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Reviewed, UniProtKB/Swiss-Prot Q9BUJ2 (HNRL1_HUMAN)

Last modified February 9, 2010. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.8

Subunit structure

Interacts with the adenovirus type 5 (Ad5) E1B-55 kDa, BRD7, HRMT1L1, TP53 and TAP. Associates with histones and BRD7. Ref.1 Ref.8 Ref.6 Ref.7 Ref.11

Subcellular location

Nucleus Ref.1 Ref.8 Ref.7.

Domain

The RGG-box domain is methylated.

Post-translational modification

Methylated. Ref.7 Ref.9

Miscellaneous

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

Sequence similarities

Contains 1 B30.2/SPRY domain.

Contains 1 SAP domain.

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Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionActivator
Repressor
Ribonucleoprotein
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from Experiment. Source: Reactome

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

response to virus Ref.1

Traceable author statement. Source: ProtInc

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentheterogeneous nuclear ribonucleoprotein complex Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding Ref.1

Traceable author statement. Source: ProtInc

protein binding Ref.11

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CNBPP626331EBI-1018153,EBI-1047529
POLR1EQ9GZS11EBI-1018153,EBI-359458
TP53P046376EBI-1018153,EBI-366083

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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: No experimental confirmation available.

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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.13 Ref.14 Ref.15 Ref.19
Modified residue2091Phosphothreonine
Modified residue2701N6-acetyllysine Ref.20
Modified residue5121Phosphoserine Ref.19 Ref.10
Modified residue7161Phosphoserine Ref.17
Modified residue7181Phosphoserine Ref.10 Ref.17

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: dbSNP rs17849624. Ref.4
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

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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).

Checksum: 05950AF9FAFD192F
Show »

FASTA80490,292
Isoform 3.

Checksum: 207A6A67EFFFA299
Show »

FASTA75284,500
Isoform 4.

Checksum: B16C6EC86B997FFA
Show »

FASTA75684,794
Isoform 5.

Checksum: A86E13953F84279F
Show »

FASTA39042,189

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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: 9733834] [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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
Tissue: Brain and Embryo.
[3]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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), VARIANT CYS-91.
Tissue: Brain, Eye, Muscle and Placenta.
[5]"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: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-856.
Tissue: Uterus.
[6]"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: 10668806] [Abstract]
Cited for: INTERACTION WITH TAP.
[7]"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: 11513728] [Abstract]
Cited for: METHYLATION, SUBCELLULAR LOCATION, INTERACTION WITH HRMT1L1.
[8]"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: 12489984] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH BRD7, ASSOCIATION WITH HISTONES AND BRD7, SUBCELLULAR LOCATION.
[9]"Protein arginine methylation during lytic adenovirus infection."
Kzhyshkowska J., Kremmer E., Hofmann M., Wolf H., Dobner T.
Biochem. J. 383:259-265(2004) [PubMed: 15242333] [Abstract]
Cited for: METHYLATION DURING ADENOVIRAL INFECTION.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-718, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 15907477] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"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: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
[14]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
[15]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
[16]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 AND SER-718, MASS SPECTROMETRY.
[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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209 AND SER-716, MASS SPECTROMETRY.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-512, MASS SPECTROMETRY.
Tissue: T-cell.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-270, MASS SPECTROMETRY.
+Additional computationally mapped references.

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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.
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.
IPIIPI00013070.
IPI00167147.
IPI00386971.
IPI00402391.
IPI00736859.
PIRT08776.
T13159.
RefSeqNP_008971.2.
NP_653333.1.
UniGeneHs.155218
Hs.718642

3D structure databases

SMRQ9BUJ2. Positions 212-389, 379-554.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BUJ2. 14 interactions.
STRINGQ9BUJ2.

PTM databases

PhosphoSiteQ9BUJ2.

Proteomic databases

PRIDEQ9BUJ2.

Genome annotation databases

EnsemblENST00000392006; ENSP00000375863; ENSG00000105323; Homo sapiens. [Genome view]
GeneID11100.
KEGGhsa:11100.
UCSCuc002opz.2. human.
uc002oqb.2. human.
uc002oqc.2. human.
uc002oqf.2. human.
uc010ehm.1. human.

Organism-specific databases

CTD11100.
GeneCardsGC19P046463.
H-InvDBHIX0015150.
HGNCHGNC:17011. HNRNPUL1.
MIM605800. gene.
PharmGKBPA134899936.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12773.
HOVERGENQ9BUJ2.
InParanoidQ9BUJ2.
OMASGPDGHY.
PhylomeDBQ9BUJ2.

Enzyme and pathway databases

ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9BUJ2.
BgeeQ9BUJ2.
CleanExHS_HNRNPUL1.
GenevestigatorQ9BUJ2.
GermOnlineENSG00000105323. Homo sapiens.

Family and domain databases

InterProIPR001870. B302.
IPR003034. SAP_DNA_bd.
IPR018355. SPla/RYanodine_receptor_sg.
IPR003877. SPRY_rcpt.
[Graphical view]
PfamPF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
PROSITEPS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42198.
SOURCESearch...

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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: February 9, 2010
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 19

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents