Q5T2T1 (MPP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MAGUK p55 subfamily member 7

Gene names

Name:

MPP7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact. Ref.9
Subunit structure	Heterodimer; able to heterodimerize via its C-terminal L27 domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with DLG1 via its N-terminal L27 domain. Interacts with MPP5 and INADL/PATJ. Ref.6 Ref.7 Ref.9
Subcellular location	Membrane; Peripheral membrane protein. Cell junction › tight junction. Cell junction › adherens junction Ref.7 Ref.9.
Induction	Down-regulated in patients suffering of passive Heymann nephritis (at protein level). Ref.8
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.
Sequence caution	The sequence CAI12709.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI13640.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI17344.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell junction Membrane Tight junction
Coding sequence diversity	Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	establishment of cell polarity Traceable author statement Ref.9. Source: BHF-UCL positive regulation of protein complex assembly Inferred from direct assay Ref.7. Source: BHF-UCL protein localization to adherens junction Inferred from mutant phenotype Ref.7. Source: BHF-UCL tight junction assembly Inferred from direct assay Ref.9. Source: BHF-UCL
Cellular_component	MPP7-DLG1-LIN7 complex Inferred from direct assay Ref.7PubMed 20702775. Source: BHF-UCL tight junction Inferred from direct assay Ref.9. Source: BHF-UCL
Molecular_function	protein complex scaffold Inferred from direct assay Ref.7PubMed 20702775. Source: BHF-UCL protein heterodimerization activity Inferred from direct assay Ref.7. Source: BHF-UCL signaling adaptor activity Non-traceable author statement Ref.5. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 576

576

MAGUK p55 subfamily member 7

PRO_0000320027

Regions

Domain

10 – 65

56

L27 1

Domain

67 – 122

56

L27 2

Domain

139 – 220

82

PDZ

Domain

228 – 298

71

SH3

Domain

368 – 560

193

Guanylate kinase-like

Amino acid modifications

Modified residue

409

1

Phosphoserine Ref.10 Ref.11

Natural variations

Natural variant

322

1

K → R. Ref.1 Ref.3 Ref.4
Corresponds to variant rs2997211 [ dbSNP | Ensembl ].

VAR_039110

Experimental info

Mutagenesis

38

1

L → S: Abolishes interaction with DLG1. Ref.9

Mutagenesis

95

1

L → S: Does not affect the interaction with DLG1. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

576

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Helix

14 – 19

6

Helix

21 – 25

5

Turn

26 – 28

3

Helix

34 – 41

8

Helix

47 – 61

15

Helix

72 – 84

13

Helix

90 – 98

9

Helix

102 – 115

14

Beta strand

138 – 147

10

Beta strand

151 – 155

5

Turn

157 – 159

3

Beta strand

162 – 167

6

Helix

172 – 176

5

Beta strand

184 – 188

5

Beta strand

191 – 193

3

Helix

198 – 207

10

Beta strand

210 – 217

8

Sequences

	Sequence		Length	Mass (Da)
	Q5T2T1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 86366E460A08C6A7	FASTA	576	65,524
	10 20 30 40 50 60 MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY 70 80 90 100 110 120 EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD 130 140 150 160 170 180 PVLPPMPEDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIIVARIMRG GAADRSGLIH 190 200 210 220 230 240 VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN 250 260 270 280 290 300 PNEDKAIPCK EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL 310 320 330 340 350 360 RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY 370 380 390 400 410 420 RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI 430 440 450 460 470 480 SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK 490 500 510 520 530 540 PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD 550 560 570 KIIINDDLTV AFNELKTTFD KLETETHWVP VSWLHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-322. Tissue: Hippocampus.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-322.
[4]	"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], VARIANT ARG-322. Tissue: Testis.
[5]	"Identification and characterization of human MPP7 gene and mouse Mpp7 gene in silico." Katoh M., Katoh M. Int. J. Mol. Med. 13:333-338(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[6]	"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells." Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T. Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INADL AND MPP5.
[7]	"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions." Bohl J., Brimer N., Lyons C., Vande Pol S.B. J. Biol. Chem. 282:9392-9400(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH DLG1; LIN7A; LIN7B AND LIN7C.
[8]	"Markedly increased urinary preprohaptoglobin and haptoglobin in passive Heymann nephritis: a differential proteomics approach." Ngai H.-H., Sit W.-H., Jiang P.-P., Thongboonkerd V., Wan J.-M. J. Proteome Res. 6:3313-3320(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
[9]	"The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation." Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A. Mol. Biol. Cell 18:1744-1755(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DLG1 AND MPP5, MUTAGENESIS OF LEU-38 AND LEU-95.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK315046 mRNA. Translation: BAG37526.1.
AL390866, AL355501, AL391423 Genomic DNA. Translation: CAI12708.1.
AL390866, AL355501, AL391423 Genomic DNA. Translation: CAI12709.1. Sequence problems.
AL355501, AL390866, AL391423 Genomic DNA. Translation: CAI13640.1. Sequence problems.
AL355501, AL390866, AL391423 Genomic DNA. Translation: CAI13641.1.
AL391423, AL355501, AL390866 Genomic DNA. Translation: CAI17344.1. Sequence problems.
AL391423, AL355501, AL390866 Genomic DNA. Translation: CAI17345.1.
CH471072 Genomic DNA. Translation: EAW86045.1.
CH471072 Genomic DNA. Translation: EAW86047.1.
BC038105 mRNA. Translation: AAH38105.1.

IPI

IPI00217617.

RefSeq

NP_775767.2. NM_173496.3.

UniGene

Hs.499159.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LRA	X-ray	2.95	A	9-120	[»]
3O46	X-ray	1.30	A	135-225	[»]

ProteinModelPortal

Q5T2T1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q5T2T1. 1 interaction.

STRING

9606.ENSP00000337907.

PTM databases

PhosphoSite

Q5T2T1.

Polymorphism databases

DMDM

74762233.

Proteomic databases

PaxDb

Q5T2T1.

PRIDE

Q5T2T1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337532; ENSP00000337907; ENSG00000150054.
ENST00000375719; ENSP00000364871; ENSG00000150054.
ENST00000375732; ENSP00000364884; ENSG00000150054.
ENST00000441595; ENSP00000398319; ENSG00000150054.
ENST00000540098; ENSP00000438693; ENSG00000150054.

GeneID

143098.

KEGG

hsa:143098.

UCSC

uc001iua.1. human.

Organism-specific databases

CTD

143098.

GeneCards

GC10M028382.

H-InvDB

HIX0008732.

HGNC

HGNC:26542. MPP7.

HPA

HPA037598.

MIM

610973. gene.

neXtProt

NX_Q5T2T1.

PharmGKB

PA134985345.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0194.

HOGENOM

HOG000233034.

HOVERGEN

HBG001858.

InParanoid

Q5T2T1.

OMA

QGAAKPF.

OrthoDB

EOG42NJ07.

PhylomeDB

Q5T2T1.

Gene expression databases

ArrayExpress

Q5T2T1.

Bgee

Q5T2T1.

CleanEx

HS_MPP7.

Genevestigator

Q5T2T1.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR014775. L27_C.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00856. 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]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5T2T1.

GenomeRNAi

143098.

NextBio

84649.

SOURCE

Search...

Entry information

Entry name

MPP7_HUMAN

Accession

Primary (citable) accession number: Q5T2T1
Secondary accession number(s): B2RCC9 , B5MDZ3, D3DRW3, Q5T2T0, Q8IY28

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.