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Protein

AN1-type zinc finger protein 2B

Gene

Zfand2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 5246AN1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri97 – 14549AN1-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
AN1-type zinc finger protein 2B
Alternative name(s):
Arsenite-inducible RNA-associated protein-like protein
Short name:
AIRAP-like protein
Gene namesi
Name:Zfand2b
Synonyms:Airapl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1916068. Zfand2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi254 – 2541C → S: Loss of localization to the endoplasmic reticulum. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257AN1-type zinc finger protein 2BPRO_0000232877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91X58.
MaxQBiQ91X58.
PaxDbiQ91X58.
PRIDEiQ91X58.

PTM databases

iPTMnetiQ91X58.
PhosphoSiteiQ91X58.

Expressioni

Gene expression databases

BgeeiQ91X58.
CleanExiMM_ZFAND2B.
ExpressionAtlasiQ91X58. baseline and differential.
GenevisibleiQ91X58. MM.

Interactioni

Subunit structurei

Interacts (via VIM motif) with VCP. Upon exposure to arsenite, associates with proteasomes.By similarity1 Publication

Protein-protein interaction databases

DIPiDIP-46091N.
STRINGi10090.ENSMUSP00000027394.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi199 – 21012Combined sources
Turni215 – 2184Combined sources
Helixi222 – 23514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XKHX-ray3.00C/E/H187-240[»]
ProteinModelPortaliQ91X58.
SMRiQ91X58. Positions 5-44, 93-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 21620UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 24020UIM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 15111VCP/p97-interacting motif (VIM)By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi170 – 1756Poly-Ser

Sequence similaritiesi

Contains 2 AN1-type zinc fingers.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 5246AN1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri97 – 14549AN1-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3183. Eukaryota.
ENOG4111JCH. LUCA.
GeneTreeiENSGT00730000110968.
HOGENOMiHOG000243115.
HOVERGENiHBG061194.
InParanoidiQ91X58.
OMAiNPRPVSN.
PhylomeDBiQ91X58.
TreeFamiTF314219.

Family and domain databases

Gene3Di4.10.1110.10. 2 hits.
InterProiIPR003903. UIM_dom.
IPR000058. Znf_AN1.
[Graphical view]
PfamiPF01428. zf-AN1. 2 hits.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
SM00154. ZnF_AN1. 2 hits.
[Graphical view]
PROSITEiPS50330. UIM. 1 hit.
PS51039. ZF_AN1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91X58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFPDLGAHC SEPSCQRLDF LPLKCDACSG IFCADHVAYA QHHCGSAYQK
60 70 80 90 100
DIQVPVCPLC NVPVPVARGE PPDRAVGEHI DRDCRSDPAQ QKRKIFTNKC
110 120 130 140 150
ERSGCRQREM MKLTCDRCGR NFCIKHRHPL DHECSGEGHQ TSRAGLAAIS
160 170 180 190 200
RAQGLASTST APSPSRTLPS SSSPSRATPQ LPTRTASPVI ALQNGLSEDE
210 220 230 240 250
ALQRALELSL AEAKPQVLSS QEEDDLALAQ ALSASEAEYQ QQQAQSRSLK

PSNCSLC
Length:257
Mass (Da):27,895
Last modified:December 1, 2001 - v1
Checksum:iD9B35C96BB3876E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741P → S in BAB23266 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004332 mRNA. Translation: BAB23266.1.
AK151430 mRNA. Translation: BAE30394.1.
BC011495 mRNA. Translation: AAH11495.1.
CCDSiCCDS15064.1.
RefSeqiNP_001153377.1. NM_001159905.1.
NP_001153378.1. NM_001159906.1.
NP_081122.2. NM_026846.3.
UniGeneiMm.32646.

Genome annotation databases

EnsembliENSMUST00000027394; ENSMUSP00000027394; ENSMUSG00000026197.
ENSMUST00000160439; ENSMUSP00000125086; ENSMUSG00000026197.
GeneIDi68818.
KEGGimmu:68818.
UCSCiuc007bnw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004332 mRNA. Translation: BAB23266.1.
AK151430 mRNA. Translation: BAE30394.1.
BC011495 mRNA. Translation: AAH11495.1.
CCDSiCCDS15064.1.
RefSeqiNP_001153377.1. NM_001159905.1.
NP_001153378.1. NM_001159906.1.
NP_081122.2. NM_026846.3.
UniGeneiMm.32646.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XKHX-ray3.00C/E/H187-240[»]
ProteinModelPortaliQ91X58.
SMRiQ91X58. Positions 5-44, 93-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46091N.
STRINGi10090.ENSMUSP00000027394.

PTM databases

iPTMnetiQ91X58.
PhosphoSiteiQ91X58.

Proteomic databases

EPDiQ91X58.
MaxQBiQ91X58.
PaxDbiQ91X58.
PRIDEiQ91X58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027394; ENSMUSP00000027394; ENSMUSG00000026197.
ENSMUST00000160439; ENSMUSP00000125086; ENSMUSG00000026197.
GeneIDi68818.
KEGGimmu:68818.
UCSCiuc007bnw.2. mouse.

Organism-specific databases

CTDi130617.
MGIiMGI:1916068. Zfand2b.

Phylogenomic databases

eggNOGiKOG3183. Eukaryota.
ENOG4111JCH. LUCA.
GeneTreeiENSGT00730000110968.
HOGENOMiHOG000243115.
HOVERGENiHBG061194.
InParanoidiQ91X58.
OMAiNPRPVSN.
PhylomeDBiQ91X58.
TreeFamiTF314219.

Miscellaneous databases

NextBioi328001.
PROiQ91X58.
SOURCEiSearch...

Gene expression databases

BgeeiQ91X58.
CleanExiMM_ZFAND2B.
ExpressionAtlasiQ91X58. baseline and differential.
GenevisibleiQ91X58. MM.

Family and domain databases

Gene3Di4.10.1110.10. 2 hits.
InterProiIPR003903. UIM_dom.
IPR000058. Znf_AN1.
[Graphical view]
PfamiPF01428. zf-AN1. 2 hits.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
SM00154. ZnF_AN1. 2 hits.
[Graphical view]
PROSITEiPS50330. UIM. 1 hit.
PS51039. ZF_AN1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Embryo.
  2. "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].
    Strain: FVB/N.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans."
    Yun C., Stanhill A., Yang Y., Zhang Y., Haynes C.M., Xu C.F., Neubert T.A., Mor A., Philips M.R., Ron D.
    Proc. Natl. Acad. Sci. U.S.A. 105:7094-7099(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROTEASOMES, MUTAGENESIS OF CYS-254.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiZFN2B_MOUSE
AccessioniPrimary (citable) accession number: Q91X58
Secondary accession number(s): Q9D0W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.