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P29374

- ARI4A_HUMAN

UniProt

P29374 - ARI4A_HUMAN

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Protein

AT-rich interactive domain-containing protein 4A

Gene

ARID4A

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

Functioni

Interacts with the viral protein-binding domain of the retinoblastoma protein.

GO - Molecular functioni

  1. DNA binding Source: GDB
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. erythrocyte development Source: Ensembl
  2. histone H3-K4 trimethylation Source: Ensembl
  3. histone H3-K9 trimethylation Source: Ensembl
  4. histone H4-K20 trimethylation Source: Ensembl
  5. negative regulation of transcription, DNA-templated Source: GDB
  6. regulation of gene expression by genetic imprinting Source: Ensembl
  7. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_228222. HDACs deacetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
AT-rich interactive domain-containing protein 4A
Short name:
ARID domain-containing protein 4A
Alternative name(s):
Retinoblastoma-binding protein 1
Short name:
RBBP-1
Gene namesi
Name:ARID4A
Synonyms:RBBP1, RBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9885. ARID4A.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: GDB
  2. transcriptional repressor complex Source: GDB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34249.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12571257AT-rich interactive domain-containing protein 4APRO_0000200580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei538 – 5381Phosphoserine1 Publication
Modified residuei542 – 5421Phosphoserine1 Publication
Modified residuei676 – 6761Phosphoserine1 Publication
Modified residuei1109 – 11091Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29374.
PaxDbiP29374.
PRIDEiP29374.

PTM databases

PhosphoSiteiP29374.

Expressioni

Gene expression databases

BgeeiP29374.
CleanExiHS_ARID4A.
HS_RBP1.
ExpressionAtlasiP29374. baseline and differential.
GenevestigatoriP29374.

Organism-specific databases

HPAiHPA048899.

Interactioni

Subunit structurei

Interacts with BRMS1. Identified in mSin3A corepressor complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2.1 Publication

Protein-protein interaction databases

BioGridi111861. 25 interactions.
DIPiDIP-463N.
IntActiP29374. 4 interactions.
MINTiMINT-150005.
STRINGi9606.ENSP00000347602.

Structurei

Secondary structure

1
1257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi15 – 206Combined sources
Beta strandi23 – 4220Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 525Combined sources
Turni53 – 553Combined sources
Beta strandi56 – 583Combined sources
Beta strandi65 – 695Combined sources
Beta strandi75 – 9319Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 1053Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi221 – 2244Combined sources
Turni226 – 2283Combined sources
Helixi239 – 2446Combined sources
Helixi246 – 25611Combined sources
Turni262 – 2643Combined sources
Helixi269 – 2724Combined sources
Beta strandi578 – 5858Combined sources
Beta strandi588 – 60215Combined sources
Beta strandi605 – 6128Combined sources
Beta strandi621 – 6244Combined sources
Helixi625 – 6273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LCCNMR-A568-635[»]
2MAMNMR-A4-121[»]
2YRVNMR-A170-273[»]
ProteinModelPortaliP29374.
SMRiP29374. Positions 4-121, 170-277, 306-397, 568-635.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini309 – 40193ARIDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni951 – 96414Retinoblastoma protein bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 ARID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG248805.
GeneTreeiENSGT00510000046413.
HOGENOMiHOG000015398.
HOVERGENiHBG058247.
InParanoidiP29374.
OMAiISPSCND.
OrthoDBiEOG7PVWNP.
PhylomeDBiP29374.
TreeFamiTF106427.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID/BRIGHT_DNA-bd.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform I (identifier: P29374-1) [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
MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL
60 70 80 90 100
VQDDQVKGPL RVGAIVETRT SDGSFQEAII SKLTDASWYT VVFDDGDERT
110 120 130 140 150
LRRTSLCLKG ERHFAESETL DQLPLTNPEH FGTPVIAKKT NRGRRSSLPV
160 170 180 190 200
TEDEKEEESS EEEDEDKRRL NDELLGKVVS VVSATERTEW YPALVISPSC
210 220 230 240 250
NDDITVKKDQ CLVRSFIDSK FYSIARKDIK EVDILNLPES ELSTKPGLQK
260 270 280 290 300
ASIFLKTRVV PDNWKMDISE ILESSSSDDE DGPAEENDEE KEKEAKKTEE
310 320 330 340 350
EVPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV
360 370 380 390 400
YHQGGCDNID SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC
410 420 430 440 450
RSANIQFRTV HHHEPKVKEE KKDLEESMEE ALKLDQEMPL TEVKSEPEEN
460 470 480 490 500
IDSNSESERE EIELKSPRGR RRIARDVNSI KKEIEEEKTE DKLKDNDTEN
510 520 530 540 550
KDVDDDYETA EKKENELLLG RKNTPKQKEK KIKKQEDSDK DSDEEEEKSQ
560 570 580 590 600
EREETESKCD SEGEEDEEDM EPCLTGTKVK VKYGRGKTQK IYEASIKSTE
610 620 630 640 650
IDDGEVLYLV HYYGWNVRYD EWVKADRIIW PLDKGGPKKK QKKKAKNKED
660 670 680 690 700
SEKDEKRDEE RQKSKRGRPP LKSTLSSNMP YGLSKTANSE GKSDSCSSDS
710 720 730 740 750
ETEDALEKNL INEELSLKDE LEKNENLNDD KLDEENPKIS AHILKENDRT
760 770 780 790 800
QMQPLETLKL EVGENEQIVQ IFGNKMEKTE EVKKEAEKSP KGKGRRSKTK
810 820 830 840 850
DLSLEIIKIS SFGQNEAGSE PHIEAHSLEL SSLDNKNFSS ATEDEIDQCV
860 870 880 890 900
KEKKLKRKIL GQSSPEKKIR IENGMEMTNT VSQERTSDCI GSEGMKNLNF
910 920 930 940 950
EQHFERENEG MPSLIAESNQ CIQQLTSERF DSPAEETVNI PLKEDEDAMP
960 970 980 990 1000
LIGPETLVCH EVDLDDLDEK DKTSIEDVAV ESSESNSLVS IPPALPPVVQ
1010 1020 1030 1040 1050
HNFSVASPLT LSQDESRSVK SESDITIEVD SIAEESQEGL CERESANGFE
1060 1070 1080 1090 1100
TNVASGTCSI IVQERESREK GQKRPSDGNS GLMAKKQKRT PKRTSAAAKN
1110 1120 1130 1140 1150
EKNGTGQSSD SEDLPVLDNS SKCTPVKHLN VSKPQKLARS PARISPHIKD
1160 1170 1180 1190 1200
GEKDKHREKH PNSSPRTYKW SFQLNELDNM NSTERISFLQ EKLQEIRKYY
1210 1220 1230 1240 1250
MSLKSEVATI DRRRKRLKKK DREVSHAGAS MSSASSDTGM SPSSSSPPQN

VLAVECR
Length:1,257
Mass (Da):142,752
Last modified:September 23, 2008 - v3
Checksum:i5B3F6A5AFB7588CF
GO
Isoform II (identifier: P29374-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1121-1174: Missing.

Show »
Length:1,203
Mass (Da):136,495
Checksum:iB2A06AA7071AAAE2
GO
Isoform III (identifier: P29374-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1106-1174: Missing.
     1175-1175: N → D

Show »
Length:1,188
Mass (Da):134,951
Checksum:i0576FA849F761B54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851V → L in AAB28543. (PubMed:8414517)Curated
Sequence conflicti618 – 6181R → S in AAB28543. (PubMed:8414517)Curated
Sequence conflicti653 – 6531K → V in AAB25833. (PubMed:8455946)Curated
Sequence conflicti653 – 6531K → V in AAB25834. (PubMed:8455946)Curated
Sequence conflicti653 – 6531K → V in AAB25835. (PubMed:8455946)Curated
Sequence conflicti1178 – 11781D → S no nucleotide entry (PubMed:1857421)Curated
Sequence conflicti1196 – 12016IRKYYM → SENIICL no nucleotide entry (PubMed:1857421)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti412 – 4121H → P.
Corresponds to variant rs34982206 [ dbSNP | Ensembl ].
VAR_031566
Natural varianti724 – 7241N → S.
Corresponds to variant rs2230098 [ dbSNP | Ensembl ].
VAR_031567
Natural varianti779 – 7791T → A.1 Publication
Corresponds to variant rs1051858 [ dbSNP | Ensembl ].
VAR_031568

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1106 – 117469Missing in isoform III. 1 PublicationVSP_004371Add
BLAST
Alternative sequencei1121 – 117454Missing in isoform II. 1 PublicationVSP_004373Add
BLAST
Alternative sequencei1175 – 11751N → D in isoform III. 1 PublicationVSP_004372

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66427 mRNA. Translation: AAB28543.1.
AL132989 Genomic DNA. No translation available.
AL139021 Genomic DNA. No translation available.
S57153 mRNA. Translation: AAB25833.1.
S57160 mRNA. Translation: AAB25834.1.
S57162 mRNA. Translation: AAB25835.2.
CCDSiCCDS45114.1. [P29374-2]
CCDS9732.1. [P29374-1]
CCDS9733.1. [P29374-3]
PIRiI58383.
RefSeqiNP_002883.3. NM_002892.3. [P29374-1]
NP_075376.2. NM_023000.2. [P29374-2]
NP_075377.2. NM_023001.2. [P29374-3]
UniGeneiHs.161000.

Genome annotation databases

EnsembliENST00000348476; ENSP00000344556; ENSG00000032219. [P29374-3]
ENST00000355431; ENSP00000347602; ENSG00000032219. [P29374-1]
ENST00000395168; ENSP00000378597; ENSG00000032219. [P29374-2]
ENST00000431317; ENSP00000397368; ENSG00000032219. [P29374-3]
GeneIDi5926.
KEGGihsa:5926.
UCSCiuc001xdo.3. human. [P29374-2]
uc001xdp.3. human. [P29374-1]
uc001xdq.3. human. [P29374-3]

Polymorphism databases

DMDMi206729929.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66427 mRNA. Translation: AAB28543.1 .
AL132989 Genomic DNA. No translation available.
AL139021 Genomic DNA. No translation available.
S57153 mRNA. Translation: AAB25833.1 .
S57160 mRNA. Translation: AAB25834.1 .
S57162 mRNA. Translation: AAB25835.2 .
CCDSi CCDS45114.1. [P29374-2 ]
CCDS9732.1. [P29374-1 ]
CCDS9733.1. [P29374-3 ]
PIRi I58383.
RefSeqi NP_002883.3. NM_002892.3. [P29374-1 ]
NP_075376.2. NM_023000.2. [P29374-2 ]
NP_075377.2. NM_023001.2. [P29374-3 ]
UniGenei Hs.161000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LCC NMR - A 568-635 [» ]
2MAM NMR - A 4-121 [» ]
2YRV NMR - A 170-273 [» ]
ProteinModelPortali P29374.
SMRi P29374. Positions 4-121, 170-277, 306-397, 568-635.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111861. 25 interactions.
DIPi DIP-463N.
IntActi P29374. 4 interactions.
MINTi MINT-150005.
STRINGi 9606.ENSP00000347602.

PTM databases

PhosphoSitei P29374.

Polymorphism databases

DMDMi 206729929.

Proteomic databases

MaxQBi P29374.
PaxDbi P29374.
PRIDEi P29374.

Protocols and materials databases

DNASUi 5926.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000348476 ; ENSP00000344556 ; ENSG00000032219 . [P29374-3 ]
ENST00000355431 ; ENSP00000347602 ; ENSG00000032219 . [P29374-1 ]
ENST00000395168 ; ENSP00000378597 ; ENSG00000032219 . [P29374-2 ]
ENST00000431317 ; ENSP00000397368 ; ENSG00000032219 . [P29374-3 ]
GeneIDi 5926.
KEGGi hsa:5926.
UCSCi uc001xdo.3. human. [P29374-2 ]
uc001xdp.3. human. [P29374-1 ]
uc001xdq.3. human. [P29374-3 ]

Organism-specific databases

CTDi 5926.
GeneCardsi GC14P058766.
H-InvDB HIX0037655.
HGNCi HGNC:9885. ARID4A.
HPAi HPA048899.
MIMi 180201. gene.
neXtProti NX_P29374.
PharmGKBi PA34249.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248805.
GeneTreei ENSGT00510000046413.
HOGENOMi HOG000015398.
HOVERGENi HBG058247.
InParanoidi P29374.
OMAi ISPSCND.
OrthoDBi EOG7PVWNP.
PhylomeDBi P29374.
TreeFami TF106427.

Enzyme and pathway databases

Reactomei REACT_228222. HDACs deacetylate histones.

Miscellaneous databases

ChiTaRSi ARID4A. human.
EvolutionaryTracei P29374.
GeneWikii ARID4A.
GenomeRNAii 5926.
NextBioi 23080.
PROi P29374.
SOURCEi Search...

Gene expression databases

Bgeei P29374.
CleanExi HS_ARID4A.
HS_RBP1.
ExpressionAtlasi P29374. baseline and differential.
Genevestigatori P29374.

Family and domain databases

Gene3Di 1.10.150.60. 1 hit.
InterProi IPR001606. ARID/BRIGHT_DNA-bd.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view ]
SUPFAMi SSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEi PS51011. ARID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
    Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
    Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), VARIANT ALA-779.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites."
    Otterson G.A., Kratzke R.A., Lin A.Y., Johnston P.G., Kaye F.J.
    Oncogene 8:949-957(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 338-1257 (ISOFORMS I; II AND III), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
  4. "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product."
    Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A., Hanobik M.G., Huber H.E., Oliff A.
    Nature 352:251-254(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 855-1203 (ISOFORM I).
  5. "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription."
    Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A., Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.
    J. Biol. Chem. 279:1562-1569(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; BRMS1; RBBP4 AND RBBP7.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-676 AND SER-1109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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-538 AND SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution structure of the RBB1NT domain of human RB(Retinoblastoma)-binding protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 170-277.

Entry informationi

Entry nameiARI4A_HUMAN
AccessioniPrimary (citable) accession number: P29374
Secondary accession number(s): Q15991, Q15992, Q15993
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 23, 2008
Last modified: November 26, 2014
This is version 134 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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