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Q9BUJ2 (HNRL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Heterogeneous nuclear ribonucleoprotein U-like protein 1
Alternative name(s):
Adenovirus early region 1B-associated protein 5
E1B-55 kDa-associated protein 5
Short name=E1B-AP5
Gene names
Name:HNRNPUL1
Synonyms:E1BAP5, HNRPUL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length856 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro. Ref.1 Ref.9

Subunit structure

Interacts with the adenovirus type 5 (Ad5) E1B-55 kDa, BRD7, PRMT2, TP53 and NXF1. Associates with histones and BRD7. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11

Subcellular location

Nucleus Ref.1 Ref.8 Ref.9.

Domain

The RGG-box domain is methylated.

Post-translational modification

Methylated. Ref.8 Ref.10

Miscellaneous

Its methylation is enhanced in the late phase of adenoviral infection.

Sequence similarities

Contains 1 B30.2/SPRY domain.

Contains 1 SAP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BRD7Q9NPI15EBI-1018153,EBI-711221

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BUJ2-1)

Also known as: Isoform a;

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: Q9BUJ2-2)

Also known as: Isoform b;

The sequence of this isoform differs from the canonical sequence as follows:
     755-806: Missing.
Isoform 3 (identifier: Q9BUJ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     35-77: Missing.
     263-333: Missing.
     754-754: Q → QSFGFFPSTFQ
Isoform 4 (identifier: Q9BUJ2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
Isoform 5 (identifier: Q9BUJ2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-460: Missing.
     461-562: KMRVMGLRRQ...VPDHAVLEMK → MGFCHVGQAG...CSLWGTSFLL
     754-754: Q → QSFGFFPSTFQ
Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 856856Heterogeneous nuclear ribonucleoprotein U-like protein 1
PRO_0000227555

Regions

Domain3 – 3735SAP
Domain191 – 388198B30.2/SPRY
Repeat612 – 61431-1
Repeat620 – 62231-2
Repeat639 – 64131-3
Repeat645 – 64731-4
Repeat656 – 65831-5
Region1 – 103103Necessary for interaction with HRMT1L1
Region213 – 856644Necessary for interaction with TP53
Region456 – 594139Necessary for interaction with BRD7 and transcriptional activation
Region612 – 658475 X 3 AA repeats of R-G-G
Region612 – 65847Necessary for transcription repression
Compositional bias613 – 66654Gly-rich
Compositional bias670 – 68920Asn-rich
Compositional bias692 – 811120Pro-rich
Compositional bias757 – 84589Tyr-rich
Compositional bias806 – 83227Gln-rich

Amino acid modifications

Modified residue1941Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16 Ref.19
Modified residue5121Phosphoserine Ref.19 Ref.20 Ref.22
Modified residue7181Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 460460Missing in isoform 5.
VSP_017546
Alternative sequence1 – 100100Missing in isoform 4.
VSP_017547
Alternative sequence35 – 7743Missing in isoform 3.
VSP_017548
Alternative sequence263 – 33371Missing in isoform 3.
VSP_017549
Alternative sequence461 – 562102KMRVM…VLEMK → MGFCHVGQAGLELLTSGDPP ASASQSAGITGVSHRARPSV FVFLIHYSSFLHLLPSGRPL FWVEGTRLQKVLTSSSCSLW GTSFLL in isoform 5.
VSP_017550
Alternative sequence7541Q → QSFGFFPSTFQ in isoform 3 and isoform 5.
VSP_017551
Alternative sequence755 – 80652Missing in isoform 2.
VSP_017552
Natural variant911G → C. Ref.5
Corresponds to variant rs17849624 [ dbSNP | Ensembl ].
VAR_025606

Experimental info

Sequence conflict271A → T in CAA07548. Ref.1
Sequence conflict5081N → S in BAC86806. Ref.2
Sequence conflict6191G → A in CAA07548. Ref.1
Sequence conflict6251G → A in CAA07548. Ref.1
Sequence conflict6621S → N in CAA07548. Ref.1
Sequence conflict6911A → S in BAC86806. Ref.2
Sequence conflict7731A → G in CAA07548. Ref.1

Sequences

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

Last modified March 21, 2006. Version 2.
Checksum: 6E57C0271E5F3A77

FASTA85695,739
        10         20         30         40         50         60 
MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLQAALEAE EPDDERELDA DDEPGRPGHI 

        70         80         90        100        110        120 
NEEVETEGGS ELEGTAQPPP PGLQPHAEPG GYSGPDGHYA MDNITRQNQF YDTQVIKQEN 

       130        140        150        160        170        180 
ESGYERRPLE MEQQQAYRPE MKTEMKQGAP TSFLPPEASQ LKPDRQQFQS RKRPYEENRG 

       190        200        210        220        230        240 
RGYFEHREDR RGRSPQPPAE EDEDDFDDTL VAIDTYNCDL HFKVARDRSS GYPLTIEGFA 

       250        260        270        280        290        300 
YLWSGARASY GVRRGRVCFE MKINEEISVK HLPSTEPDPH VVRIGWSLDS CSTQLGEEPF 

       310        320        330        340        350        360 
SYGYGGTGKK STNSRFENYG DKFAENDVIG CFADFECGND VELSFTKNGK WMGIAFRIQK 

       370        380        390        400        410        420 
EALGGQALYP HVLVKNCAVE FNFGQRAEPY CSVLPGFTFI QHLPLSERIR GTVGPKSKAE 

       430        440        450        460        470        480 
CEILMMVGLP AAGKTTWAIK HAASNPSKKY NILGTNAIMD KMRVMGLRRQ RNYAGRWDVL 

       490        500        510        520        530        540 
IQQATQCLNR LIQIAARKKR NYILDQTNVY GSAQRRKMRP FEGFQRKAIV ICPTDEDLKD 

       550        560        570        580        590        600 
RTIKRTDEEG KDVPDHAVLE MKANFTLPDV GDFLDEVLFI ELQREEADKL VRQYNEEGRK 

       610        620        630        640        650        660 
AGPPPEKRFD NRGGGGFRGR GGGGGFQRYE NRGPPGGNRG GFQNRGGGSG GGGNYRGGFN 

       670        680        690        700        710        720 
RSGGGGYSQN RWGNNNRDNN NSNNRGSYNR APQQQPPPQQ PPPPQPPPQQ PPPPPSYSPA 

       730        740        750        760        770        780 
RNPPGASTYN KNSNIPGSSA NTSTPTVSSY SPPQPSYSQP PYNQGGYSQG YTAPPPPPPP 

       790        800        810        820        830        840 
PPAYNYGSYG GYNPAPYTPP PPPTAQTYPQ PSYNQYQQYA QQWNQYYQNQ GQWPPYYGNY 

       850 
DYGSYSGNTQ GGTSTQ 

« Hide

Isoform 2 (Isoform b) [UniParc].

Checksum: 05950AF9FAFD192F
Show »

FASTA80490,292
Isoform 3 [UniParc].

Checksum: 207A6A67EFFFA299
Show »

FASTA75284,500
Isoform 4 [UniParc].

Checksum: B16C6EC86B997FFA
Show »

FASTA75684,794
Isoform 5 [UniParc].

Checksum: A86E13953F84279F
Show »

FASTA39042,189

References

« Hide 'large scale' references
[1]"E1B-55kilodalton-associated protein: a cellular protein with RNA-binding activity implicated in nucleocytoplasmic transport of adenovirus and cellular mRNAs."
Gabler S., Schuett H., Groitl P., Wolf H., Shenk T., Dobner T.
J. Virol. 72:7960-7971(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MRNA PROCESSING, INTERACTION WITH ADENOVIRUS 5 E1B-55 KDA, RNA-BINDING, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[2]"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] (ISOFORMS 1; 3 AND 5).
Tissue: Brain and Embryo.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1; 2 AND 4), VARIANT CYS-91.
Tissue: Brain, Eye, Muscle and Placenta.
[6]"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 355-856.
Tissue: Uterus.
[7]"The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates."
Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.
RNA 6:136-158(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NXF1.
[8]"Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1."
Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H., Dobner T.
Biochem. J. 358:305-314(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION, INTERACTION WITH PRMT2, SUBCELLULAR LOCATION.
[9]"Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7."
Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T.
Biochem. J. 371:385-393(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH BRD7, ASSOCIATION WITH HISTONES AND BRD7, SUBCELLULAR LOCATION.
[10]"Protein arginine methylation during lytic adenovirus infection."
Kzhyshkowska J., Kremmer E., Hofmann M., Wolf H., Dobner T.
Biochem. J. 383:259-265(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION DURING ADENOVIRAL INFECTION.
[11]"The interaction of the hnRNP family member E1B-AP5 with p53."
Barral P.M., Rusch A., Turnell A.S., Gallimore P.H., Byrd P.J., Dobner T., Grand R.J.
FEBS Lett. 579:2752-2758(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53.
[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-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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.
[14]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-194 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-194 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"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-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007509 mRNA. Translation: CAA07548.1.
AK021455 mRNA. Translation: BAB13831.1.
AK022863 mRNA. Translation: BAG51129.1.
AK127057 mRNA. Translation: BAC86806.1.
AC011462 Genomic DNA. No translation available.
AC011510 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57025.1.
BC002564 mRNA. Translation: AAH02564.1.
BC009988 mRNA. Translation: AAH09988.2.
BC014232 mRNA. Translation: AAH14232.1.
BC027713 mRNA. Translation: AAH27713.1.
AL050146 mRNA. Translation: CAB43291.1.
CCDSCCDS12576.1. [Q9BUJ2-1]
CCDS12577.1. [Q9BUJ2-4]
PIRT08776.
T13159.
RefSeqNP_008971.2. NM_007040.3. [Q9BUJ2-1]
NP_653333.1. NM_144732.2. [Q9BUJ2-4]
XP_005258523.1. XM_005258466.1. [Q9BUJ2-4]
UniGeneHs.155218.
Hs.718642.

3D structure databases

ProteinModelPortalQ9BUJ2.
SMRQ9BUJ2. Positions 1-37, 243-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116281. 94 interactions.
IntActQ9BUJ2. 49 interactions.
MINTMINT-121512.

PTM databases

PhosphoSiteQ9BUJ2.

Polymorphism databases

DMDM90101344.

Proteomic databases

MaxQBQ9BUJ2.
PaxDbQ9BUJ2.
PRIDEQ9BUJ2.

Protocols and materials databases

DNASU11100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378215; ENSP00000367460; ENSG00000105323. [Q9BUJ2-3]
ENST00000392006; ENSP00000375863; ENSG00000105323. [Q9BUJ2-1]
ENST00000593587; ENSP00000472629; ENSG00000105323. [Q9BUJ2-4]
ENST00000595018; ENSP00000473132; ENSG00000105323. [Q9BUJ2-4]
ENST00000602130; ENSP00000470687; ENSG00000105323. [Q9BUJ2-2]
GeneID11100.
KEGGhsa:11100.
UCSCuc002opz.4. human. [Q9BUJ2-1]
uc002oqc.4. human. [Q9BUJ2-3]
uc002oqf.4. human. [Q9BUJ2-5]
uc010ehl.1. human. [Q9BUJ2-4]
uc010ehm.3. human. [Q9BUJ2-2]

Organism-specific databases

CTD11100.
GeneCardsGC19P041768.
HGNCHGNC:17011. HNRNPUL1.
HPACAB046477.
HPA046290.
HPA049475.
MIM605800. gene.
neXtProtNX_Q9BUJ2.
PharmGKBPA162391519.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297571.
HOVERGENHBG061101.
InParanoidQ9BUJ2.
KOK15047.
OMASGPDGHY.
OrthoDBEOG79CZ07.
PhylomeDBQ9BUJ2.
TreeFamTF317301.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9BUJ2.
BgeeQ9BUJ2.
CleanExHS_HNRNPUL1.
GenevestigatorQ9BUJ2.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR027025. hnRNP_U_like_1.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERPTHR12381:SF41. PTHR12381:SF41. 1 hit.
PfamPF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPUL1. human.
GeneWikiHNRPUL1.
GenomeRNAi11100.
NextBio42198.
PROQ9BUJ2.
SOURCESearch...

Entry information

Entry nameHNRL1_HUMAN
AccessionPrimary (citable) accession number: Q9BUJ2
Secondary accession number(s): B3KMW7 expand/collapse secondary AC list , O76022, Q6ZSZ0, Q7L8P4, Q8N6Z4, Q96G37, Q9HAL3, Q9UG75
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 129 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM