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Q4LE39 (ARI4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
AT-rich interactive domain-containing protein 4B

Short name=ARID domain-containing protein 4B
Alternative name(s):
180 kDa Sin3-associated polypeptide
Short name=Sin3-associated polypeptide p180
Breast cancer-associated antigen BRCAA1
Histone deacetylase complex subunit SAP180
Retinoblastoma-binding protein 1-like 1
Gene names
Name:ARID4B
Synonyms:BRCAA1, RBBP1L1, RBP1L1, SAP180
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. Ref.2

Subunit structure

Component of a Sin3A corepressor complex consisting of SIN3A, SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2. Ref.2

Subcellular location

Nucleus By similarity. Cytoplasm. Note: Cytoplasmic in breast cancer cells. Ref.1 Ref.3

Tissue specificity

Highly expressed in the testis and in breast, lung, colon, pancreatic and ovarian cancers. Expressed at low levels in the thymus, prostate and ovary. Ref.1 Ref.2 Ref.3

Domain

The C-terminus mediates interaction with mSin3A corepressor complex. Ref.2

The N-terminus is involved in transcriptional repression by HDAC-independent mechanisms. Ref.2

The ARID domain is involved in stabilizing the mSin3A corepressor complex on DNA. Ref.2

Sequence similarities

Contains 1 ARID domain.

Sequence caution

The sequence AAD41239.1 differs from that shown. Reason: Frameshift at positions 859, 869, 1287 and 1311.

The sequence AAF23433.3 differs from that shown. Reason: Frameshift at positions 1287 and 1311.

The sequence BAB14428.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE06114.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI13751.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ETS1P149212EBI-2680990,EBI-913209

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q4LE39-1)

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: Q4LE39-2)

The sequence of this isoform differs from the canonical sequence as follows:
     529-614: Missing.
Isoform 3 (identifier: Q4LE39-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1150-1153: TNSS → SAPH
     1154-1312: Missing.
Isoform 4 (identifier: Q4LE39-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-319: Missing.
     1112-1122: ACTGQKRVKDA → GEKENVYVDLF
     1123-1312: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13121312AT-rich interactive domain-containing protein 4B
PRO_0000282863

Regions

Domain306 – 39893ARID
Region465 – 4739Antigenic epitope
Region1130 – 11378Antigenic epitope
Coiled coil728 – 75427 Potential
Coiled coil1231 – 127040 Potential
Compositional bias154 – 1596Poly-Ser
Compositional bias268 – 567300Glu-rich
Compositional bias1095 – 11017Poly-Ser
Compositional bias1271 – 130333Ser-rich

Amino acid modifications

Modified residue2761Phosphoserine Ref.18
Modified residue6661Phosphoserine Ref.13
Modified residue6751Phosphoserine Ref.13 Ref.16
Modified residue7171Phosphoserine Ref.12
Modified residue7781Phosphoserine Ref.16 Ref.18
Modified residue7901Phosphoserine Ref.13 Ref.15 Ref.16 Ref.18
Modified residue7931Phosphothreonine Ref.13 Ref.15 Ref.16 Ref.18
Modified residue10141Phosphoserine Ref.15
Modified residue10261Phosphothreonine Ref.15
Modified residue11501Phosphothreonine Ref.13
Modified residue11521Phosphoserine Ref.13
Modified residue11531Phosphoserine Ref.13
Modified residue11551Phosphoserine Ref.13
Modified residue11591Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 319319Missing in isoform 4.
VSP_024230
Alternative sequence529 – 61486Missing in isoform 2.
VSP_024231
Alternative sequence1112 – 112211ACTGQKRVKDA → GEKENVYVDLF in isoform 4.
VSP_024232
Alternative sequence1123 – 1312190Missing in isoform 4.
VSP_024233
Alternative sequence1150 – 11534TNSS → SAPH in isoform 3.
VSP_024234
Alternative sequence1154 – 1312159Missing in isoform 3.
VSP_024235

Experimental info

Sequence conflict151D → G in AAO63590. Ref.2
Sequence conflict791V → A in AAO63590. Ref.2
Sequence conflict3301R → Q in AAF28341. Ref.1
Sequence conflict3301R → Q in AAF23433. Ref.3
Sequence conflict4001A → P in BAA89794. Ref.4
Sequence conflict4361I → IEFCGR in AAF23433. Ref.3
Sequence conflict4371K → Q in BAA89794. Ref.4
Sequence conflict559 – 5613DNN → ATI in BAA89794. Ref.4
Sequence conflict5681C → S in BAA89794. Ref.4
Sequence conflict5751V → A in BAA89794. Ref.4
Sequence conflict5841N → H in BAA89794. Ref.4
Sequence conflict6051L → S in AAF36964. Ref.9
Sequence conflict6161D → G in AAF36964. Ref.9
Sequence conflict8131D → G in AAO63590. Ref.2
Sequence conflict915 – 9173RLQ → LP in AAF23433. Ref.3
Sequence conflict9401L → R in AAF23433. Ref.3
Sequence conflict10001K → E in AAF28341. Ref.1
Sequence conflict10001K → E in AAF36964. Ref.9
Sequence conflict10011T → Q in AAF23433. Ref.3
Sequence conflict10321S → P in AAO63590. Ref.2
Sequence conflict10871S → N in AAO63590. Ref.2
Sequence conflict11181R → G in CAI46047. Ref.8
Sequence conflict11441K → T in AAF23433. Ref.3
Sequence conflict11441K → T in AAD41239. Ref.10
Sequence conflict1243 – 12442IR → NQ in AAF23433. Ref.3
Sequence conflict1243 – 12442IR → NQ in AAD41239. Ref.10
Sequence conflict12901V → A in AAF28341. Ref.1
Sequence conflict12901V → A in AAF36964. Ref.9

Sequences

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

Last modified April 3, 2007. Version 2.
Checksum: E4175FF80F5217EE

FASTA1,312147,809
        10         20         30         40         50         60 
MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL 

        70         80         90        100        110        120 
KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL 

       130        140        150        160        170        180 
DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD EDEDDRKQID ELLGKVVCVD 

       190        200        210        220        230        240 
YISLDKKKAL WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK 

       250        260        270        280        290        300 
PDAVLKQAFE QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE 

       310        320        330        340        350        360 
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA 

       370        380        390        400        410        420 
VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIEFQMALPE KVVNKQCKEC 

       430        440        450        460        470        480 
ENVKEIKVKE ENETEIKEIK MEEERNIIPR EEKPIEDEIE RKENIKPSLG SKKNLLESIP 

       490        500        510        520        530        540 
THSDQEKEVN IKKPEDNENL DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE 

       550        560        570        580        590        600 
EAEEEEEEEE EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG 

       610        620        630        640        650        660 
EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD KDEKYSPKNC 

       670        680        690        700        710        720 
KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI TSILNGLQAS ESSAEDSEQE 

       730        740        750        760        770        780 
DERGAQDMDN NGKEESKIDH LTNNRNDLIS KEEQNSSSLL EENKVHADLV ISKPVSKSPE 

       790        800        810        820        830        840 
RLRKDIEVLS EDTDYEEDEV TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG 

       850        860        870        880        890        900 
KKEEKAKNKE SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE 

       910        920        930        940        950        960 
VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE AAASPPHPAP 

       970        980        990       1000       1010       1020 
EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK TVEVNDRKAE FPSSGSNSVL 

      1030       1040       1050       1060       1070       1080 
NTPPTTPESP SSVTVTEGSR QQSSVTVSEP LAPNQEEVRS IKSETDSTIE VDSVAGELQD 

      1090       1100       1110       1120       1130       1140 
LQSEGNSSPA GFDASVSSSS SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV 

      1150       1160       1170       1180       1190       1200 
VNNKKKGKGT NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK 

      1210       1220       1230       1240       1250       1260 
DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL KSEVASIDRR 

      1270       1280       1290       1300       1310 
RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS SASQNGMSVE CR 

« Hide

Isoform 2 [UniParc].

Checksum: 3ADAB4A897403AD9
Show »

FASTA1,226137,607
Isoform 3 [UniParc].

Checksum: 9C540DF507EBC220
Show »

FASTA1,153130,418
Isoform 4 [UniParc].

Checksum: AC58481D8DE15417
Show »

