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Q9BVJ6 (UT14A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U3 small nucleolar RNA-associated protein 14 homolog A
Alternative name(s):
Antigen NY-CO-16
Serologically defined colon cancer antigen 16
Gene names
Name:UTP14A
Synonyms:SDCCAG16
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length771 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be required for ribosome biogenesis By similarity.

Subcellular location

Nucleusnucleolus Ref.5.

Tissue specificity

Ubiquitously expressed. Ref.6

Post-translational modification

Citrullinated by PADI4 By similarity.

Miscellaneous

The human genome also contains the UTP14C gene, an autosomal retrotransposed copy of this X-linked gene. Evolution of autosomal retrogenes from X-linked progenitors compensates for X-chromosome silencing during male meiosis.

Sequence similarities

Belongs to the UTP14 family.

Sequence caution

The sequence CAI42909.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processRibosome biogenesis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMCitrullination
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

small-subunit processome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15383276PubMed 21900206. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GADD45GO952573EBI-473284,EBI-448202

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BVJ6-1)

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.
Isoform 2 (identifier: Q9BVJ6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MTANRLAESLLA → MKGDFRKKKSEA
     13-180: Missing.
Note: Gene prediction based on EST data. No experimental confirmation available.
Isoform 3 (identifier: Q9BVJ6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     128-179: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 771771U3 small nucleolar RNA-associated protein 14 homolog A
PRO_0000065733

Regions

Coiled coil40 – 6728 Potential
Coiled coil216 – 29075 Potential
Coiled coil317 – 34731 Potential

Amino acid modifications

Modified residue291Phosphoserine Ref.10 Ref.12
Modified residue311Phosphoserine Ref.10 Ref.12
Modified residue521Phosphoserine Ref.10 Ref.13
Modified residue771Phosphoserine Ref.10
Modified residue2051Phosphothreonine Ref.13
Modified residue4051Phosphoserine Ref.10 Ref.14
Modified residue4071Phosphoserine Ref.10 Ref.14
Modified residue4331Citrulline By similarity
Modified residue4371Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue4451Phosphoserine Ref.7 Ref.10 Ref.13 Ref.14
Modified residue4531Phosphoserine Ref.13 Ref.14
Modified residue5691Phosphoserine Ref.13
Modified residue5891Citrulline By similarity

Natural variations

Alternative sequence1 – 1212MTANR…ESLLA → MKGDFRKKKSEA in isoform 2.
VSP_014475
Alternative sequence13 – 180168Missing in isoform 2.
VSP_014476
Alternative sequence128 – 17952Missing in isoform 3.
VSP_046389
Natural variant4871V → A.
Corresponds to variant rs2281278 [ dbSNP | Ensembl ].
VAR_022811
Natural variant7711D → G. Ref.1
Corresponds to variant rs1055032 [ dbSNP | Ensembl ].
VAR_069181

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: DF82C264BA6486FE

FASTA77187,978
        10         20         30         40         50         60 
MTANRLAESL LALSQQEELA DLPKDYLLSE SEDEGDNDGE RKHQKLLEAI SSLDGKNRRK 

        70         80         90        100        110        120 
LAERSEASLK VSEFNVSSEG SGEKLVLADL LEPVKTSSSL ATVKKQLSRV KSKKTVELPL 

       130        140        150        160        170        180 
NKEEIERIHR EVAFNKTAQV LSKWDPVVLK NRQAEQLVFP LEKEEPAIAP IEHVLSGWKA 

       190        200        210        220        230        240 
RTPLEQEIFN LLHKNKQPVT DPLLTPVEKA SLRAMSLEEA KMRRAELQRA RALQSYYEAK 

       250        260        270        280        290        300 
ARREKKIKSK KYHKVVKKGK AKKALKEFEQ LRKVNPAAAL EELEKIEKAR MMERMSLKHQ 

       310        320        330        340        350        360 
NSGKWAKSKA IMAKYDLEAR QAMQEQLSKN KELTQKLQVA SESEEEEGGT EDVEELLVPD 

       370        380        390        400        410        420 
VVNEVQMNAD GPNPWMLRSC TSDTKEAATQ EDPEQLPELE AHGVSESEGE ERPVAEEEIL 

       430        440        450        460        470        480 
LREFEERRSL RKRSELSQDA EPAGSQETKD SGSQEVLSEL RVLSQKLKEN HQSRKQKASS 

       490        500        510        520        530        540 
EGTIPQVQRE EPAPEEEEPL LLQRPERVQT LEELEELGKE ECFQNKELPR PVLEGQQSER 

