFSLSSERNESVIHYPESTEPEIQQEMSTSQPDCNVDSCSVSSGYGTFCISELNLYKSKDPKEFMEHIDVPKGQYVAPAVPAESLVDGVKNENFYIQTPEECHVSLKEDVSISPGEFEHNFLGENKVSEVYSGKTNSNAITSWAQKLKQNQPKRAHVEDGGSRSKQGNEQSKKTPIEKSDFAAATHPRAFYLSKPDETPNAWMSDSGTGLTYWKLEEKDMHHSLPETLEKTFISLSSTDVSPNQSNTSNEMKLPSLKDIYYKKQRENKQLPERNLTSASNPNHPPEVLTLDPTLHMKPKQQISGIQPHGLPNALDDRISFSPDSVLEPSMSSPSDIDSFSQASNVTSQLPGFPKYPSHTKASPVDSWKNQTFQNESRTSSTFPSVYTITSNDISVNTVDEENTVMVASASVSQSQLPGTANSVPECISLTSLEDPVILSKIRQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISGVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRIHVRPSRANTLATSDVSRRKWLIPGAEYSIFTGQPLDTQDSNVDNQLEETCSLGHRSPLEKDSSPGSSSTSLLIKKQRETSDTPIMRALKELDEGKIFKNWGTQTEKEDTSNINPRQTETSVNASRSPEKCAQQRQKRLNSASQRSSSLPPSNRKSSTPTKREIMLTPVTVAYSPKRSPKENLSPGFSHLLSKNESSPIRFDILLDDLDTVPVSTLQRTNPRKQLQFLPLDDSEEKTYSEKATDNHVNHSSCPEPVPNGVKKVSVRTAWEKNKSVSYEQCKPVSVTPQGNDFEYTAKIRTLAETERFFDELTKEKDQIEAALSRMPSPGGRITLQTRLNQEALEDRLERINRELGSVRMTLKKFHVLRTSANL
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q99550-1; Sequence=Displayed; Name=2; IsoId=Q99550-2; Sequence=VSP_035838
Alternative Sequence
1151..1183; EALEDRLERINRELGSVRMTLKKFHVLRTSANL -> TPQICEESSHKCAFAGHYVPCHLYDYRFQG (in isoform 2)

Domain & Motif Annotations

Compositional Bias
324..334; Basic and acidic residues; 483..495; Low complexity; 921..936; Polar residues; 949..967; Low complexity
Coiled Coil
609..804; 1109..1174
Region
28..52; Disordered; 300..334; Disordered; 401..800; Required for its centrosomal localization; 451..500; Interaction with CEP97; 472..495; Disordered; 801..1031; Interaction with KIF24; 863..894; Disordered; 910..999; Disordered
Clinical Relevance4
Antibody
Interaction Protein (4)
ENSG00000108953ENSG00000164924ENSG00000170027ENSG00000264364
Interaction Count
4
Interaction Dataset (2)
biogrid_opencellintact_biogrid
Supporting Publications1
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.