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Protein

Putative methyltransferase C9orf114

Gene

C9orf114

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required both for chromosome alignment and for association of the centrosomes with the poles of the bipolar spindle during metaphase.1 Publication

GO - Molecular functioni

  1. methyltransferase activity Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Putative methyltransferase C9orf114Curated (EC:2.1.1.-Curated)
Gene namesi
Name:C9orf114
Synonyms:CENP-32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:26933. C9orf114.

Subcellular locationi

Chromosomecentromerekinetochore 1 Publication
Note: Associated with the outer kinetochore.1 Publication

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134958095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Putative methyltransferase C9orf114PRO_0000238468Add
BLAST

Proteomic databases

MaxQBiQ5T280.
PaxDbiQ5T280.
PRIDEiQ5T280.

PTM databases

PhosphoSiteiQ5T280.

Expressioni

Gene expression databases

BgeeiQ5T280.
CleanExiHS_C9orf114.
ExpressionAtlasiQ5T280. baseline and differential.
GenevestigatoriQ5T280.

Organism-specific databases

HPAiHPA022990.

Interactioni

Protein-protein interaction databases

BioGridi119567. 8 interactions.
IntActiQ5T280. 3 interactions.
MINTiMINT-4826834.
STRINGi9606.ENSP00000354812.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi74 – 807Combined sources
Helixi81 – 866Combined sources
Helixi90 – 10617Combined sources
Beta strandi110 – 1156Combined sources
Helixi137 – 15014Combined sources
Helixi153 – 1553Combined sources
Helixi156 – 1594Combined sources
Helixi167 – 1726Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi240 – 2478Combined sources
Helixi251 – 2566Combined sources
Beta strandi263 – 2697Combined sources
Helixi270 – 2756Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi293 – 2953Combined sources
Helixi296 – 2983Combined sources
Beta strandi305 – 3106Combined sources
Helixi318 – 3236Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 3438Combined sources
Beta strandi347 – 3493Combined sources
Helixi353 – 37220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RG1X-ray1.86A/B64-376[»]
ProteinModelPortaliQ5T280.
SMRiQ5T280. Positions 75-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2106.
GeneTreeiENSGT00390000016537.
HOGENOMiHOG000230622.
HOVERGENiHBG058241.
InParanoidiQ5T280.
KOiK09142.
OMAiKDLQYAG.
OrthoDBiEOG773XGP.
PhylomeDBiQ5T280.
TreeFamiTF105821.

Family and domain databases

Gene3Di3.40.1280.10. 2 hits.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR012340. NA-bd_OB-fold.
IPR003750. Put_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PANTHERiPTHR12150. PTHR12150. 1 hit.
PfamiPF02598. Methyltrn_RNA_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF75217. SSF75217. 2 hits.

Sequencei

Sequence statusi: Complete.

Q5T280-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAERGRKRPC GPGEHGQRIE WRKWKQQKKE EKKKWKDLKL MKKLERQRAQ
60 70 80 90 100
EEQAKRLEEE EAAAEKEDRG RPYTLSVALP GSILDNAQSP ELRTYLAGQI
110 120 130 140 150
ARACAIFCVD EIVVFDEEGQ DAKTVEGEFT GVGKKGQACV QLARILQYLE
160 170 180 190 200
CPQYLRKAFF PKHQDLQFAG LLNPLDSPHH MRQDEESEFR EGIVVDRPTR
210 220 230 240 250
PGHGSFVNCG MKKEVKIDKN LEPGLRVTVR LNQQQHPDCK TYHGKVVSSQ
260 270 280 290 300
DPRTKAGLYW GYTVRLASCL SAVFAEAPFQ DGYDLTIGTS ERGSDVASAQ
310 320 330 340 350
LPNFRHALVV FGGLQGLEAG ADADPNLEVA EPSVLFDLYV NTCPGQGSRT
360 370
IRTEEAILIS LAALQPGLIQ AGARHT
Length:376
Mass (Da):42,009
Last modified:February 20, 2007 - v3
Checksum:i30A5AA406834DC27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431C → Y in AAH33677. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631A → V.
Corresponds to variant rs34500948 [ dbSNP | Ensembl ].
VAR_050844
Natural varianti130 – 1301T → R.1 Publication
Corresponds to variant rs6478854 [ dbSNP | Ensembl ].
VAR_026552
Natural varianti369 – 3691I → T.1 Publication
Corresponds to variant rs2280843 [ dbSNP | Ensembl ].
VAR_026553

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL441992 Genomic DNA. Translation: CAI15413.1.
BC010579 mRNA. Translation: AAH10579.1.
BC033677 mRNA. Translation: AAH33677.1.
BC039590 mRNA. Translation: AAH39590.1.
BC046133 mRNA. Translation: AAH46133.1.
BC063644 mRNA. Translation: AAH63644.1.
BC021273 mRNA. Translation: AAH21273.1.
CCDSiCCDS6913.1.
RefSeqiNP_057474.2. NM_016390.3.
UniGeneiHs.224137.

Genome annotation databases

EnsembliENST00000361256; ENSP00000354812; ENSG00000198917.
GeneIDi51490.
KEGGihsa:51490.
UCSCiuc004bwd.3. human.

Polymorphism databases

DMDMi126302532.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL441992 Genomic DNA. Translation: CAI15413.1.
BC010579 mRNA. Translation: AAH10579.1.
BC033677 mRNA. Translation: AAH33677.1.
BC039590 mRNA. Translation: AAH39590.1.
BC046133 mRNA. Translation: AAH46133.1.
BC063644 mRNA. Translation: AAH63644.1.
BC021273 mRNA. Translation: AAH21273.1.
CCDSiCCDS6913.1.
RefSeqiNP_057474.2. NM_016390.3.
UniGeneiHs.224137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RG1X-ray1.86A/B64-376[»]
ProteinModelPortaliQ5T280.
SMRiQ5T280. Positions 75-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119567. 8 interactions.
IntActiQ5T280. 3 interactions.
MINTiMINT-4826834.
STRINGi9606.ENSP00000354812.

PTM databases

PhosphoSiteiQ5T280.

Polymorphism databases

DMDMi126302532.

Proteomic databases

MaxQBiQ5T280.
PaxDbiQ5T280.
PRIDEiQ5T280.

Protocols and materials databases

DNASUi51490.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361256; ENSP00000354812; ENSG00000198917.
GeneIDi51490.
KEGGihsa:51490.
UCSCiuc004bwd.3. human.

Organism-specific databases

CTDi51490.
GeneCardsiGC09M131581.
HGNCiHGNC:26933. C9orf114.
HPAiHPA022990.
neXtProtiNX_Q5T280.
PharmGKBiPA134958095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2106.
GeneTreeiENSGT00390000016537.
HOGENOMiHOG000230622.
HOVERGENiHBG058241.
InParanoidiQ5T280.
KOiK09142.
OMAiKDLQYAG.
OrthoDBiEOG773XGP.
PhylomeDBiQ5T280.
TreeFamiTF105821.

Miscellaneous databases

GenomeRNAii51490.
NextBioi55150.

Gene expression databases

BgeeiQ5T280.
CleanExiHS_C9orf114.
ExpressionAtlasiQ5T280. baseline and differential.
GenevestigatoriQ5T280.

Family and domain databases

Gene3Di3.40.1280.10. 2 hits.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR012340. NA-bd_OB-fold.
IPR003750. Put_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PANTHERiPTHR12150. PTHR12150. 1 hit.
PfamiPF02598. Methyltrn_RNA_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF75217. SSF75217. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANTS ARG-130 AND THR-369.
    Tissue: Brain, Eye, Leukocyte, Ovary and Testis.
  3. "The protein composition of mitotic chromosomes determined using multiclassifier combinatorial proteomics."
    Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L., Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T., Earnshaw W.C., Rappsilber J.
    Cell 142:810-821(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCI114_HUMAN
AccessioniPrimary (citable) accession number: Q5T280
Secondary accession number(s): Q0D2P6
, Q6P469, Q6PGP9, Q6PIJ1, Q6PJV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 20, 2007
Last modified: February 4, 2015
This is version 77 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

Miscellaneous

Depletion with RNAi causes a significant accumulation of cells in later prometaphase with misaligned chromosomes.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.