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Protein

Charged multivesicular body protein 1a

Gene

CHMP1A

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

Functioni

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing.4 Publications

GO - Molecular functioni

  • metallopeptidase activity Source: ProtInc
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: ProtInc

GO - Biological processi

  • cell division Source: UniProtKB
  • cell separation after cytokinesis Source: UniProtKB
  • gene silencing Source: UniProtKB
  • mitotic chromosome condensation Source: UniProtKB
  • mitotic metaphase plate congression Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by glucose Source: UniProtKB
  • nucleus organization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • proteolysis Source: GOC
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • vacuolar transport Source: InterPro
  • vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Cell cycle, Cell division, Protein transport, Transcription, Transcription regulation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 1a
Alternative name(s):
Chromatin-modifying protein 1a
Short name:
CHMP1a
Vacuolar protein sorting-associated protein 46-1
Short name:
Vps46-1
Short name:
hVps46-1
Gene namesi
Name:CHMP1A
Synonyms:CHMP11 Publication, KIAA00471 Publication, PCOLN3, PRSM11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:8740. CHMP1A.

Subcellular locationi

  • Cytoplasm
  • Endosome membrane; Peripheral membrane protein
  • Nucleus matrix

  • Note: The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On overexpression, it localizes to nuclear bodies characterized by nuclease-resistant condensed chromatin.

GO - Cellular componenti

  • condensed nuclear chromosome Source: UniProtKB
  • early endosome Source: UniProtKB
  • endomembrane system Source: UniProtKB
  • ESCRT III complex Source: InterPro
  • extracellular exosome Source: UniProtKB
  • microtubule organizing center Source: UniProtKB
  • nuclear matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pontocerebellar hypoplasia 8 (PCH8)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive neurodevelopmental disorder characterized by severe psychomotor retardation, abnormal movements, hypotonia, spasticity, and variable visual defects. Brain MRI shows pontocerebellar hypoplasia, decreased cerebral white matter, and a thin corpus callosum.

See also OMIM:614961

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911L → A: No effect on interaction with IST1; when associated with L-194. 1 Publication
Mutagenesisi194 – 1941L → A: No effect on interaction with IST1; when associated with L-194. 1 Publication

Organism-specific databases

MIMi614961. phenotype.
Orphaneti324569. Pontocerebellar hypoplasia type 8.
PharmGKBiPA33085.

Polymorphism and mutation databases

DMDMi62510514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Charged multivesicular body protein 1aPRO_0000211448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei173 – 1731Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HD42.
PaxDbiQ9HD42.
PRIDEiQ9HD42.

PTM databases

PhosphoSiteiQ9HD42.

Expressioni

Tissue specificityi

Expressed in placenta, cultured skin fibroblasts and in osteoblast cell line MG-63.1 Publication

Inductioni

By muristerone.1 Publication

Gene expression databases

BgeeiQ9HD42.
CleanExiHS_CHMP1A.
ExpressionAtlasiQ9HD42. baseline and differential.
GenevestigatoriQ9HD42.

Interactioni

Subunit structurei

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Self-associates. Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B. Interacts with PHF1. Interacts with IST1. Interacts with MITD1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAMBPO956303EBI-1057156,EBI-396676
USP8P408183EBI-1057156,EBI-1050865

Protein-protein interaction databases

BioGridi111148. 22 interactions.
DIPiDIP-50647N.
IntActiQ9HD42. 5 interactions.
MINTiMINT-6946738.
STRINGi9606.ENSP00000253475.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 19512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQ9NMR-B180-196[»]
2YMBX-ray3.40F/H184-196[»]
4A5XX-ray1.91C/D184-196[»]
ProteinModelPortaliQ9HD42.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HD42.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili5 – 4743Sequence AnalysisAdd
BLAST
Coiled coili102 – 12423Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 19511MIT-interacting motifAdd
BLAST

Sequence similaritiesi

Belongs to the SNF7 family.Sequence Analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG331649.
GeneTreeiENSGT00550000074957.
HOGENOMiHOG000241980.
HOVERGENiHBG080200.
InParanoidiQ9HD42.
OrthoDBiEOG7BP843.
PhylomeDBiQ9HD42.
TreeFamiTF300076.

Family and domain databases

InterProiIPR029888. CHMP1A.
IPR005024. Snf7_fam.
[Graphical view]
PANTHERiPTHR10476:SF7. PTHR10476:SF7. 1 hit.
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 11 Publication (identifier: Q9HD42-1) [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
MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE
60 70 80 90 100
NAIRKKNEGV NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL
110 120 130 140 150
STMDLQKVSS VMDRFEQQVQ NLDVHTSVME DSMSSATTLT TPQEQVDSLI
160 170 180 190
MQIAEENGLE VLDQLSQLPE GASAVGESSV RSQEDQLSRR LAALRN
Length:196
Mass (Da):21,703
Last modified:March 1, 2001 - v1
Checksum:i85D0ED7D10828D60
GO
Isoform 2Curated (identifier: Q9HD42-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:68
Mass (Da):7,363
Checksum:iF58834B1C0E254DB
GO

Sequence cautioni

The sequence AAC50775.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence BAA07557.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771Q → D in AAC50775 (PubMed:8863740).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128Missing in isoform 2. 1 PublicationVSP_051716Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58048 mRNA. Translation: AAC50775.1. Sequence problems.
AF281063 mRNA. Translation: AAG01448.1.
D38554 mRNA. Translation: BAA07557.1. Sequence problems.
BT006841 mRNA. Translation: AAP35487.1.
AC010538 Genomic DNA. No translation available.
BC007527 mRNA. No translation available.
BC010000 mRNA. Translation: AAH10000.2.
BC132711 mRNA. Translation: AAI32712.1.
BC132713 mRNA. Translation: AAI32714.1.
CCDSiCCDS45552.1. [Q9HD42-1]
PIRiJC4963.
RefSeqiNP_002759.2. NM_002768.4. [Q9HD42-1]
UniGeneiHs.589427.

Genome annotation databases

EnsembliENST00000397901; ENSP00000380998; ENSG00000131165. [Q9HD42-1]
GeneIDi5119.
KEGGihsa:5119.
UCSCiuc002fnu.4. human. [Q9HD42-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58048 mRNA. Translation: AAC50775.1. Sequence problems.
AF281063 mRNA. Translation: AAG01448.1.
D38554 mRNA. Translation: BAA07557.1. Sequence problems.
BT006841 mRNA. Translation: AAP35487.1.
AC010538 Genomic DNA. No translation available.
BC007527 mRNA. No translation available.
BC010000 mRNA. Translation: AAH10000.2.
BC132711 mRNA. Translation: AAI32712.1.
BC132713 mRNA. Translation: AAI32714.1.
CCDSiCCDS45552.1. [Q9HD42-1]
PIRiJC4963.
RefSeqiNP_002759.2. NM_002768.4. [Q9HD42-1]
UniGeneiHs.589427.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQ9NMR-B180-196[»]
2YMBX-ray3.40F/H184-196[»]
4A5XX-ray1.91C/D184-196[»]
ProteinModelPortaliQ9HD42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111148. 22 interactions.
DIPiDIP-50647N.
IntActiQ9HD42. 5 interactions.
MINTiMINT-6946738.
STRINGi9606.ENSP00000253475.

PTM databases

PhosphoSiteiQ9HD42.

Polymorphism and mutation databases

DMDMi62510514.

Proteomic databases

MaxQBiQ9HD42.
PaxDbiQ9HD42.
PRIDEiQ9HD42.

Protocols and materials databases

DNASUi5119.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397901; ENSP00000380998; ENSG00000131165. [Q9HD42-1]
GeneIDi5119.
KEGGihsa:5119.
UCSCiuc002fnu.4. human. [Q9HD42-1]

Organism-specific databases

CTDi5119.
GeneCardsiGC16M089710.
H-InvDBHIX0013363.
HGNCiHGNC:8740. CHMP1A.
MIMi164010. gene.
614961. phenotype.
neXtProtiNX_Q9HD42.
Orphaneti324569. Pontocerebellar hypoplasia type 8.
PharmGKBiPA33085.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG331649.
GeneTreeiENSGT00550000074957.
HOGENOMiHOG000241980.
HOVERGENiHBG080200.
InParanoidiQ9HD42.
OrthoDBiEOG7BP843.
PhylomeDBiQ9HD42.
TreeFamiTF300076.

Miscellaneous databases

ChiTaRSiCHMP1A. human.
EvolutionaryTraceiQ9HD42.
GeneWikiiCHMP1A.
GenomeRNAii5119.
NextBioi19738.
PROiQ9HD42.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HD42.
CleanExiHS_CHMP1A.
ExpressionAtlasiQ9HD42. baseline and differential.
GenevestigatoriQ9HD42.

Family and domain databases

InterProiIPR029888. CHMP1A.
IPR005024. Snf7_fam.
[Graphical view]
PANTHERiPTHR10476:SF7. PTHR10476:SF7. 1 hit.
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)."
    Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R., Callen D.F., Prockop D.J., Peltonen L., Kadler K.E.
    Gene 174:135-143(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, TISSUE SPECIFICITY.
    Tissue: Fibroblast and Placenta.
  2. "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
    Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
    J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    Tissue: Placenta1 Publication.
  3. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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] (ISOFORMS 1 AND 2).
    Tissue: BrainImported and Kidney1 Publication.
  7. "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
    Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
    J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A.
  8. Cited for: INTERACTION WITH CHMP1B; VPS4A AND VPS4B.
  9. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH CHMP1B AND VPS4A.
  10. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: INTERACTION WITH IST1.
  13. "Biochemical analyses of human IST1 and its function in cytokinesis."
    Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
    Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IST1, MUTAGENESIS OF LEU-191 AND LEU-194.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INVOLVEMENT IN PCH8.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: STRUCTURE BY NMR OF 180-196 IN COMPLEX WITH VPS4A.
  18. "ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes."
    Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M., Lamers M.H., Williams R.L., Martin-Serrano J.
    Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 184-196 IN COMPLEX WITH MITD1, FUNCTION, INTERACTION WITH MITD1.

Entry informationi

Entry nameiCHM1A_HUMAN
AccessioniPrimary (citable) accession number: Q9HD42
Secondary accession number(s): A2RU09
, Q14468, Q15779, Q96G31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2001
Last modified: May 27, 2015
This is version 118 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

Caution

Was originally (PubMed:8863740) thought to be a metalloprotease (PRSM1). This was based on a wrong translation of the ORF which gave rise to a putative protein of 318 AA containing a pattern reminiscent of zinc metalloproteases.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.