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Protein

Abscission/NoCut checkpoint regulator

Gene

ZFYVE19

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

Functioni

Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri74 – 13360FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate binding Source: UniProtKB

GO - Biological processi

  • abscission Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • negative regulation of cytokinesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

Lipid-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Abscission/NoCut checkpoint regulator
Short name:
ANCHR
Alternative name(s):
MLL partner containing FYVE domain
Zinc finger FYVE domain-containing protein 19
Gene namesi
Name:ZFYVE19
Synonyms:ANCHR, MPFYVE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:20758. ZFYVE19.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • midbody Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving ZFYVE19 is associated with acute myeloblastic leukemia (AML). Translocation t(11;15)(q23;q14) with KMT2A/MLL1 (PubMed:12618766).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011R → A: Abolishes binding to phosphatidylinositol-3-phosphate (PtdIns(3)P) without affecting localization to the midbody. 1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei145 – 1462Breakpoint for translocation to form KMT2A/MLL1-ZFYVE19

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA134906967.

Polymorphism and mutation databases

BioMutaiZFYVE19.
DMDMi296453076.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Abscission/NoCut checkpoint regulatorPRO_0000098718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki207 – 207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei243 – 2431PhosphothreonineCombined sources
Modified residuei354 – 3541PhosphoserineCombined sources
Modified residuei463 – 4631PhosphoserineCombined sources
Isoform 3 (identifier: Q96K21-3)
Modified residuei286 – 2861PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96K21.
MaxQBiQ96K21.
PaxDbiQ96K21.
PRIDEiQ96K21.

PTM databases

iPTMnetiQ96K21.
PhosphoSiteiQ96K21.

Expressioni

Tissue specificityi

Detected in brain, heart, skeletal muscle, kidney and liver.1 Publication

Gene expression databases

BgeeiQ96K21.
CleanExiHS_ZFYVE19.
ExpressionAtlasiQ96K21. baseline and differential.
GenevisibleiQ96K21. HS.

Organism-specific databases

HPAiHPA040283.

Interactioni

Subunit structurei

Interacts (via MIM1-B) with VPS4A; interaction takes place at the midbody ring following cytokinesis checkpoint activation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CAPN7Q7Z4793EBI-10187928,EBI-10213454
CCHCR1Q8TD31-33EBI-10187928,EBI-10175300
HTTP428583EBI-6448240,EBI-466029
MITD1Q8WV923EBI-6448240,EBI-2691489
VPS4BO753513EBI-6448240,EBI-2514459

Protein-protein interaction databases

BioGridi124370. 43 interactions.
DIPiDIP-60854N.
IntActiQ96K21. 6 interactions.
STRINGi9606.ENSP00000347498.

Structurei

3D structure databases

ProteinModelPortaliQ96K21.
SMRiQ96K21. Positions 76-150, 418-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili311 – 37565Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi174 – 18714MIM1-AAdd
BLAST
Motifi326 – 33914MIM1-BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi412 – 4176Poly-Glu
Compositional biasi421 – 44424Cys-richAdd
BLAST

Domaini

The FYVE-type zinc finger mediates binding to phosphatidylinositol-3-phosphate (PtdIns3P).1 Publication
The MIM1-B motif mediates interaction with VPS4A.1 Publication