       550        560        570        580        590        600 
TPNNRPDAPK EKKKKEQMID LQNLLTTQSP SVKSLAVPTI EELEDEEERN HRQMIKEAFA 

       610        620        630        640        650        660 
GDDVIRDFLK EKREAVEASK PKDVDLTLPG WGEWGGVGLK PSAKKRRRFL IKAPEGPPRK 

       670        680        690        700        710        720 
DKNLPNVIIN EKRNIHAAAH QVRVLPYPFT HHWQFERTIQ TPIGSTWNTQ RAFQKLTTPK 

       730        740        750        760        770 
VVTKPGHIIN PIKAEDVGYR SSSRSDLSVI QRNPKRITTR HKKQLKKCSV D 

« Hide

Isoform 2 [UniParc].

Checksum: EA095325D8028787
Show »

FASTA60369,264
Isoform 3 [UniParc].

Checksum: 8555F377424722C1
Show »

FASTA71982,005

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 3), VARIANT GLY-771.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Cervix, Eye and Muscle.
[5]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"The mouse juvenile spermatogonial depletion (jsd) phenotype is due to a mutation in the X-derived retrogene, mUtp14b."
Rohozinski J., Bishop C.E.
Proc. Natl. Acad. Sci. U.S.A. 101:11695-11700(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"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-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-52; SER-77; SER-405; SER-407 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-29; SER-31 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-52; THR-205; SER-445; SER-453 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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-405; SER-407; SER-437; SER-445 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK291918 mRNA. Translation: BAF84607.1.
AK298578 mRNA. Translation: BAG60770.1.
AL034405 Genomic DNA. Translation: CAI42908.1.
AL034405 Genomic DNA. Translation: CAI42909.1. Sequence problems.
CH471107 Genomic DNA. Translation: EAX11820.1.
BC001149 mRNA. Translation: AAH01149.1.
BC009649 mRNA. Translation: AAH09649.1.
BC014987 mRNA. Translation: AAH14987.1.
CCDSCCDS14615.1. [Q9BVJ6-1]
CCDS55489.1. [Q9BVJ6-3]
RefSeqNP_001159693.1. NM_001166221.1. [Q9BVJ6-3]
NP_006640.2. NM_006649.3. [Q9BVJ6-1]
UniGeneHs.458598.

3D structure databases

ProteinModelPortalQ9BVJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116026. 86 interactions.
DIPDIP-32505N.
IntActQ9BVJ6. 44 interactions.
MINTMINT-1396425.
STRING9606.ENSP00000377944.

PTM databases

PhosphoSiteQ9BVJ6.

Polymorphism databases

DMDM68566226.

2D gel databases

SWISS-2DPAGEQ9BVJ6.

Proteomic databases

MaxQBQ9BVJ6.
PeptideAtlasQ9BVJ6.
PRIDEQ9BVJ6.

Protocols and materials databases

DNASU10813.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371042; ENSP00000360081; ENSG00000156697. [Q9BVJ6-2]
ENST00000394422; ENSP00000377944; ENSG00000156697. [Q9BVJ6-1]
ENST00000425117; ENSP00000388669; ENSG00000156697. [Q9BVJ6-3]
GeneID10813.
KEGGhsa:10813.
UCSCuc004euz.3. human. [Q9BVJ6-1]

Organism-specific databases

CTD10813.
GeneCardsGC0XP129040.
HGNCHGNC:10665. UTP14A.
MIM300508. gene.
neXtProtNX_Q9BVJ6.
PharmGKBPA35595.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000231396.
HOVERGENHBG056550.
KOK14567.
OMARTAWDEE.
OrthoDBEOG7DZ8K1.
PhylomeDBQ9BVJ6.
TreeFamTF314531.

Gene expression databases

ArrayExpressQ9BVJ6.
BgeeQ9BVJ6.
CleanExHS_UTP14A.
GenevestigatorQ9BVJ6.

Family and domain databases

InterProIPR006709. SSU_processome_Utp14.
[Graphical view]
PANTHERPTHR14150. PTHR14150. 1 hit.
PfamPF04615. Utp14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUTP14A. human.
GeneWikiUTP14A.
GenomeRNAi10813.
NextBio41075.
PROQ9BVJ6.
SOURCESearch...

Entry information

Entry nameUT14A_HUMAN
AccessionPrimary (citable) accession number: Q9BVJ6
Secondary accession number(s): A8K7A3 expand/collapse secondary AC list , A8MVQ1, B4DQ08, E9PEL7, Q5JYF1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM