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Q9UQN3

- CHM2B_HUMAN

UniProt

Q9UQN3 - CHM2B_HUMAN

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Protein

Charged multivesicular body protein 2b

Gene
CHMP2B, CGI-84
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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
Complete GO annotation...

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. Late endosome membrane; Peripheral membrane protein Inferred 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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.

Miscellaneous databases

EvolutionaryTraceiQ9UQN3.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 5531 Reviewed predictionAdd
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.

Sequence similaritiesi

Belongs to the SNF7 family.

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

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. VSP_045142Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

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