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Protein

Ashwin

Gene

C2orf49

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

Functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Ashwin
Gene namesi
Name:C2orf49
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:28772. C2orf49.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • tRNA-splicing ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162379179.

Polymorphism and mutation databases

DMDMi74733311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 232232AshwinPRO_0000268859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei197 – 1971PhosphothreonineCombined sources
Modified residuei198 – 1981PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BVC5.
MaxQBiQ9BVC5.
PaxDbiQ9BVC5.
PeptideAtlasiQ9BVC5.
PRIDEiQ9BVC5.

PTM databases

iPTMnetiQ9BVC5.
PhosphoSiteiQ9BVC5.

Expressioni

Gene expression databases

BgeeiQ9BVC5.
CleanExiHS_C2orf49.
ExpressionAtlasiQ9BVC5. baseline and differential.
GenevisibleiQ9BVC5. HS.

Organism-specific databases

HPAiHPA043846.
HPA060814.

Interactioni

Subunit structurei

Component of the tRNA-splicing ligase complex.2 Publications

Protein-protein interaction databases

BioGridi122525. 10 interactions.
MINTiMINT-3297606.
STRINGi9606.ENSP00000258457.

Structurei

3D structure databases

ProteinModelPortaliQ9BVC5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ashwin family.Curated

Phylogenomic databases

eggNOGiENOG410IGF7. Eukaryota.
ENOG4111XKJ. LUCA.
GeneTreeiENSGT00390000007488.
HOGENOMiHOG000034099.
HOVERGENiHBG080774.
InParanoidiQ9BVC5.
KOiK15432.
OMAiQHEMKNE.
OrthoDBiEOG7M3J1X.
PhylomeDBiQ9BVC5.
TreeFamiTF332084.

Family and domain databases

InterProiIPR024887. Ashwin.
[Graphical view]
PfamiPF15323. Ashwin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BVC5-1) [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
MAGDVGGRSC TDSELLLHPE LLSQEFLLLT LEQKNIAVET DVRVNKDSLT
60 70 80 90 100
DLYVQHAIPL PQRDLPKNRW GKMMEKKREQ HEIKNETKRS STVDGLRKRP
110 120 130 140 150
LIVFDGSSTS TSIKVKKTEN GDNDRLKPPP QASFTSNAFR KLSNSSSSVS
160 170 180 190 200
PLILSSNLPV NNKTEHNNND AKQNHDLTHR KSPSGPVKSP PLSPVGTTPV
210 220 230
KLKRAAPKEE AEAMNNLKPP QAKRKIQHVT WP
Length:232
Mass (Da):25,858
Last modified:June 1, 2001 - v1
Checksum:i27A5611FA270FB3E
GO
Isoform 2 (identifier: Q9BVC5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRRLRVTTHASLRPSTSLPQRFLRGALWVADWGLLATTM
     131-172: Missing.

Note: No experimental confirmation available.
Show »
Length:228
Mass (Da):25,675
Checksum:i114F61B4181DA412
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851G → D.1 Publication
Corresponds to variant rs28930676 [ dbSNP | Ensembl ].
VAR_029759

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRRLRVTTHASLRPSTSLPQ RFLRGALWVADWGLLATTM in isoform 2. 1 PublicationVSP_054353
Alternative sequencei131 – 17242Missing in isoform 2. 1 PublicationVSP_054354Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK127661 mRNA. Translation: BAG54545.1.
AK304268 mRNA. Translation: BAG65131.1.
AC012360 Genomic DNA. Translation: AAY15011.1.
BC001310 mRNA. Translation: AAH01310.1.
CCDSiCCDS2068.1. [Q9BVC5-1]
RefSeqiNP_001273466.1. NM_001286537.1.
NP_076998.1. NM_024093.2. [Q9BVC5-1]
XP_005264076.2. XM_005264019.3. [Q9BVC5-1]
UniGeneiHs.549577.

Genome annotation databases

EnsembliENST00000258457; ENSP00000258457; ENSG00000135974. [Q9BVC5-1]
GeneIDi79074.
KEGGihsa:79074.
UCSCiuc002tcs.3. human. [Q9BVC5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK127661 mRNA. Translation: BAG54545.1.
AK304268 mRNA. Translation: BAG65131.1.
AC012360 Genomic DNA. Translation: AAY15011.1.
BC001310 mRNA. Translation: AAH01310.1.
CCDSiCCDS2068.1. [Q9BVC5-1]
RefSeqiNP_001273466.1. NM_001286537.1.
NP_076998.1. NM_024093.2. [Q9BVC5-1]
XP_005264076.2. XM_005264019.3. [Q9BVC5-1]
UniGeneiHs.549577.

3D structure databases

ProteinModelPortaliQ9BVC5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122525. 10 interactions.
MINTiMINT-3297606.
STRINGi9606.ENSP00000258457.

PTM databases

iPTMnetiQ9BVC5.
PhosphoSiteiQ9BVC5.

Polymorphism and mutation databases

DMDMi74733311.

Proteomic databases

EPDiQ9BVC5.
MaxQBiQ9BVC5.
PaxDbiQ9BVC5.
PeptideAtlasiQ9BVC5.
PRIDEiQ9BVC5.

Protocols and materials databases

DNASUi79074.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258457; ENSP00000258457; ENSG00000135974. [Q9BVC5-1]
GeneIDi79074.
KEGGihsa:79074.
UCSCiuc002tcs.3. human. [Q9BVC5-1]

Organism-specific databases

CTDi79074.
GeneCardsiC2orf49.
HGNCiHGNC:28772. C2orf49.
HPAiHPA043846.
HPA060814.
neXtProtiNX_Q9BVC5.
PharmGKBiPA162379179.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGF7. Eukaryota.
ENOG4111XKJ. LUCA.
GeneTreeiENSGT00390000007488.
HOGENOMiHOG000034099.
HOVERGENiHBG080774.
InParanoidiQ9BVC5.
KOiK15432.
OMAiQHEMKNE.
OrthoDBiEOG7M3J1X.
PhylomeDBiQ9BVC5.
TreeFamiTF332084.

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Miscellaneous databases

GenomeRNAii79074.
NextBioi35477281.
PROiQ9BVC5.

Gene expression databases

BgeeiQ9BVC5.
CleanExiHS_C2orf49.
ExpressionAtlasiQ9BVC5. baseline and differential.
GenevisibleiQ9BVC5. HS.

Family and domain databases

InterProiIPR024887. Ashwin.
[Graphical view]
PfamiPF15323. Ashwin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2), VARIANT ASP-185.
    Tissue: Trachea.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Placenta.
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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].
  7. "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-182; SER-189; SER-193; THR-197 AND THR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-189; SER-193 AND THR-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
  11. "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-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."
    Popow J., Jurkin J., Schleiffer A., Martinez J.
    Nature 511:104-107(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.

Entry informationi

Entry nameiASHWN_HUMAN
AccessioniPrimary (citable) accession number: Q9BVC5
Secondary accession number(s): B3KXN3, B4E2G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.