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri74 – 13360FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1818. Eukaryota.
ENOG410XNRF. LUCA.
GeneTreeiENSGT00390000016108.
HOGENOMiHOG000231992.
HOVERGENiHBG057281.
InParanoidiQ96K21.
OMAiRCGNTQQ.
PhylomeDBiQ96K21.
TreeFamiTF317652.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96K21-1) [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
MNYDSQQPPL PPLPYAGCRR ASGFPALGRG GTVPVGVWGG AGQGREGRSW
60 70 80 90 100
GEGPRGPGLG RRDLSSADPA VLGATMESRC YGCAVKFTLF KKEYGCKNCG
110 120 130 140 150
RAFCSGCLSF SAAVPRTGNT QQKVCKQCHE VLTRGSSANA SKWSPPQNYK
160 170 180 190 200
KRVAALEAKQ KPSTSQSQGL TRQDQMIAER LARLRQENKP KLVPSQAEIE
210 220 230 240 250
ARLAALKDER QGSIPSTQEM EARLAALQGR VLPSQTPQPA HHTPDTRTQA
260 270 280 290 300
QQTQDLLTQL AAEVAIDESW KGGGPAASLQ NDLNQGGPGS TNSKRQANWS
310 320 330 340 350
LEEEKSRLLA EAALELREEN TRQERILALA KRLAMLRGQD PERVTLQDYR
360 370 380 390 400
LPDSDDDEDE ETAIQRVLQQ LTEEASLDEA SGFNIPAEQA SRPWTQPRGA
410 420 430 440 450
EPEAQDVDPR PEAEEEELPW CCICNEDATL RCAGCDGDLF CARCFREGHD
460 470
AFELKEHQTS AYSPPRAGQE H
Length:471
Mass (Da):51,546
Last modified:May 18, 2010 - v3
Checksum:i0F07D2DDFD19864D
GO
Isoform 2 (identifier: Q96K21-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MNYDSQQPPL...AVKFTLFKKE → MPAVAEALGQ...DLPDSSGKLQ

Show »
Length:461
Mass (Da):50,534
Checksum:i0366891B7E766686
GO
Isoform 3 (identifier: Q96K21-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-343: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:403
Mass (Da):43,934
Checksum:iF2D8DF956362DABF
GO
Isoform 4 (identifier: Q96K21-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-175: Missing.

Note: No experimental confirmation available.
Show »
Length:296
Mass (Da):32,963
Checksum:i53D85D6E28C521A1
GO

Sequence cautioni

The sequence AAH21092.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO73862.1 differs from that shown. Reason: Frameshift at position 459. Curated
The sequence BAB55338.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041C → R in AAH21092 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti210 – 2101R → H.
Corresponds to variant rs34819163 [ dbSNP | Ensembl ].
VAR_057494
Natural varianti376 – 3761S → A.2 Publications
Corresponds to variant rs690347 [ dbSNP | Ensembl ].
VAR_060474
Natural varianti398 – 3981R → C.
Corresponds to variant rs72735636 [ dbSNP | Ensembl ].
VAR_060475

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 175175Missing in isoform 4. 1 PublicationVSP_046008Add
BLAST
Alternative sequencei1 – 9393MNYDS…LFKKE → MPAVAEALGQEGPPDLSRSA FLATVLTSLSAAFSSMPSSA YSLPFSRSLELDYHTSSCFR GTMVKADCPVPITDLPDSSG KLQ in isoform 2. 1 PublicationVSP_013791Add
BLAST
Alternative sequencei276 – 34368Missing in isoform 3. 1 PublicationVSP_013792Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF445414 mRNA. Translation: AAO73862.1. Frameshift.
AK027746 mRNA. Translation: BAB55338.1. Different initiation.
AK122779 mRNA. Translation: BAG53724.1.
AC012476 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92451.1.
BC021092 mRNA. Translation: AAH21092.1. Different initiation.
CCDSiCCDS42025.1. [Q96K21-1]
CCDS58353.1. [Q96K21-2]
CCDS58354.1. [Q96K21-3]
CCDS58355.1. [Q96K21-4]
RefSeqiNP_001070736.1. NM_001077268.1. [Q96K21-1]
NP_001245349.1. NM_001258420.1. [Q96K21-3]
NP_001245350.1. NM_001258421.1. [Q96K21-4]
NP_116239.3. NM_032850.4. [Q96K21-2]
UniGeneiHs.121676.

Genome annotation databases

EnsembliENST00000299173; ENSP00000299173; ENSG00000166140. [Q96K21-3]
ENST00000336455; ENSP00000337824; ENSG00000166140. [Q96K21-2]
ENST00000355341; ENSP00000347498; ENSG00000166140. [Q96K21-1]
ENST00000564258; ENSP00000457617; ENSG00000166140. [Q96K21-4]
GeneIDi84936.
KEGGihsa:84936.
UCSCiuc001zmt.2. human. [Q96K21-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF445414 mRNA. Translation: AAO73862.1. Frameshift.
AK027746 mRNA. Translation: BAB55338.1. Different initiation.
AK122779 mRNA. Translation: BAG53724.1.
AC012476 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92451.1.
BC021092 mRNA. Translation: AAH21092.1. Different initiation.
CCDSiCCDS42025.1. [Q96K21-1]
CCDS58353.1. [Q96K21-2]
CCDS58354.1. [Q96K21-3]
CCDS58355.1. [Q96K21-4]
RefSeqiNP_001070736.1. NM_001077268.1. [Q96K21-1]
NP_001245349.1. NM_001258420.1. [Q96K21-3]
NP_001245350.1. NM_001258421.1. [Q96K21-4]
NP_116239.3. NM_032850.4. [Q96K21-2]
UniGeneiHs.121676.

3D structure databases

ProteinModelPortaliQ96K21.
SMRiQ96K21. Positions 76-150, 418-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124370. 43 interactions.
DIPiDIP-60854N.
IntActiQ96K21. 6 interactions.
STRINGi9606.ENSP00000347498.

PTM databases

iPTMnetiQ96K21.
PhosphoSiteiQ96K21.

Polymorphism and mutation databases

BioMutaiZFYVE19.
DMDMi296453076.

Proteomic databases

EPDiQ96K21.
MaxQBiQ96K21.
PaxDbiQ96K21.
PRIDEiQ96K21.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299173; ENSP00000299173; ENSG00000166140. [Q96K21-3]
ENST00000336455; ENSP00000337824; ENSG00000166140. [Q96K21-2]
ENST00000355341; ENSP00000347498; ENSG00000166140. [Q96K21-1]
ENST00000564258; ENSP00000457617; ENSG00000166140. [Q96K21-4]
GeneIDi84936.
KEGGihsa:84936.
UCSCiuc001zmt.2. human. [Q96K21-1]

Organism-specific databases

CTDi84936.
GeneCardsiZFYVE19.
H-InvDBHIX0012140.
HGNCiHGNC:20758. ZFYVE19.
HPAiHPA040283.
neXtProtiNX_Q96K21.
PharmGKBiPA134906967.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1818. Eukaryota.
ENOG410XNRF. LUCA.
GeneTreeiENSGT00390000016108.
HOGENOMiHOG000231992.
HOVERGENiHBG057281.
InParanoidiQ96K21.
OMAiRCGNTQQ.
PhylomeDBiQ96K21.
TreeFamiTF317652.

Miscellaneous databases

ChiTaRSiZFYVE19. human.
GeneWikiiZFYVE19.
GenomeRNAii84936.
PROiQ96K21.

Gene expression databases

BgeeiQ96K21.
CleanExiHS_ZFYVE19.
ExpressionAtlasiQ96K21. baseline and differential.
GenevisibleiQ96K21. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15."
    Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J., Rowley J.D.
    Oncogene 22:1400-1410(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-471 (ISOFORM 1), VARIANT ALA-376.
    Tissue: Ovary and Synovium.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 64-471 (ISOFORM 3), VARIANT ALA-376.
    Tissue: Lung.
  6. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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 THR-243; SER-354 AND SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
    Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
    Nat. Cell Biol. 16:550-560(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, MUTAGENESIS OF ARG-101.
  14. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiANCHR_HUMAN
AccessioniPrimary (citable) accession number: Q96K21
Secondary accession number(s): B3KVB2
, C9JNF4, H3BUF9, Q86WC2, Q8WU96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 130 of the entry and version 3 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

Phosphorylated in vitro at Ser-22 by AURKB; however, phosphorylation at this site could not be confirmed in vivo.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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