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Q9NV58

- RN19A_HUMAN

UniProt

Q9NV58 - RN19A_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF19A

Gene

RNF19A

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

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection.5 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 17948RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 26466IBR-typeAdd
BLAST
Zinc fingeri301 – 33232RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. transcription factor binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. microtubule cytoskeleton organization Source: UniProtKB
  2. protein ubiquitination Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF19A (EC:6.3.2.-)
Alternative name(s):
Double ring-finger protein
Short name:
Dorfin
RING finger protein 19A
p38
Gene namesi
Name:RNF19A
Synonyms:RNF19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:13432. RNF19A.

Subcellular locationi

Membrane Curated; Multi-pass membrane protein Curated. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 4 Publications
Note: Present in the hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parkinson disease patients.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321C → S: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-135. 1 Publication
Mutagenesisi135 – 1351C → S: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-132. 1 Publication

Organism-specific databases

PharmGKBiPA162401601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838E3 ubiquitin-protein ligase RNF19APRO_0000056061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei631 – 6311Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NV58.
PaxDbiQ9NV58.
PRIDEiQ9NV58.

PTM databases

PhosphoSiteiQ9NV58.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart. Ubiquitously expressed in the central nervous system.1 Publication

Gene expression databases

BgeeiQ9NV58.
CleanExiHS_RNF19A.
ExpressionAtlasiQ9NV58. baseline and differential.
GenevestigatoriQ9NV58.

Organism-specific databases

HPAiCAB011455.
HPA023652.

Interactioni

Subunit structurei

Interacts with UBE2L3 and UBE2L6. Interacts with transcription factor Sp1. Interacts with VCP, CASR, SNCAIP and with some SOD1 variants which cause amyotrophic lateral sclerosis, but not with wild-type SOD1.6 Publications

Protein-protein interaction databases

BioGridi117405. 15 interactions.
IntActiQ9NV58. 7 interactions.
STRINGi9606.ENSP00000342667.

Structurei

3D structure databases

ProteinModelPortaliQ9NV58.
SMRiQ9NV58. Positions 130-362.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST
Transmembranei424 – 44421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni660 – 838179Interaction with CASRAdd
BLAST

Sequence similaritiesi

Belongs to the RBR family. RNF19 subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 17948RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 26466IBR-typeAdd
BLAST
Zinc fingeri301 – 33232RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG245345.
GeneTreeiENSGT00750000117406.
HOVERGENiHBG052073.
InParanoidiQ9NV58.
KOiK11972.
OMAiSNMKINE.
OrthoDBiEOG7JDQXT.
PhylomeDBiQ9NV58.
TreeFamiTF324777.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR002867. Znf_C6HC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NV58-1) [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
MQEQEIGFIS KYNEGLCVNT DPVSILTSIL DMSLHRQMGS DRDLQSSASS
60 70 80 90 100
VSLPSVKKAP KKRRISIGSL FRRKKDNKRK SRELNGGVDG IASIESIHSE
110 120 130 140 150
MCTDKNSIFS TNTSSDNGLT SISKQIGDFI ECPLCLLRHS KDRFPDIMTC
160 170 180 190 200
HHRSCVDCLR QYLRIEISES RVNISCPECT ERFNPHDIRL ILSDDVLMEK
210 220 230 240 250
YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT CGREGCGTEF
260 270 280 290 300
CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
310 320 330 340 350
CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW
360 370 380 390 400
GKKPWSRKKK ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN
410 420 430 440 450
RYEGKDVSKH KRNLAIAGGV TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV
460 470 480 490 500
PISLCRSGGC GVSAGNGKGV RIEFDDENDI NVGGTNTAVD TTSVAEARHN
510 520 530 540 550
PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA LAGASITGSL
560 570 580 590 600
SGSAMVNCFN RLEVQADVQK ERYSLSGESG TVSLGTVSDN ASTKAMAGSI
610 620 630 640 650
LNSYIPLDKE GNSMEVQVDI ESKPSKFRHN SGSSSVDDGS ATRSHAGGSS
660 670 680 690 700
SGLPEGKSSA TKWSKEATAG KKSKSGKLRK KGNMKINETR EDMDAQLLEQ
710 720 730 740 750
QSTNSSEFEA PSLSDSMPSV ADSHSSHFSE FSCSDLESMK TSCSHGSSDY
760 770 780 790 800
HTRFATVNIL PEVENDRLEN SPHQCSISVV TQTASCSEVS QLNHIAEEHG
810 820 830
NNGIKPNVDL YFGDALKETN NNHSHQTMEL KVAIQTEI
Length:838
Mass (Da):90,696
Last modified:October 17, 2006 - v3
Checksum:i00A7DED5023FDC06
GO
Isoform 2 (identifier: Q9NV58-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     572-604: RYSLSGESGTVSLGTVSDNASTKAMAGSILNSY → AAVAAAGRWAYSPATLRCRRSEELKNIHDSS
     605-838: Missing.

