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Q14168 (MPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAGUK p55 subfamily member 2
Alternative name(s):
Discs large homolog 2
Protein MPP2
Gene names
Name:MPP2
Synonyms:DLG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 2 L27 domains.

Contains 1 PDZ (DHR) domain.

Contains 1 SH3 domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14168-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14168-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-74: Missing.
Isoform 3 (identifier: Q14168-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MPVAATNSET → MAGSPGSGVSLEGISLESSEEAELQRE
     51-74: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576MAGUK p55 subfamily member 2
PRO_0000094573

Regions

Domain8 – 6053L27 1
Domain84 – 14259L27 2
Domain185 – 24056PDZ
Domain249 – 31769SH3
Domain374 – 561188Guanylate kinase-like

Amino acid modifications

Modified residue1411Phosphothreonine Ref.8
Modified residue1451Phosphoserine By similarity

Natural variations

Alternative sequence1 – 1010MPVAATNSET → MAGSPGSGVSLEGISLESSE EAELQRE in isoform 3.
VSP_022951
Alternative sequence51 – 7424Missing in isoform 2 and isoform 3.
VSP_003156

Experimental info

Sequence conflict801E → G in CAI56746. Ref.4
Sequence conflict104 – 1052HV → QL in CAA58067. Ref.1
Sequence conflict104 – 1052HV → QL in BAD97280. Ref.2
Sequence conflict104 – 1052HV → QL in CAB66489. Ref.3
Sequence conflict104 – 1052HV → QL in CAI56746. Ref.4
Sequence conflict104 – 1052HV → QL in AAH30287. Ref.6
Sequence conflict2421S → N in CAA58067. Ref.1

Secondary structure

.............. 576
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 2, 2010. Version 3.
Checksum: A08E858EA646A305

FASTA57664,581
        10         20         30         40         50         60 
MPVAATNSET AMQQVLDNLG SLPSATGAAE LDLIFLRGIM ESPIVRSLAK VIMVLWFMQQ 

        70         80         90        100        110        120 
NVFVPMKYML KYFGAHERLE ETKLEAVRDN NLELVQEILR DLAHVAEQSS TAAELAHILQ 

       130        140        150        160        170        180 
EPHFQSLLET HDSVASKTYE TPPPSPGLDP TFSNQPVPPD AVRMVGIRKT AGEHLGVTFR 

       190        200        210        220        230        240 
VEGGELVIAR ILHGGMVAQQ GLLHVGDIIK EVNGQPVGSD PRALQELLRN ASGSVILKIL 

       250        260        270        280        290        300 
PSYQEPHLPR QVFVKCHFDY DPARDSLIPC KEAGLRFNAG DLLQIVNQDD ANWWQACHVE 

       310        320        330        340        350        360 
GGSAGLIPSQ LLEEKRKAFV KRDLELTPNS GTLCGSLSGK KKKRMMYLTT KNAEFDRHEL 

       370        380        390        400        410        420 
LIYEEVARMP PFRRKTLVLI GAQGVGRRSL KNKLIMWDPD RYGTTVPYTS RRPKDSEREG 

       430        440        450        460        470        480 
QGYSFVSRGE MEADVRAGRY LEHGEYEGNL YGTRIDSIRG VVAAGKVCVL DVNPQAVKVL 

       490        500        510        520        530        540 
RTAEFVPYVV FIEAPDFETL RAMNRAALES GISTKQLTEA DLRRTVEESS RIQRGYGHYF 

       550        560        570 
DLCLVNSNLE RTFRELQTAM EKLRTEPQWV PVSWVY 

« Hide

Isoform 2 [UniParc].

Checksum: 81BBB336B3C9DA89
Show »

FASTA55261,585
Isoform 3 [UniParc].

Checksum: 40FE59BE6B6D998C
Show »

FASTA56963,315

References

« Hide 'large scale' references
[1]"A gene (DLG2) located at 17q12-q21 encodes a new homologue of the Drosophila tumor suppressor dlg-A."
Mazoyer S., Gayther S.A., Nagai M.A., Smith S.A., Dunning A., van Rensburg E.J., Albertsen H., White R., Ponder B.A.J.
Genomics 28:25-31(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Amygdala.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Salivary gland.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Solution structure of the PDZ domain from human maguk p55 subfamily member 2."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 163-240.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82895 mRNA. Translation: CAA58067.1.
AK223560 mRNA. Translation: BAD97280.1.
AL136554 mRNA. Translation: CAB66489.1.
CR936598 mRNA. Translation: CAI56746.1.
AC007993 Genomic DNA. No translation available.
BC030287 mRNA. Translation: AAH30287.1.
PIRA57653.
RefSeqNP_001265299.1. NM_001278370.1.
NP_001265300.1. NM_001278371.1.
NP_001265301.1. NM_001278372.1.
NP_001265302.1. NM_001278373.1.
NP_001265303.1. NM_001278374.1.
NP_001265304.1. NM_001278375.1.
NP_001265305.1. NM_001278376.1.
NP_001265310.1. NM_001278381.1.
NP_005365.4. NM_005374.4.
UniGeneHs.514208.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7KNMR-A163-240[»]
ProteinModelPortalQ14168.
SMRQ14168. Positions 6-244, 252-571.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110495. 7 interactions.
IntActQ14168. 7 interactions.
MINTMINT-4532844.
STRING9606.ENSP00000269095.

PTM databases

PhosphoSiteQ14168.

Polymorphism databases

DMDM290457681.

Proteomic databases

PaxDbQ14168.
PRIDEQ14168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269095; ENSP00000269095; ENSG00000108852. [Q14168-2]
ENST00000377184; ENSP00000366389; ENSG00000108852. [Q14168-3]
ENST00000461854; ENSP00000428286; ENSG00000108852. [Q14168-1]
GeneID4355.
KEGGhsa:4355.
UCSCuc002ien.1. human. [Q14168-3]
uc002ieo.1. human. [Q14168-2]
uc010win.1. human. [Q14168-1]

Organism-specific databases

CTD4355.
GeneCardsGC17M041963.
H-InvDBHIX0013870.
HGNCHGNC:7220. MPP2.
HPAHPA026486.
MIM600723. gene.
neXtProtNX_Q14168.
PharmGKBPA30925.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000233034.
HOVERGENHBG001858.
InParanoidQ14168.
OrthoDBEOG79CXZ5.
PhylomeDBQ14168.
TreeFamTF314263.

Gene expression databases

ArrayExpressQ14168.
BgeeQ14168.
CleanExHS_DLG2.
HS_MPP2.
GenevestigatorQ14168.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR014775. L27_C.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14168.
GeneWikiMPP2.
GenomeRNAi4355.
NextBio17134.
PROQ14168.
SOURCESearch...

Entry information

Entry nameMPP2_HUMAN
AccessionPrimary (citable) accession number: Q14168
Secondary accession number(s): Q53ES9, Q5CZB9, Q9BQJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 2, 2010
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM