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Protein

Charged multivesicular body protein 2a

Gene

CHMP2A

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

Functioni

Probable core 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 HIV-1 p6- and p9-dependent virus release.2 Publications

GO - Molecular functioni

  • phosphatidylcholine binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • cell separation after cytokinesis Source: UniProtKB
  • endosomal transport Source: Reactome
  • establishment of protein localization Source: UniProtKB
  • membrane invagination Source: UniProtKB
  • membrane organization Source: Reactome
  • mitotic metaphase plate congression Source: UniProtKB
  • negative regulation of cell death Source: UniProtKB
  • negative regulation of centriole elongation Source: UniProtKB
  • nucleus organization Source: UniProtKB
  • positive regulation of exosomal secretion Source: UniProtKB
  • positive regulation of viral release from host cell Source: UniProtKB
  • post-Golgi vesicle-mediated transport Source: Reactome
  • protein heterooligomerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein polymerization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • regulation of viral process Source: UniProtKB
  • vacuolar transport Source: InterPro
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome
  • viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_19287. Lysosome Vesicle Biogenesis.
REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 2a
Alternative name(s):
Chromatin-modifying protein 2a
Short name:
CHMP2a
Putative breast adenocarcinoma marker BC-2
Vacuolar protein sorting-associated protein 2-1
Short name:
Vps2-1
Short name:
hVps2-1
Gene namesi
Name:CHMP2A
Synonyms:BC2, CHMP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30216. CHMP2A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • membrane coat Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1702DE → AA: Diminishes interaction with VPS4B. 1 Publication
Mutagenesisi181 – 22242Missing : Membrane association; releases autoinhibition. 1 PublicationAdd
BLAST
Mutagenesisi216 – 2161L → A: Diminishes interaction with VTA1. 1 Publication
Mutagenesisi217 – 2226Missing : Abolishes interaction with VTA1. 1 Publication

Organism-specific databases

PharmGKBiPA142672111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Charged multivesicular body protein 2aPRO_0000211462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei184 – 1841Phosphoserine1 Publication
Modified residuei185 – 1851Phosphothreonine1 Publication
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei203 – 2031Phosphoserine1 Publication

Post-translational modificationi

ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43633.
PaxDbiO43633.
PeptideAtlasiO43633.
PRIDEiO43633.

2D gel databases

OGPiO43633.

PTM databases

PhosphoSiteiO43633.

Expressioni

Gene expression databases

BgeeiO43633.
CleanExiHS_CHMP2A.
ExpressionAtlasiO43633. baseline and differential.
GenevisibleiO43633. HS.

Organism-specific databases

HPAiHPA041153.
HPA042031.

Interactioni

Subunit structurei

Probable core 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. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DOCK8Q8NF50-23EBI-2692789,EBI-10174653

Protein-protein interaction databases

BioGridi118091. 21 interactions.
DIPiDIP-48533N.
IntActiO43633. 7 interactions.
MINTiMINT-5005843.
STRINGi9606.ENSP00000310440.

Structurei

3D structure databases

ProteinModelPortaliO43633.
SMRiO43633. Positions 9-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 222167Interaction with VPS4BAdd
BLAST
Regioni217 – 2226Interaction with VTA1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili12 – 5342Sequence AnalysisAdd
BLAST
Coiled coili195 – 22228Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi210 – 22011MIT-interacting motifAdd
BLAST

Domaini

The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074737.
HOGENOMiHOG000177218.
HOVERGENiHBG107298.
InParanoidiO43633.
KOiK12191.
OMAiKNGQMGA.
PhylomeDBiO43633.
TreeFamiTF300118.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM
60 70 80 90 100
AKQGQMDAVR IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA
110 120 130 140 150
QAMKGVTKAM GTMNRQLKLP QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA
160 170 180 190 200
MGDEEDEEES DAVVSQVLDE LGLSLTDELS NLPSTGGSLS VAAGGKKAEA
210 220
AASALADADA DLEERLKNLR RD
Length:222
Mass (Da):25,104
Last modified:June 1, 1998 - v1
Checksum:iF2B86C623829E32E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042384 mRNA. Translation: AAC00005.1.
AJ277113 Genomic DNA. Translation: CAC14310.1.
AY364248 mRNA. Translation: AAQ76807.1.
BT007298 mRNA. Translation: AAP35962.1.
CR457002 mRNA. Translation: CAG33283.1.
AK311974 mRNA. Translation: BAG34913.1.
CH471135 Genomic DNA. Translation: EAW72609.1.
BC002502 mRNA. Translation: AAH02502.1.
CCDSiCCDS12986.1.
RefSeqiNP_055268.1. NM_014453.3.
NP_940818.1. NM_198426.2.
UniGeneiHs.12107.

