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Protein

MPN domain-containing protein

Gene

MPND

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable protease.By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Names & Taxonomyi

Protein namesi
Recommended name:
MPN domain-containing protein (EC:3.4.-.-)
Gene namesi
Name:MPND
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:25934. MPND.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162396091.

Polymorphism and mutation databases

BioMutaiMPND.
DMDMi74728961.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 471470MPN domain-containing proteinPRO_0000278804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei178 – 1781PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8N594.
MaxQBiQ8N594.
PaxDbiQ8N594.
PeptideAtlasiQ8N594.
PRIDEiQ8N594.

PTM databases

iPTMnetiQ8N594.
PhosphoSiteiQ8N594.

Expressioni

Gene expression databases

BgeeiQ8N594.
CleanExiHS_MPND.
ExpressionAtlasiQ8N594. baseline and differential.
GenevisibleiQ8N594. HS.

Organism-specific databases

HPAiHPA043274.
HPA045475.

Interactioni

Protein-protein interaction databases

BioGridi124386. 2 interactions.
IntActiQ8N594. 1 interaction.
STRINGi9606.ENSP00000262966.

Structurei

3D structure databases

ProteinModelPortaliQ8N594.
SMRiQ8N594. Positions 280-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 375109MPNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi349 – 36214JAMM motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 6833Gly-richAdd
BLAST
Compositional biasi182 – 1876Poly-Glu
Compositional biasi191 – 1955Poly-Glu

Domaini

The JAMM motif may mediate the protease activity.By similarity

Sequence similaritiesi

Belongs to the peptidase M67 family.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiKOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063766.
HOGENOMiHOG000293280.
HOVERGENiHBG081983.
InParanoidiQ8N594.
OrthoDBiEOG783MTW.
PhylomeDBiQ8N594.
TreeFamiTF324811.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N594-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAPEPLSPA GGAGEEAPEE DEDEAEAEDP ERPNAGAGGG RSGGGGSSVS
60 70 80 90 100
GGGGGGGAGA GGCGGPGGAL TRRAVTLRVL LKDALLEPGA GVLSIYYLGK
110 120 130 140 150
KFLGDLQPDG RIMWQETGQT FNSPSAWATH CKKLVNPAKK SGCGWASVKY
160 170 180 190 200
KGQKLDKYKA TWLRLHQLHT PATAADESPA SEGEEEELLM EEEEEDVLAG
210 220 230 240 250
VSAEDKSRRP LGKSPSEPAH PEATTPGKRV DSKIRVPVRY CMLGSRDLAR
260 270 280 290 300
NPHTLVEVTS FAAINKFQPF NVAVSSNVLF LLDFHSHLTR SEVVGYLGGR
310 320 330 340 350
WDVNSQMLTV LRAFPCRSRL GDAETAAAIE EEIYQSLFLR GLSLVGWYHS
360 370 380 390 400
HPHSPALPSL QDIDAQMDYQ LRLQGSSNGF QPCLALLCSP YYSGNPGPES
410 420 430 440 450
KISPFWVMPP PEMLLVEFYK GSPDLVRLQE PWSQEHTYLD KLKISLASRT
460 470
PKDQSLCHVL EQVCGVLKQG S
Length:471
Mass (Da):50,662
Last modified:October 1, 2002 - v1
Checksum:i9D05932C816F828D
GO
Isoform 2 (identifier: Q8N594-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-332: Missing.
     412-412: E → EQRPSDYGIPMDVEMAYVQDSFLTNDILHEM

Show »
Length:451
Mass (Da):48,586
Checksum:i54770893A56F7A9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931E → K in BAB55432 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei283 – 33250Missing in isoform 2. 1 PublicationVSP_023400Add
BLAST
Alternative sequencei412 – 4121E → EQRPSDYGIPMDVEMAYVQD SFLTNDILHEM in isoform 2. 1 PublicationVSP_023401

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027887 mRNA. Translation: BAB55432.1.
AC007292 Genomic DNA. Translation: AAD24592.1.
AC007292 Genomic DNA. Translation: AAD24593.1.
AC104521 Genomic DNA. No translation available.
BC032652 mRNA. Translation: AAH32652.1.
CCDSiCCDS42470.1. [Q8N594-1]
CCDS54200.1. [Q8N594-2]
RefSeqiNP_001153318.1. NM_001159846.2. [Q8N594-2]
NP_116257.2. NM_032868.5. [Q8N594-1]
UniGeneiHs.321689.

Genome annotation databases

EnsembliENST00000262966; ENSP00000262966; ENSG00000008382. [Q8N594-1]
ENST00000359935; ENSP00000353015; ENSG00000008382. [Q8N594-2]
GeneIDi84954.
KEGGihsa:84954.
UCSCiuc002mae.3. human. [Q8N594-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027887 mRNA. Translation: BAB55432.1.
AC007292 Genomic DNA. Translation: AAD24592.1.
AC007292 Genomic DNA. Translation: AAD24593.1.
AC104521 Genomic DNA. No translation available.
BC032652 mRNA. Translation: AAH32652.1.
CCDSiCCDS42470.1. [Q8N594-1]
CCDS54200.1. [Q8N594-2]
RefSeqiNP_001153318.1. NM_001159846.2. [Q8N594-2]
NP_116257.2. NM_032868.5. [Q8N594-1]
UniGeneiHs.321689.

3D structure databases

ProteinModelPortaliQ8N594.
SMRiQ8N594. Positions 280-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124386. 2 interactions.
IntActiQ8N594. 1 interaction.
STRINGi9606.ENSP00000262966.

PTM databases

iPTMnetiQ8N594.
PhosphoSiteiQ8N594.

Polymorphism and mutation databases

BioMutaiMPND.
DMDMi74728961.

Proteomic databases

EPDiQ8N594.
MaxQBiQ8N594.
PaxDbiQ8N594.
PeptideAtlasiQ8N594.
PRIDEiQ8N594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262966; ENSP00000262966; ENSG00000008382. [Q8N594-1]
ENST00000359935; ENSP00000353015; ENSG00000008382. [Q8N594-2]
GeneIDi84954.
KEGGihsa:84954.
UCSCiuc002mae.3. human. [Q8N594-1]

Organism-specific databases

CTDi84954.
GeneCardsiMPND.
HGNCiHGNC:25934. MPND.
HPAiHPA043274.
HPA045475.
neXtProtiNX_Q8N594.
PharmGKBiPA162396091.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063766.
HOGENOMiHOG000293280.
HOVERGENiHBG081983.
InParanoidiQ8N594.
OrthoDBiEOG783MTW.
PhylomeDBiQ8N594.
TreeFamiTF324811.

Miscellaneous databases

ChiTaRSiMPND. human.
GenomeRNAii84954.
PROiQ8N594.

Gene expression databases

BgeeiQ8N594.
CleanExiHS_MPND.
ExpressionAtlasiQ8N594. baseline and differential.
GenevisibleiQ8N594. HS.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] (ISOFORM 2).
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 1).
    Tissue: Eye.
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMPND_HUMAN
AccessioniPrimary (citable) accession number: Q8N594
Secondary accession number(s): Q96SJ0, Q9Y2P1, Q9Y2P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.