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Q9BVJ6

- UT14A_HUMAN

UniProt

Q9BVJ6 - UT14A_HUMAN

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Protein
U3 small nucleolar RNA-associated protein 14 homolog A
Gene
UTP14A, SDCCAG16
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 A
PRO_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 – 4331Citrulline By similarity
Modified residuei437 – 4371Phosphoserine3 Publications
Modified residuei445 – 4451Phosphoserine4 Publications
Modified residuei453 – 4531Phosphoserine2 Publications
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei589 – 5891Citrulline By 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. 44 interactions.
MINTiMINT-1396425.
STRINGi9606.ENSP00000377944.

Structurei

3D structure databases

ProteinModelPortaliQ9BVJ6.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili40 – 6728 Reviewed prediction
Add
BLAST
Coiled coili216 – 29075 Reviewed prediction
Add
BLAST
Coiled coili317 – 34731 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the UTP14 family.

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.
VSP_014475Add
BLAST
Alternative sequencei13 – 180168Missing in isoform 2.
VSP_014476Add
BLAST
Alternative sequencei128 – 17952Missing in isoform 3.
VSP_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

EnsembliENST00000371042; ENSP00000360081; ENSG00000156697. [Q9BVJ6-2]
ENST00000394422; 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. 44 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 ENST00000371042 ; ENSP00000360081 ; ENSG00000156697 . [Q9BVJ6-2 ]
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

« 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 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: September 3, 2014
This is version 113 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