Genome annotation databases

EnsembliENST00000312547; ENSP00000310440; ENSG00000130724.
ENST00000600118; ENSP00000469240; ENSG00000130724.
ENST00000601220; ENSP00000472680; ENSG00000130724.
GeneIDi27243.
KEGGihsa:27243.
UCSCiuc002qti.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042384 mRNA. Translation: AAC00005.1.
AJ277113 Genomic DNA. Translation: CAC14310.1.
AY364248 mRNA. Translation: AAQ76807.1.
BT007298 mRNA. Translation: AAP35962.1.
CR457002 mRNA. Translation: CAG33283.1.
AK311974 mRNA. Translation: BAG34913.1.
CH471135 Genomic DNA. Translation: EAW72609.1.
BC002502 mRNA. Translation: AAH02502.1.
CCDSiCCDS12986.1.
RefSeqiNP_055268.1. NM_014453.3.
NP_940818.1. NM_198426.2.
UniGeneiHs.12107.

3D structure databases

ProteinModelPortaliO43633.
SMRiO43633. Positions 9-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118091. 21 interactions.
DIPiDIP-48533N.
IntActiO43633. 7 interactions.
MINTiMINT-5005843.
STRINGi9606.ENSP00000310440.

PTM databases

PhosphoSiteiO43633.

2D gel databases

OGPiO43633.

Proteomic databases

MaxQBiO43633.
PaxDbiO43633.
PeptideAtlasiO43633.
PRIDEiO43633.

Protocols and materials databases

DNASUi27243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312547; ENSP00000310440; ENSG00000130724.
ENST00000600118; ENSP00000469240; ENSG00000130724.
ENST00000601220; ENSP00000472680; ENSG00000130724.
GeneIDi27243.
KEGGihsa:27243.
UCSCiuc002qti.3. human.

Organism-specific databases

CTDi27243.
GeneCardsiGC19M059062.
HGNCiHGNC:30216. CHMP2A.
HPAiHPA041153.
HPA042031.
MIMi610893. gene.
neXtProtiNX_O43633.
PharmGKBiPA142672111.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074737.
HOGENOMiHOG000177218.
HOVERGENiHBG107298.
InParanoidiO43633.
KOiK12191.
OMAiKNGQMGA.
PhylomeDBiO43633.
TreeFamiTF300118.

Enzyme and pathway databases

ReactomeiREACT_19287. Lysosome Vesicle Biogenesis.
REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.

Miscellaneous databases

ChiTaRSiCHMP2A. human.
GeneWikiiCHMP2A.
GenomeRNAii27243.
NextBioi50143.
PROiO43633.
SOURCEiSearch...

Gene expression databases

BgeeiO43633.
CleanExiHS_CHMP2A.
ExpressionAtlasiO43633. baseline and differential.
GenevisibleiO43633. HS.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Slater C., Thill G., Obar R.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Role of the BC-2 gene in breast cancer."
    Koczan D., Reimer T., Rump A., Merck-Rousseau M.F., Rosenthal A., Friese K., Thiesen H.J.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
    Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
    BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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].
    Tissue: Skeletal muscle.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Skin.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1.
    Tissue: Platelet.
  10. "Materials and methods for detection of breast cancer."
    Keesee S.K., Obar R., Wu Y.-J.
    Patent number US5914238, 05-JUN-1996
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-222, PROTEIN SEQUENCE OF 75-89 AND 197-205.
  11. "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: INTERACTION WITH VPS4B.
  12. Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH VPS4A AND VPS4B.
  13. "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: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP1B; CHMP2B; CHMP3; CHMP4A; CHMP4B; CHMP4C; CHMP5 AND VPS4A.
  14. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  15. "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
    Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
    Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MITD1.
  16. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
    Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
    EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain."
    Shim S., Kimpler L.A., Hanson P.I.
    Traffic 8:1068-1079(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH VPS4B, MUTAGENESIS OF 181-ASN--ASP-222.
  18. "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly."
    Shim S., Merrill S.A., Hanson P.I.
    Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VTA1, MUTAGENESIS OF 169-ASP-GLU-170; LEU-216 AND 217-LYS--ASP-222.
  19. Cited for: POLYMERIZATION WITH CHMP3, ELECTRON MICROSCOPY.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
    Kuang Z., Seo E.J., Leis J.
    J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION, INTERACTION WITH VTA1 AND VPS4A.
  22. "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-184; THR-185; SER-188; SER-190 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCHM2A_HUMAN
AccessioniPrimary (citable) accession number: O43633
Secondary accession number(s): B2R4W6, Q3ZTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 1998
Last modified: June 24, 2015
This is version 129 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

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. 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.