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Q9BVJ6

- UT14A_HUMAN

UniProt

Q9BVJ6 - UT14A_HUMAN

Protein

U3 small nucleolar RNA-associated protein 14 homolog A

Gene

UTP14A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May be required for ribosome biogenesis.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. rRNA processing Source: InterPro

    Keywords - Biological processi

    Ribosome biogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U3 small nucleolar RNA-associated protein 14 homolog A
    Alternative name(s):
    Antigen NY-CO-16
    Serologically defined colon cancer antigen 16
    Gene namesi
    Name:UTP14A
    Synonyms:SDCCAG16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10665. UTP14A.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell
    2. small-subunit processome Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35595.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 771771U3 small nucleolar RNA-associated protein 14 homolog APRO_0000065733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291Phosphoserine2 Publications
    Modified residuei31 – 311Phosphoserine2 Publications
    Modified residuei52 – 521Phosphoserine2 Publications
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei205 – 2051Phosphothreonine1 Publication
    Modified residuei405 – 4051Phosphoserine2 Publications
    Modified residuei407 – 4071Phosphoserine2 Publications
    Modified residuei433 – 4331CitrullineBy similarity
    Modified residuei437 – 4371Phosphoserine3 Publications
    Modified residuei445 – 4451Phosphoserine4 Publications
    Modified residuei453 – 4531Phosphoserine2 Publications
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei589 – 5891CitrullineBy similarity

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BVJ6.
    PeptideAtlasiQ9BVJ6.
    PRIDEiQ9BVJ6.

    2D gel databases

    SWISS-2DPAGEQ9BVJ6.

    PTM databases

    PhosphoSiteiQ9BVJ6.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9BVJ6.
    BgeeiQ9BVJ6.
    CleanExiHS_UTP14A.
    GenevestigatoriQ9BVJ6.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GADD45GO952573EBI-473284,EBI-448202

    Protein-protein interaction databases

    BioGridi116026. 87 interactions.
    DIPiDIP-32505N.
    IntActiQ9BVJ6. 45 interactions.
    MINTiMINT-1396425.
    STRINGi9606.ENSP00000377944.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BVJ6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili40 – 6728Sequence AnalysisAdd
    BLAST
    Coiled coili216 – 29075Sequence AnalysisAdd
    BLAST
    Coiled coili317 – 34731Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the UTP14 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    HOGENOMiHOG000231396.
    HOVERGENiHBG056550.
    KOiK14567.
    OMAiRTAWDEE.
    OrthoDBiEOG7DZ8K1.
    PhylomeDBiQ9BVJ6.
    TreeFamiTF314531.

    Family and domain databases

    InterProiIPR006709. SSU_processome_Utp14.
    [Graphical view]
    PANTHERiPTHR14150. PTHR14150. 1 hit.
    PfamiPF04615. Utp14. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BVJ6-1) [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

    MTANRLAESL LALSQQEELA DLPKDYLLSE SEDEGDNDGE RKHQKLLEAI    50
    SSLDGKNRRK LAERSEASLK VSEFNVSSEG SGEKLVLADL LEPVKTSSSL 100
    ATVKKQLSRV KSKKTVELPL NKEEIERIHR EVAFNKTAQV LSKWDPVVLK 150
    NRQAEQLVFP LEKEEPAIAP IEHVLSGWKA RTPLEQEIFN LLHKNKQPVT 200
    DPLLTPVEKA SLRAMSLEEA KMRRAELQRA RALQSYYEAK ARREKKIKSK 250
    KYHKVVKKGK AKKALKEFEQ LRKVNPAAAL EELEKIEKAR MMERMSLKHQ 300
    NSGKWAKSKA IMAKYDLEAR QAMQEQLSKN KELTQKLQVA SESEEEEGGT 350
    EDVEELLVPD VVNEVQMNAD GPNPWMLRSC TSDTKEAATQ EDPEQLPELE 400
    AHGVSESEGE ERPVAEEEIL LREFEERRSL RKRSELSQDA EPAGSQETKD 450
    SGSQEVLSEL RVLSQKLKEN HQSRKQKASS EGTIPQVQRE EPAPEEEEPL 500
    LLQRPERVQT LEELEELGKE ECFQNKELPR PVLEGQQSER TPNNRPDAPK 550
    EKKKKEQMID LQNLLTTQSP SVKSLAVPTI EELEDEEERN HRQMIKEAFA 600
    GDDVIRDFLK EKREAVEASK PKDVDLTLPG WGEWGGVGLK PSAKKRRRFL 650
    IKAPEGPPRK DKNLPNVIIN EKRNIHAAAH QVRVLPYPFT HHWQFERTIQ 700
    TPIGSTWNTQ RAFQKLTTPK VVTKPGHIIN PIKAEDVGYR SSSRSDLSVI 750
    QRNPKRITTR HKKQLKKCSV D 771
    Length:771
    Mass (Da):87,978
    Last modified:June 1, 2001 - v1
    Checksum:iDF82C264BA6486FE
    GO
    Isoform 2 (identifier: Q9BVJ6-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:603
    Mass (Da):69,264
    Checksum:iEA095325D8028787
    GO
    Isoform 3 (identifier: Q9BVJ6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-179: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:719
    Mass (Da):82,005
    Checksum:i8555F377424722C1
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti487 – 4871V → A.
    Corresponds to variant rs2281278 [ dbSNP | Ensembl ].
    VAR_022811
    Natural varianti771 – 7711D → G.1 Publication
    Corresponds to variant rs1055032 [ dbSNP | Ensembl ].
    VAR_069181

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1212MTANR…ESLLA → MKGDFRKKKSEA in isoform 2. CuratedVSP_014475Add
    BLAST
    Alternative sequencei13 – 180168Missing in isoform 2. CuratedVSP_014476Add
    BLAST
    Alternative sequencei128 – 17952Missing in isoform 3. 1 PublicationVSP_046389Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14615.1. [Q9BVJ6-1]
    CCDS55489.1. [Q9BVJ6-3]
    RefSeqiNP_001159693.1. NM_001166221.1. [Q9BVJ6-3]
    NP_006640.2. NM_006649.3. [Q9BVJ6-1]
    UniGeneiHs.458598.

    Genome annotation databases

    EnsembliENST00000394422; ENSP00000377944; ENSG00000156697. [Q9BVJ6-1]
    ENST00000425117; ENSP00000388669; ENSG00000156697. [Q9BVJ6-3]
    GeneIDi10813.
    KEGGihsa:10813.
    UCSCiuc004euz.3. human. [Q9BVJ6-1]

    Polymorphism databases

    DMDMi68566226.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14615.1. [Q9BVJ6-1 ]
    CCDS55489.1. [Q9BVJ6-3 ]
    RefSeqi NP_001159693.1. NM_001166221.1. [Q9BVJ6-3 ]
    NP_006640.2. NM_006649.3. [Q9BVJ6-1 ]
    UniGenei Hs.458598.

    3D structure databases

    ProteinModelPortali Q9BVJ6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116026. 87 interactions.
    DIPi DIP-32505N.
    IntActi Q9BVJ6. 45 interactions.
    MINTi MINT-1396425.
    STRINGi 9606.ENSP00000377944.

    PTM databases

    PhosphoSitei Q9BVJ6.

    Polymorphism databases

    DMDMi 68566226.

    2D gel databases

    SWISS-2DPAGE Q9BVJ6.

    Proteomic databases

    MaxQBi Q9BVJ6.
    PeptideAtlasi Q9BVJ6.
    PRIDEi Q9BVJ6.

    Protocols and materials databases

    DNASUi 10813.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394422 ; ENSP00000377944 ; ENSG00000156697 . [Q9BVJ6-1 ]
    ENST00000425117 ; ENSP00000388669 ; ENSG00000156697 . [Q9BVJ6-3 ]
    GeneIDi 10813.
    KEGGi hsa:10813.
    UCSCi uc004euz.3. human. [Q9BVJ6-1 ]

    Organism-specific databases

    CTDi 10813.
    GeneCardsi GC0XP129040.
    HGNCi HGNC:10665. UTP14A.
    MIMi 300508. gene.
    neXtProti NX_Q9BVJ6.
    PharmGKBi PA35595.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000231396.
    HOVERGENi HBG056550.
    KOi K14567.
    OMAi RTAWDEE.
    OrthoDBi EOG7DZ8K1.
    PhylomeDBi Q9BVJ6.
    TreeFami TF314531.

    Miscellaneous databases

    ChiTaRSi UTP14A. human.
    GeneWikii UTP14A.
    GenomeRNAii 10813.
    NextBioi 41075.
    PROi Q9BVJ6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVJ6.
    Bgeei Q9BVJ6.
    CleanExi HS_UTP14A.
    Genevestigatori Q9BVJ6.

    Family and domain databases

    InterProi IPR006709. SSU_processome_Utp14.
    [Graphical view ]
    PANTHERi PTHR14150. PTHR14150. 1 hit.
    Pfami PF04615. Utp14. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 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.
      , 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. 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].

    Entry informationi

    Entry nameiUT14A_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVJ6
    Secondary accession number(s): A8K7A3
    , A8MVQ1, B4DQ08, E9PEL7, Q5JYF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 114 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

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3