FASTA80391,140

References

« Hide 'large scale' references
[1]"RBP1L1, a retinoblastoma-binding protein-related gene encoding an antigenic epitope abundantly expressed in human carcinomas and normal testis."
Cao J.-N., Gao T.-W., Stanbridge E.J., Irie R.
J. Natl. Cancer Inst. 93:1159-1165(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Identification and characterization of three new components of the mSin3A corepressor complex."
Fleischer T.C., Yun U.J., Ayer D.E.
Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE SPECIFICITY, IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[3]"Characterization of BRCAA1 and its novel antigen epitope identification."
Cui D., Jin G., Gao T.W., Sun T., Tian F., Estrada G.G., Gao H., Sarai A.
Cancer Epidemiol. Biomarkers Prev. 13:1136-1145(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Rheumatoid arthritis antigenic protein similar to retinoblastoma binding protein 1 (RBP1)."
Tanaka M.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Synovium.
[5]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-651 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-424.
Tissue: Hippocampus, Kidney and Lung.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1149 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-1312.
Tissue: Adipose tissue and Testis.
[9]"Human breast carcinoma-associated antigen isoform I."
Cao J., Irie R.F., Stanbridge E.J.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 440-1312 (ISOFORM 1).
[10]"Human Rb binding protein homolog gene, partial CDS."
Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1312.
[11]"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] OF 828-1312.
[12]"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-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-666; SER-675; SER-790; THR-793; THR-1150; SER-1152; SER-1153; SER-1155 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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-790; THR-793; SER-1014 AND THR-1026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-675; SER-778; SER-790 AND THR-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-276; SER-778; SER-790 AND THR-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF214114 mRNA. Translation: AAF28341.2.
AY220790 mRNA. Translation: AAO63590.1.
AF208045 mRNA. Translation: AAF23433.3. Frameshift.
AB030181 mRNA. Translation: BAA89794.1.
AB210032 mRNA. Translation: BAE06114.1. Different initiation.
AL391994, AL133418 Genomic DNA. Translation: CAI13747.2.
AL391994 Genomic DNA. Translation: CAI13749.1.
AL391994, AL133418 Genomic DNA. Translation: CAI13751.1. Sequence problems.
AL133418, AL391994 Genomic DNA. Translation: CAI22961.2.
AL133418, AL391994 Genomic DNA. Translation: CAI22962.1.
BC048959 mRNA. Translation: AAH48959.1. Different termination.
BC062536 mRNA. Translation: AAH62536.1. Different termination.
BC104632 mRNA. Translation: AAI04633.1. Different termination.
BC130418 mRNA. Translation: AAI30419.1.
BX648820 mRNA. Translation: CAI46047.1.
AL133594 mRNA. Translation: CAB63731.1.
AF227899 mRNA. Translation: AAF36964.1.
AF083249 mRNA. Translation: AAD41239.1. Frameshift.
AK023144 mRNA. Translation: BAB14428.1. Different initiation.
PIRT43497.
RefSeqNP_001193723.1. NM_001206794.1.
NP_057458.4. NM_016374.5.
NP_112739.2. NM_031371.3.
UniGeneHs.575782.

3D structure databases

ProteinModelPortalQ4LE39.
SMRQ4LE39. Positions 5-121, 170-271, 308-394, 564-632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119708. 12 interactions.
IntActQ4LE39. 11 interactions.

PTM databases

PhosphoSiteQ4LE39.

Polymorphism databases

DMDM143955276.

Proteomic databases

PaxDbQ4LE39.
PRIDEQ4LE39.

Protocols and materials databases

DNASU51742.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264183; ENSP00000264183; ENSG00000054267. [Q4LE39-1]
ENST00000349213; ENSP00000264184; ENSG00000054267. [Q4LE39-2]
ENST00000366603; ENSP00000355562; ENSG00000054267. [Q4LE39-1]
ENST00000421364; ENSP00000394663; ENSG00000054267. [Q4LE39-3]
GeneID51742.
KEGGhsa:51742.
UCSCuc001hwq.3. human. [Q4LE39-1]
uc001hwr.3. human. [Q4LE39-2]
uc001hwt.4. human. [Q4LE39-4]

Organism-specific databases

CTD51742.
GeneCardsGC01M235296.
HGNCHGNC:15550. ARID4B.
HPAHPA027333.
MIM609696. gene.
neXtProtNX_Q4LE39.
PharmGKBPA134940494.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248805.
HOVERGENHBG058247.
InParanoidQ4LE39.
OMAFRLVHKL.
PhylomeDBQ4LE39.
TreeFamTF106427.

Gene expression databases

BgeeQ4LE39.
GenevestigatorQ4LE39.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR028853. ARID4B.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERPTHR13964:SF3. PTHR13964:SF3. 1 hit.
PfamPF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARID4B. human.
GeneWikiARID4B.
GenomeRNAi51742.
NextBio55820.
PROQ4LE39.
SOURCESearch...

Entry information

Entry nameARI4B_HUMAN
AccessionPrimary (citable) accession number: Q4LE39
Secondary accession number(s): A1L465 expand/collapse secondary AC list , Q3MHV4, Q5HY99, Q5T2C2, Q5T2C3, Q5T2C4, Q5T2C5, Q5T2C6, Q6P600, Q86UX1, Q86WR4, Q9H915, Q9NYU3, Q9NZB6, Q9NZG4, Q9P2W4, Q9UF62, Q9Y6E1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: March 19, 2014
This is version 85 of the entry and version 2 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM