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Q5T2T1

- MPP7_HUMAN

UniProt

Q5T2T1 - MPP7_HUMAN

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Protein

MAGUK p55 subfamily member 7

Gene
MPP7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. protein binding Source: BHF-UCL
  2. protein complex scaffold Source: BHF-UCL
  3. protein domain specific binding Source: BHF-UCL
  4. protein heterodimerization activity Source: BHF-UCL
  5. signaling adaptor activity Source: BHF-UCL

GO - Biological processi

  1. establishment of cell polarity Source: BHF-UCL
  2. positive regulation of protein complex assembly Source: BHF-UCL
  3. positive regulation of signal transduction Source: GOC
  4. protein localization to adherens junction Source: BHF-UCL
  5. tight junction assembly Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
MAGUK p55 subfamily member 7
Gene namesi
Name:MPP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:26542. MPP7.

Subcellular locationi

Membrane; Peripheral membrane protein. Cell junctiontight junction. Cell junctionadherens junction 2 Publications

GO - Cellular componenti

  1. adherens junction Source: BHF-UCL
  2. cell junction Source: HPA
  3. mitochondrion Source: HPA
  4. MPP7-DLG1-LIN7 complex Source: BHF-UCL
  5. tight junction Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381L → S: Abolishes interaction with DLG1. 1 Publication
Mutagenesisi95 – 951L → S: Does not affect the interaction with DLG1. 1 Publication

Organism-specific databases

PharmGKBiPA134985345.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576MAGUK p55 subfamily member 7PRO_0000320027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei409 – 4091Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5T2T1.
PaxDbiQ5T2T1.
PRIDEiQ5T2T1.

PTM databases

PhosphoSiteiQ5T2T1.

Expressioni

Inductioni

Down-regulated in patients suffering of passive Heymann nephritis (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ5T2T1.
BgeeiQ5T2T1.
CleanExiHS_MPP7.
GenevestigatoriQ5T2T1.

Organism-specific databases

HPAiHPA037598.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi126785. 4 interactions.
IntActiQ5T2T1. 2 interactions.
STRINGi9606.ENSP00000337907.

Structurei

Secondary structure

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134
Helixi14 – 196
Helixi21 – 255
Turni26 – 283
Helixi34 – 418
Helixi47 – 6115
Helixi72 – 8413
Helixi90 – 989
Helixi102 – 11514
Beta strandi138 – 14710
Beta strandi151 – 1555
Turni157 – 1593
Beta strandi162 – 1676
Helixi172 – 1765
Beta strandi184 – 1885
Beta strandi191 – 1933
Helixi198 – 20710
Beta strandi210 – 2178

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRAX-ray2.95A7-120[»]
3O46X-ray1.30A135-225[»]
ProteinModelPortaliQ5T2T1.
SMRiQ5T2T1. Positions 1-219, 232-570.

Miscellaneous databases

EvolutionaryTraceiQ5T2T1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 6556L27 1Add
BLAST
Domaini67 – 12256L27 2Add
BLAST
Domaini139 – 22082PDZAdd
BLAST
Domaini228 – 29871SH3Add
BLAST
Domaini368 – 560193Guanylate kinase-likeAdd
BLAST

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 2 L27 domains.
Contains 1 PDZ (DHR) domain.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiQ5T2T1.
OMAiSRDDQGA.
OrthoDBiEOG79CXZ5.
PhylomeDBiQ5T2T1.
TreeFamiTF314263.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. 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]
PfamiPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. 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]

Sequencei

Sequence statusi: Complete.

Q5T2T1-1 [UniParc]FASTAAdd to Basket

« Hide

MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL    50
VKIHEKLHYY EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS 100
KPNVKALLSV HDTVAQKNYD PVLPPMPEDI DDEEDSVKII RLVKNREPLG 150
ATIKKDEQTG AIIVARIMRG GAADRSGLIH VGDELREVNG IPVEDKRPEE 200
IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN PNEDKAIPCK 250
EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL 300
RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD 350
VPTYEEVTPY RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV 400
PHTTRARRSQ ESDGVEYIFI SKHLFETDVQ NNKFIEYGEY KNNYYGTSID 450
SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK PYVIFIKPPS IERLRETRKN 500
AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD KIIINDDLTV 550
AFNELKTTFD KLETETHWVP VSWLHS 576
Length:576
Mass (Da):65,524
Last modified:December 21, 2004 - v1
Checksum:i86366E460A08C6A7
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221K → R.3 Publications
Corresponds to variant rs2997211 [ dbSNP | Ensembl ].
VAR_039110

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7158.1.
RefSeqiNP_775767.2. NM_173496.3.
XP_005252424.1. XM_005252367.1.
UniGeneiHs.499159.

Genome annotation databases

EnsembliENST00000337532; ENSP00000337907; ENSG00000150054.
ENST00000375719; ENSP00000364871; ENSG00000150054.
ENST00000375732; ENSP00000364884; ENSG00000150054.
ENST00000540098; ENSP00000438693; ENSG00000150054.
GeneIDi143098.
KEGGihsa:143098.
UCSCiuc001iua.1. human.

Polymorphism databases

DMDMi74762233.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS7158.1.
RefSeqi NP_775767.2. NM_173496.3.
XP_005252424.1. XM_005252367.1.
UniGenei Hs.499159.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LRA X-ray 2.95 A 7-120 [» ]
3O46 X-ray 1.30 A 135-225 [» ]
ProteinModelPortali Q5T2T1.
SMRi Q5T2T1. Positions 1-219, 232-570.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126785. 4 interactions.
IntActi Q5T2T1. 2 interactions.
STRINGi 9606.ENSP00000337907.

PTM databases

PhosphoSitei Q5T2T1.

Polymorphism databases

DMDMi 74762233.

Proteomic databases

MaxQBi Q5T2T1.
PaxDbi Q5T2T1.
PRIDEi Q5T2T1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337532 ; ENSP00000337907 ; ENSG00000150054 .
ENST00000375719 ; ENSP00000364871 ; ENSG00000150054 .
ENST00000375732 ; ENSP00000364884 ; ENSG00000150054 .
ENST00000540098 ; ENSP00000438693 ; ENSG00000150054 .
GeneIDi 143098.
KEGGi hsa:143098.
UCSCi uc001iua.1. human.

Organism-specific databases

CTDi 143098.
GeneCardsi GC10M028382.
H-InvDB HIX0008732.
HGNCi HGNC:26542. MPP7.
HPAi HPA037598.
MIMi 610973. gene.
neXtProti NX_Q5T2T1.
PharmGKBi PA134985345.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0194.
HOGENOMi HOG000233034.
HOVERGENi HBG001858.
InParanoidi Q5T2T1.
OMAi SRDDQGA.
OrthoDBi EOG79CXZ5.
PhylomeDBi Q5T2T1.
TreeFami TF314263.

Miscellaneous databases

EvolutionaryTracei Q5T2T1.
GenomeRNAii 143098.
NextBioi 84649.
PROi Q5T2T1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5T2T1.
Bgeei Q5T2T1.
CleanExi HS_MPP7.
Genevestigatori Q5T2T1.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR008145. 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 ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiMPP7_HUMAN
AccessioniPrimary (citable) accession number: Q5T2T1
Secondary accession number(s): B2RCC9
, B5MDZ3, D3DRW3, Q5T2T0, Q8IY28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi