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Q9UQN3

- CHM2B_HUMAN

UniProt

Q9UQN3 - CHM2B_HUMAN

Protein

Charged multivesicular body protein 2b

Gene

CHMP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. protein binding Source: UniProt
    2. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. endosomal transport Source: Reactome
    3. membrane organization Source: Reactome
    4. protein transport Source: UniProtKB-KW
    5. viral life cycle Source: Reactome
    6. viral process Source: Reactome

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_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 2b
    Alternative name(s):
    CHMP2.5
    Chromatin-modifying protein 2b
    Short name:
    CHMP2b
    Vacuolar protein sorting-associated protein 2-2
    Short name:
    Vps2-2
    Short name:
    hVps2-2
    Gene namesi
    Name:CHMP2B
    ORF Names:CGI-84
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:24537. CHMP2B.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Late endosome membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular Source: LIFEdb
    5. late endosome membrane Source: UniProtKB-SubCell
    6. mitochondrion Source: HPA
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Frontotemporal dementia, chromosome 3-linked (FTD3) [MIM:600795]: Characterized by an onset of dementia in the late 50's initially characterized by behavioral and personality changes including apathy, restlessness, disinhibition and hyperorality, progressing to stereotyped behaviors, non-fluent aphasia, mutism and dystonia, with a marked lack of insight. The brains of individuals with FTD3 have no distinctive neuropathological features. They show global cortical and central atrophy, but no beta-amyloid deposits.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti148 – 1481D → Y in FTD3. 1 Publication
    VAR_023383
    Amyotrophic lateral sclerosis 17 (ALS17) [MIM:614696]: An adult-onset progressive neurodegenerative disorder with predominantly lower motor neuron involvement, manifest as muscle weakness and wasting of the upper and lower limbs, bulbar signs, and respiratory insufficiency.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291I → V in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway. 2 Publications
    VAR_038373
    Natural varianti104 – 1041T → N in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 1 Publication
    VAR_068689
    Natural varianti206 – 2061Q → H in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 2 Publications
    VAR_038374

    Keywords - Diseasei

    Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi600795. phenotype.
    614696. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    275864. Behavioral variant of frontotemporal dementia.
    100070. Progressive non-fluent aphasia.
    100069. Semantic dementia.
    PharmGKBiPA142672112.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 213212Charged multivesicular body protein 2bPRO_0000211469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei199 – 1991Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UQN3.
    PaxDbiQ9UQN3.
    PRIDEiQ9UQN3.

    PTM databases

    PhosphoSiteiQ9UQN3.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in brain, heart, skeletal muscle, spleen, kidney, liver, small intestine, pancreas, lung, placenta and leukocytes. In brain, it is expressed in cerebellum, cerebral cortex, medulla, spinal chord, occipital lobe, frontal lobe, temporal lobe and putamen.1 Publication

    Gene expression databases

    ArrayExpressiQ9UQN3.
    BgeeiQ9UQN3.
    CleanExiHS_CHMP2B.
    GenevestigatoriQ9UQN3.

    Organism-specific databases

    HPAiHPA035069.
    HPA052754.

    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. Interacts with CHMP2A. Interacts with VPS4A. Interacts with VPS4B; the interaction is direct.2 Publications

    Protein-protein interaction databases

    BioGridi117462. 15 interactions.
    DIPiDIP-50766N.
    IntActiQ9UQN3. 6 interactions.
    MINTiMINT-1430090.
    STRINGi9606.ENSP00000263780.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi201 – 21010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JQKNMR-B195-213[»]
    ProteinModelPortaliQ9UQN3.
    SMRiQ9UQN3. Positions 7-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UQN3.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili25 – 5531Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21111MIT-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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SNF7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG268821.
    HOGENOMiHOG000177218.
    HOVERGENiHBG102628.
    InParanoidiQ9UQN3.
    KOiK12192.
    OMAiKTMQDFQ.
    OrthoDBiEOG79GT8Q.
    PhylomeDBiQ9UQN3.
    TreeFamiTF314163.

    Family and domain databases

    InterProiIPR005024. Snf7.
    [Graphical view]
    PfamiPF03357. Snf7. 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. Align

    Isoform 1 (identifier: Q9UQN3-1) [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

    MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA    50
    KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG 100
    AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF 150
    DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD 200
    EEIERQLKAL GVD 213
    Length:213
    Mass (Da):23,907
    Last modified:May 1, 2000 - v1
    Checksum:iBA192A0EAC45C19B
    GO
    Isoform 2 (identifier: Q9UQN3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQL → M

    Show »
    Length:172
    Mass (Da):19,100
    Checksum:i4F61A1400473D9F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81K → R in CAB45721. (PubMed:11230166)Curated
    Sequence conflicti8 – 81K → R in CAG38487. (PubMed:14702039)Curated
    Sequence conflicti113 – 1131N → S in BAD96374. 1 PublicationCurated
    Sequence conflicti201 – 2011E → V in CAB45721. (PubMed:11230166)Curated
    Sequence conflicti201 – 2011E → V in CAG38487. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291I → V in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway. 2 Publications
    VAR_038373
    Natural varianti104 – 1041T → N in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 1 Publication
    VAR_068689
    Natural varianti148 – 1481D → Y in FTD3. 1 Publication
    VAR_023383
    Natural varianti206 – 2061Q → H in ALS17; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway. 2 Publications
    VAR_038374

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242MASLF…QEKQL → M in isoform 2. CuratedVSP_045142Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151842 mRNA. Translation: AAD34079.1.
    AL080122 mRNA. Translation: CAB45721.1.
    AK296072 mRNA. Translation: BAG58830.1.
    CR533456 mRNA. Translation: CAG38487.1.
    AK222654 mRNA. Translation: BAD96374.1.
    AC123511 Genomic DNA. No translation available.
    AC130885 Genomic DNA. No translation available.
    BC001553 mRNA. Translation: AAH01553.1.
    CCDSiCCDS2918.1. [Q9UQN3-1]
    CCDS58840.1. [Q9UQN3-2]
    PIRiT12468.
    RefSeqiNP_001231573.1. NM_001244644.1. [Q9UQN3-2]
    NP_054762.2. NM_014043.3. [Q9UQN3-1]
    UniGeneiHs.476930.

    Genome annotation databases

    EnsembliENST00000263780; ENSP00000263780; ENSG00000083937. [Q9UQN3-1]
    ENST00000471660; ENSP00000419998; ENSG00000083937. [Q9UQN3-2]
    GeneIDi25978.
    KEGGihsa:25978.
    UCSCiuc003dqp.4. human. [Q9UQN3-1]
    uc011bgn.2. human.

    Polymorphism databases

    DMDMi73917746.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151842 mRNA. Translation: AAD34079.1 .
    AL080122 mRNA. Translation: CAB45721.1 .
    AK296072 mRNA. Translation: BAG58830.1 .
    CR533456 mRNA. Translation: CAG38487.1 .
    AK222654 mRNA. Translation: BAD96374.1 .
    AC123511 Genomic DNA. No translation available.
    AC130885 Genomic DNA. No translation available.
    BC001553 mRNA. Translation: AAH01553.1 .
    CCDSi CCDS2918.1. [Q9UQN3-1 ]
    CCDS58840.1. [Q9UQN3-2 ]
    PIRi T12468.
    RefSeqi NP_001231573.1. NM_001244644.1. [Q9UQN3-2 ]
    NP_054762.2. NM_014043.3. [Q9UQN3-1 ]
    UniGenei Hs.476930.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JQK NMR - B 195-213 [» ]
    ProteinModelPortali Q9UQN3.
    SMRi Q9UQN3. Positions 7-141.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117462. 15 interactions.
    DIPi DIP-50766N.
    IntActi Q9UQN3. 6 interactions.
    MINTi MINT-1430090.
    STRINGi 9606.ENSP00000263780.

    PTM databases

    PhosphoSitei Q9UQN3.

    Polymorphism databases

    DMDMi 73917746.

    Proteomic databases

    MaxQBi Q9UQN3.
    PaxDbi Q9UQN3.
    PRIDEi Q9UQN3.

    Protocols and materials databases

    DNASUi 25978.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263780 ; ENSP00000263780 ; ENSG00000083937 . [Q9UQN3-1 ]
    ENST00000471660 ; ENSP00000419998 ; ENSG00000083937 . [Q9UQN3-2 ]
    GeneIDi 25978.
    KEGGi hsa:25978.
    UCSCi uc003dqp.4. human. [Q9UQN3-1 ]
    uc011bgn.2. human.

    Organism-specific databases

    CTDi 25978.
    GeneCardsi GC03P087360.
    GeneReviewsi CHMP2B.
    HGNCi HGNC:24537. CHMP2B.
    HPAi HPA035069.
    HPA052754.
    MIMi 600795. phenotype.
    609512. gene.
    614696. phenotype.
    neXtProti NX_Q9UQN3.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    275864. Behavioral variant of frontotemporal dementia.
    100070. Progressive non-fluent aphasia.
    100069. Semantic dementia.
    PharmGKBi PA142672112.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268821.
    HOGENOMi HOG000177218.
    HOVERGENi HBG102628.
    InParanoidi Q9UQN3.
    KOi K12192.
    OMAi KTMQDFQ.
    OrthoDBi EOG79GT8Q.
    PhylomeDBi Q9UQN3.
    TreeFami TF314163.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    ChiTaRSi CHMP2B. human.
    EvolutionaryTracei Q9UQN3.
    GeneWikii CHMP2B.
    GenomeRNAii 25978.
    NextBioi 47630.
    PROi Q9UQN3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQN3.
    Bgeei Q9UQN3.
    CleanExi HS_CHMP2B.
    Genevestigatori Q9UQN3.

    Family and domain databases

    InterProi IPR005024. Snf7.
    [Graphical view ]
    Pfami PF03357. Snf7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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: Thalamus.
    4. "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] (ISOFORM 1).
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Cervix.
    8. "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: INTERACTION WITH CHMP2A.
    9. Erratum
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
    10. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT FTD3 TYR-148.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. Cited for: STRUCTURE BY NMR OF 195-213 IN COMPLEX WITH VPS4B, INTERACTION WITH VPS4A.
    19. Cited for: VARIANT ALS17 HIS-206, VARIANT VAL-29.
    20. Cited for: VARIANTS ALS17 VAL-29; ASN-104 AND HIS-206, CHARACTERIZATION OF VARIANTS ALS17 VAL-29; ASN-104 AND HIS-206.

    Entry informationi

    Entry nameiCHM2B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQN3
    Secondary accession number(s): B4DJG8, Q53HC7, Q9Y4U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 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 3
      Human chromosome 3: 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