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Protein

Putative nucleotidyltransferase MAB21L1

Gene

MAB21L1

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

Functioni

Putative nucleotidyltransferase required for several aspects of embryonic development including normal development of the eye (By similarity). It is unclear whether it displays nucleotidyltransferase activity in vivo (PubMed:27271801). Binds single-stranded RNA (ssRNA) (PubMed:27271801).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi73Magnesium; catalyticBy similarity1
Metal bindingi75Magnesium; catalyticBy similarity1
Binding sitei248NTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi23 – 24NTPCombined sources1 Publication2
Nucleotide bindingi63 – 66NTPCombined sources1 Publication4
Nucleotide bindingi252 – 255NTPCombined sources1 Publication4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Nucleotidyltransferase, Transferase
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative nucleotidyltransferase MAB21L1Curated (EC:2.7.7.-Curated)
Alternative name(s):
Protein mab-21-like 1Imported
Gene namesi
Name:MAB21L1Imported
Synonyms:CAGR11 Publication
ORF Names:Nbla001261 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000180660.7
HGNCiHGNC:6757 MAB21L1
MIMi601280 gene
neXtProtiNX_Q13394

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi51R → C: Decreased protein stability. 1 Publication1
Mutagenesisi247R → Q: Decreased protein stability. 1 Publication1

Organism-specific databases

DisGeNETi4081
OpenTargetsiENSG00000180660
PharmGKBiPA30516

Polymorphism and mutation databases

BioMutaiMAB21L1
DMDMi74739786

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003127811 – 359Putative nucleotidyltransferase MAB21L1Add BLAST359

Proteomic databases

PaxDbiQ13394
PeptideAtlasiQ13394
PRIDEiQ13394
ProteomicsDBi59364
TopDownProteomicsiQ13394

PTM databases

iPTMnetiQ13394
PhosphoSitePlusiQ13394

Expressioni

Tissue specificityi

Expressed in brain, cerebellum and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000180660
CleanExiHS_MAB21L1
ExpressionAtlasiQ13394 baseline and differential
GenevisibleiQ13394 HS

Organism-specific databases

HPAiHPA049324
HPA059864

Interactioni

Subunit structurei

Monomer (PubMed:27271801). Homodecamer; composed of 2 back to back homopentamers (PubMed:27271801). The protein may exist as monomer in solution and oiligomerizes upon ligand binding (PubMed:27271801).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SIAH1Q8IUQ43EBI-10229059,EBI-747107

Protein-protein interaction databases

BioGridi110256, 11 interactors
IntActiQ13394, 1 interactor
STRINGi9606.ENSP00000369251

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 48Combined sources47
Beta strandi66 – 70Combined sources5
Beta strandi73 – 79Combined sources7
Beta strandi86 – 89Combined sources4
Beta strandi97 – 106Combined sources10
Turni108 – 110Combined sources3
Helixi114 – 116Combined sources3
Beta strandi121 – 123Combined sources3
Helixi125 – 142Combined sources18
Helixi146 – 148Combined sources3
Beta strandi149 – 151Combined sources3
Beta strandi159 – 162Combined sources4
Turni163 – 165Combined sources3
Beta strandi166 – 176Combined sources11
Helixi182 – 184Combined sources3
Helixi197 – 205Combined sources9
Beta strandi208 – 211Combined sources4
Beta strandi230 – 233Combined sources4
Helixi235 – 241Combined sources7
Helixi247 – 261Combined sources15
Helixi271 – 284Combined sources14
Helixi288 – 291Combined sources4
Helixi293 – 295Combined sources3
Helixi296 – 312Combined sources17
Turni326 – 329Combined sources4
Helixi332 – 351Combined sources20
Helixi353 – 358Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EOGX-ray3.05A/B/C/D/F2-359[»]
5EOMX-ray2.55A/B/C/D/E/F/G/H/I/J2-359[»]
ProteinModelPortaliQ13394
SMRiQ13394
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

While it shares structure similarities with CGAS, it also features a number of differences. The crystal structure is in inactive conformation and the enzyme would require a conformational change to be active. The nucleotidyltransferase activity is therefore unclear.1 Publication

Sequence similaritiesi

Belongs to the mab-21 family.Curated

Phylogenomic databases

eggNOGiKOG3963 Eukaryota
ENOG410XNRJ LUCA
GeneTreeiENSGT00510000046791
HOGENOMiHOG000007337
HOVERGENiHBG053080
InParanoidiQ13394
OMAiYFLPHVD
OrthoDBiEOG091G0939
PhylomeDBiQ13394
TreeFamiTF315012

Family and domain databases

InterProiView protein in InterPro
IPR024810 Mab-21_dom
PfamiView protein in Pfam
PF03281 Mab-21, 1 hit
SMARTiView protein in SMART
SM01265 Mab-21, 1 hit

Sequencei

Sequence statusi: Complete.

Q13394-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAAQAKLVY HLNKYYNEKC QARKAAIAKT IREVCKVVSD VLKEVEVQEP
60 70 80 90 100
RFISSLNEMD NRYEGLEVIS PTEFEVVLYL NQMGVFNFVD DGSLPGCAVL
110 120 130 140 150
KLSDGRKRSM SLWVEFITAS GYLSARKIRS RFQTLVAQAV DKCSYRDVVK
160 170 180 190 200
MVADTSEVKL RIRDRYVVQI TPAFKCTGIW PRSAAHWPLP HIPWPGPNRV
210 220 230 240 250
AEVKAEGFNL LSKECHSLAG KQSSAESDAW VLQFAEAENR LQMGGCRKKC
260 270 280 290 300
LSILKTLRDR HLELPGQPLN NYHMKTLVSY ECEKHPRESD WDESCLGDRL
310 320 330 340 350
NGILLQLISC LQCRRCPHYF LPNLDLFQGK PHSALENAAK QTWRLAREIL

TNPKSLEKL
Length:359
Mass (Da):40,956
Last modified:November 1, 1996 - v1
Checksum:iA27C53FBC997A049
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132F → L in CAG33701 (Ref. 3) Curated1

Polymorphismi

A CAG trinucleotide repeat occurs in the 5'-UTR of this gene. This repeat has been found to be highly polymorphic, although expanded alleles have not yet been definitely linked with any phenotypic abnormality.4 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03756870S → P. Corresponds to variant dbSNP:rs1065316Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38810 mRNA Translation: AAB47576.1
AB073388 mRNA Translation: BAE45718.1
CR457420 mRNA Translation: CAG33701.1
AL390071 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08547.1
BC028170 mRNA Translation: AAH28170.1
CCDSiCCDS9353.1
PIRiG02221
RefSeqiNP_005575.1, NM_005584.4
UniGeneiHs.584776

Genome annotation databases

EnsembliENST00000379919; ENSP00000369251; ENSG00000180660
GeneIDi4081
KEGGihsa:4081
UCSCiuc032aca.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMB211_HUMAN
AccessioniPrimary (citable) accession number: Q13394
Secondary accession number(s): Q6I9T5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 1, 1996
Last modified: June 20, 2018
This is version 126 of the entry and version 1 of the sequence. See 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 13
    Human chromosome 13: 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

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