Note: No experimental confirmation available.

Show »
Length:602
Mass (Da):65,416
Checksum:i0B210220B7C0F623
GO
Isoform 3 (identifier: Q9NV58-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Show »
Length:807
Mass (Da):87,256
Checksum:iF50D47C3EA851842
GO

Sequence cautioni

The sequence BAB14581.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB15647.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti645 – 6451H → Y in BAB39353. (PubMed:11237715)Curated
Sequence conflicti744 – 7441S → R in CAB53700. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti835 – 8351Q → H.
Corresponds to variant rs9642785 [ dbSNP | Ensembl ].
VAR_028045

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 3. 1 PublicationVSP_028631Add
BLAST
Alternative sequencei572 – 60433RYSLS…ILNSY → AAVAAAGRWAYSPATLRCRR SEELKNIHDSS in isoform 2. 1 PublicationVSP_021010Add
BLAST
Alternative sequencei605 – 838234Missing in isoform 2. 1 PublicationVSP_021011Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029316 mRNA. Translation: BAB39353.1.
BC093938 mRNA. Translation: AAH93938.1.
BC093940 mRNA. Translation: AAH93940.1.
AB271914 mRNA. Translation: BAF48117.1.
AK001774 mRNA. Translation: BAA91900.1.
AK023455 mRNA. Translation: BAB14581.1. Different initiation.
AK027070 mRNA. Translation: BAB15647.1. Different initiation.
AJ242975 mRNA. Translation: CAB45132.1.
AL110253 mRNA. Translation: CAB53700.1.
AL122096 mRNA. Translation: CAB59264.1.
CCDSiCCDS6286.1. [Q9NV58-1]
PIRiT34528.
RefSeqiNP_001267468.1. NM_001280539.1. [Q9NV58-1]
NP_056250.3. NM_015435.4. [Q9NV58-1]
NP_904355.1. NM_183419.3. [Q9NV58-1]
XP_005250910.1. XM_005250853.1. [Q9NV58-1]
UniGeneiHs.292882.

Genome annotation databases

EnsembliENST00000341084; ENSP00000342667; ENSG00000034677. [Q9NV58-1]
ENST00000517584; ENSP00000429161; ENSG00000034677.
ENST00000519449; ENSP00000428968; ENSG00000034677. [Q9NV58-1]
ENST00000616528; ENSP00000480369; ENSG00000034677. [Q9NV58-1]
GeneIDi25897.
KEGGihsa:25897.
UCSCiuc003yjj.1. human. [Q9NV58-1]

Polymorphism databases

DMDMi116242764.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029316 mRNA. Translation: BAB39353.1 .
BC093938 mRNA. Translation: AAH93938.1 .
BC093940 mRNA. Translation: AAH93940.1 .
AB271914 mRNA. Translation: BAF48117.1 .
AK001774 mRNA. Translation: BAA91900.1 .
AK023455 mRNA. Translation: BAB14581.1 . Different initiation.
AK027070 mRNA. Translation: BAB15647.1 . Different initiation.
AJ242975 mRNA. Translation: CAB45132.1 .
AL110253 mRNA. Translation: CAB53700.1 .
AL122096 mRNA. Translation: CAB59264.1 .
CCDSi CCDS6286.1. [Q9NV58-1 ]
PIRi T34528.
RefSeqi NP_001267468.1. NM_001280539.1. [Q9NV58-1 ]
NP_056250.3. NM_015435.4. [Q9NV58-1 ]
NP_904355.1. NM_183419.3. [Q9NV58-1 ]
XP_005250910.1. XM_005250853.1. [Q9NV58-1 ]
UniGenei Hs.292882.

3D structure databases

ProteinModelPortali Q9NV58.
SMRi Q9NV58. Positions 130-362.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117405. 15 interactions.
IntActi Q9NV58. 7 interactions.
STRINGi 9606.ENSP00000342667.

PTM databases

PhosphoSitei Q9NV58.

Polymorphism databases

DMDMi 116242764.

Proteomic databases

MaxQBi Q9NV58.
PaxDbi Q9NV58.
PRIDEi Q9NV58.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341084 ; ENSP00000342667 ; ENSG00000034677 . [Q9NV58-1 ]
ENST00000517584 ; ENSP00000429161 ; ENSG00000034677 .
ENST00000519449 ; ENSP00000428968 ; ENSG00000034677 . [Q9NV58-1 ]
ENST00000616528 ; ENSP00000480369 ; ENSG00000034677 . [Q9NV58-1 ]
GeneIDi 25897.
KEGGi hsa:25897.
UCSCi uc003yjj.1. human. [Q9NV58-1 ]

Organism-specific databases

CTDi 25897.
GeneCardsi GC08M101269.
HGNCi HGNC:13432. RNF19A.
HPAi CAB011455.
HPA023652.
MIMi 607119. gene.
neXtProti NX_Q9NV58.
PharmGKBi PA162401601.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245345.
GeneTreei ENSGT00750000117406.
HOVERGENi HBG052073.
InParanoidi Q9NV58.
KOi K11972.
OMAi SNMKINE.
OrthoDBi EOG7JDQXT.
PhylomeDBi Q9NV58.
TreeFami TF324777.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi RNF19A. human.
GeneWikii RNF19A.
GenomeRNAii 25897.
NextBioi 47345.
PROi Q9NV58.
SOURCEi Search...

Gene expression databases

Bgeei Q9NV58.
CleanExi HS_RNF19A.
ExpressionAtlasi Q9NV58. baseline and differential.
Genevestigatori Q9NV58.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR002867. Znf_C6HC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01485. IBR. 2 hits.
[Graphical view ]
SMARTi SM00647. IBR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."
    Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.
    Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH UBE2L3 AND UBE2L6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Spinal cord.
  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] (ISOFORM 1).
    Tissue: Brain.
  3. "Expression and promoter activity of MaLR element of Dorfin gene related to Parkinson disease."
    Kim T., Huh J., Kim H.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-89 (ISOFORM 3).
  4. "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] OF 426-838 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-838 (ISOFORM 2).
    Tissue: Hepatoma, Ovarian carcinoma and Placenta.
  5. "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
    Gunther M., Laithier M., Brison O.
    Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 422-824 (ISOFORM 1), INTERACTION WITH SP1.
    Tissue: Colon.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 524-838 (ISOFORM 1).
    Tissue: Fetal kidney and Testis.
  7. "Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity."
    Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S., Tanaka K., Taniguchi N., Sobue G.
    J. Biol. Chem. 277:36793-36798(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOD1.
  8. "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1."
    Ito T., Niwa J., Hishikawa N., Ishigaki S., Doyu M., Sobue G.
    J. Biol. Chem. 278:29106-29114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNCAIP.
  9. "Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders."
    Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S., Kakizuka A., Tanaka K., Sobue G.
    J. Biol. Chem. 279:51376-51385(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VCP, MUTAGENESIS OF CYS-132 AND CYS-135, SUBCELLULAR LOCATION.
  10. "Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin."
    Huang Y., Niwa J., Sobue G., Breitwieser G.E.
    J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CASR AND VCP.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN19A_HUMAN
AccessioniPrimary (citable) accession number: Q9NV58
Secondary accession number(s): A3KCU9
, Q52LG1, Q9H5H9, Q9H8M8, Q9UFG0, Q9UFX6, Q9Y4Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 133 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3