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Q9BUJ2

- HNRL1_HUMAN

UniProt

Q9BUJ2 - HNRL1_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein U-like protein 1
Gene
HNRNPUL1, E1BAP5, HNRPUL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. enzyme binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: Reactome
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. response to virus Source: ProtInc
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Synonyms:E1BAP5, HNRPUL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17011. HNRNPUL1.

Subcellular locationi

Nucleus 3 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 856856Heterogeneous nuclear ribonucleoprotein U-like protein 1
PRO_0000227555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Phosphoserine5 Publications
Modified residuei512 – 5121Phosphoserine3 Publications
Modified residuei718 – 7181Phosphoserine1 Publication

Post-translational modificationi

Methylated.2 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BUJ2.
PaxDbiQ9BUJ2.
PRIDEiQ9BUJ2.

PTM databases

PhosphoSiteiQ9BUJ2.

Expressioni

Gene expression databases

ArrayExpressiQ9BUJ2.
BgeeiQ9BUJ2.
CleanExiHS_HNRNPUL1.
GenevestigatoriQ9BUJ2.

Organism-specific databases

HPAiCAB046477.
HPA046290.
HPA049475.

Interactioni

Subunit structurei

Interacts with the adenovirus type 5 (Ad5) E1B-55 kDa, BRD7, PRMT2, TP53 and NXF1. Associates with histones and BRD7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRD7Q9NPI15EBI-1018153,EBI-711221

Protein-protein interaction databases

BioGridi116281. 93 interactions.
IntActiQ9BUJ2. 49 interactions.
MINTiMINT-121512.

Structurei

3D structure databases

ProteinModelPortaliQ9BUJ2.
SMRiQ9BUJ2. Positions 1-37, 243-384.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 3735SAP
Add
BLAST
Domaini191 – 388198B30.2/SPRY
Add
BLAST
Repeati612 – 61431-1
Repeati620 – 62231-2
Repeati639 – 64131-3
Repeati645 – 64731-4
Repeati656 – 65831-5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 103103Necessary for interaction with HRMT1L1
Add
BLAST
Regioni213 – 856644Necessary for interaction with TP53
Add
BLAST
Regioni456 – 594139Necessary for interaction with BRD7 and transcriptional activation
Add
BLAST
Regioni612 – 658475 X 3 AA repeats of R-G-G
Add
BLAST
Regioni612 – 65847Necessary for transcription repression
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi613 – 66654Gly-rich
Add
BLAST
Compositional biasi670 – 68920Asn-rich
Add
BLAST
Compositional biasi692 – 811120Pro-rich
Add
BLAST
Compositional biasi757 – 84589Tyr-rich
Add
BLAST
Compositional biasi806 – 83227Gln-rich
Add
BLAST

Domaini

The RGG-box domain is methylated.

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.
Contains 1 SAP domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297571.
HOVERGENiHBG061101.
InParanoidiQ9BUJ2.
KOiK15047.
OMAiSGPDGHY.
OrthoDBiEOG79CZ07.
PhylomeDBiQ9BUJ2.
TreeFamiTF317301.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR001870. 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]
PANTHERiPTHR12381:SF41. PTHR12381:SF41. 1 hit.
PfamiPF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BUJ2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLQAALEAE EPDDERELDA    50
DDEPGRPGHI NEEVETEGGS ELEGTAQPPP PGLQPHAEPG GYSGPDGHYA 100
MDNITRQNQF YDTQVIKQEN ESGYERRPLE MEQQQAYRPE MKTEMKQGAP 150
TSFLPPEASQ LKPDRQQFQS RKRPYEENRG RGYFEHREDR RGRSPQPPAE 200
EDEDDFDDTL VAIDTYNCDL HFKVARDRSS GYPLTIEGFA YLWSGARASY 250
GVRRGRVCFE MKINEEISVK HLPSTEPDPH VVRIGWSLDS CSTQLGEEPF 300
SYGYGGTGKK STNSRFENYG DKFAENDVIG CFADFECGND VELSFTKNGK 350
WMGIAFRIQK EALGGQALYP HVLVKNCAVE FNFGQRAEPY CSVLPGFTFI 400
QHLPLSERIR GTVGPKSKAE CEILMMVGLP AAGKTTWAIK HAASNPSKKY 450
NILGTNAIMD KMRVMGLRRQ RNYAGRWDVL IQQATQCLNR LIQIAARKKR 500
NYILDQTNVY GSAQRRKMRP FEGFQRKAIV ICPTDEDLKD RTIKRTDEEG 550
KDVPDHAVLE MKANFTLPDV GDFLDEVLFI ELQREEADKL VRQYNEEGRK 600
AGPPPEKRFD NRGGGGFRGR GGGGGFQRYE NRGPPGGNRG GFQNRGGGSG 650
GGGNYRGGFN RSGGGGYSQN RWGNNNRDNN NSNNRGSYNR APQQQPPPQQ 700
PPPPQPPPQQ PPPPPSYSPA RNPPGASTYN KNSNIPGSSA NTSTPTVSSY 750
SPPQPSYSQP PYNQGGYSQG YTAPPPPPPP PPAYNYGSYG GYNPAPYTPP 800
PPPTAQTYPQ PSYNQYQQYA QQWNQYYQNQ GQWPPYYGNY DYGSYSGNTQ 850
GGTSTQ 856
Length:856
Mass (Da):95,739
Last modified:March 21, 2006 - v2
Checksum:i6E57C0271E5F3A77
GO
Isoform 2 (identifier: Q9BUJ2-2) [UniParc]FASTAAdd to Basket

Also known as: Isoform b

The sequence of this isoform differs from the canonical sequence as follows:
     755-806: Missing.

Show »
Length:804
Mass (Da):90,292
Checksum:i05950AF9FAFD192F
GO
Isoform 3 (identifier: Q9BUJ2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-77: Missing.
     263-333: Missing.
     754-754: Q → QSFGFFPSTFQ

Show »
Length:752
Mass (Da):84,500
Checksum:i207A6A67EFFFA299
GO
Isoform 4 (identifier: Q9BUJ2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Show »
Length:756
Mass (Da):84,794
Checksum:iB16C6EC86B997FFA
GO
Isoform 5 (identifier: Q9BUJ2-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:390
Mass (Da):42,189
Checksum:iA86E13953F84279F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911G → C.1 Publication
Corresponds to variant rs17849624 [ dbSNP | Ensembl ].
VAR_025606

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 460460Missing in isoform 5.
VSP_017546Add
BLAST
Alternative sequencei1 – 100100Missing in isoform 4.
VSP_017547Add
BLAST
Alternative sequencei35 – 7743Missing in isoform 3.
VSP_017548Add
BLAST
Alternative sequencei263 – 33371Missing in isoform 3.
VSP_017549Add
BLAST
Alternative sequencei461 – 562102KMRVM…VLEMK → MGFCHVGQAGLELLTSGDPP ASASQSAGITGVSHRARPSV FVFLIHYSSFLHLLPSGRPL FWVEGTRLQKVLTSSSCSLW GTSFLL in isoform 5.
VSP_017550Add
BLAST
Alternative sequencei754 – 7541Q → QSFGFFPSTFQ in isoform 3 and isoform 5.
VSP_017551
Alternative sequencei755 – 80652Missing in isoform 2.
VSP_017552Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271A → T in CAA07548. 1 Publication
Sequence conflicti508 – 5081N → S in BAC86806. 1 Publication
Sequence conflicti619 – 6191G → A in CAA07548. 1 Publication
Sequence conflicti625 – 6251G → A in CAA07548. 1 Publication
Sequence conflicti662 – 6621S → N in CAA07548. 1 Publication
Sequence conflicti691 – 6911A → S in BAC86806. 1 Publication
Sequence conflicti773 – 7731A → G in CAA07548. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12576.1. [Q9BUJ2-1]
CCDS12577.1. [Q9BUJ2-4]
PIRiT08776.
T13159.
RefSeqiNP_008971.2. NM_007040.3. [Q9BUJ2-1]
NP_653333.1. NM_144732.2. [Q9BUJ2-4]
XP_005258523.1. XM_005258466.1. [Q9BUJ2-4]
UniGeneiHs.155218.
Hs.718642.

Genome annotation databases

EnsembliENST00000378215; ENSP00000367460; ENSG00000105323. [Q9BUJ2-3]
ENST00000392006; ENSP00000375863; ENSG00000105323. [Q9BUJ2-1]
ENST00000593587; ENSP00000472629; ENSG00000105323. [Q9BUJ2-4]
ENST00000595018; ENSP00000473132; ENSG00000105323. [Q9BUJ2-4]
ENST00000602130; ENSP00000470687; ENSG00000105323. [Q9BUJ2-2]
GeneIDi11100.
KEGGihsa:11100.
UCSCiuc002opz.4. human. [Q9BUJ2-1]
uc002oqc.4. human. [Q9BUJ2-3]
uc002oqf.4. human. [Q9BUJ2-5]
uc010ehl.1. human. [Q9BUJ2-4]
uc010ehm.3. human. [Q9BUJ2-2]

Polymorphism databases

DMDMi90101344.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12576.1. [Q9BUJ2-1 ]
CCDS12577.1. [Q9BUJ2-4 ]
PIRi T08776.
T13159.
RefSeqi NP_008971.2. NM_007040.3. [Q9BUJ2-1 ]
NP_653333.1. NM_144732.2. [Q9BUJ2-4 ]
XP_005258523.1. XM_005258466.1. [Q9BUJ2-4 ]
UniGenei Hs.155218.
Hs.718642.

3D structure databases

ProteinModelPortali Q9BUJ2.
SMRi Q9BUJ2. Positions 1-37, 243-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116281. 93 interactions.
IntActi Q9BUJ2. 49 interactions.
MINTi MINT-121512.

PTM databases

PhosphoSitei Q9BUJ2.

Polymorphism databases

DMDMi 90101344.

Proteomic databases

MaxQBi Q9BUJ2.
PaxDbi Q9BUJ2.
PRIDEi Q9BUJ2.

Protocols and materials databases

DNASUi 11100.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378215 ; ENSP00000367460 ; ENSG00000105323 . [Q9BUJ2-3 ]
ENST00000392006 ; ENSP00000375863 ; ENSG00000105323 . [Q9BUJ2-1 ]
ENST00000593587 ; ENSP00000472629 ; ENSG00000105323 . [Q9BUJ2-4 ]
ENST00000595018 ; ENSP00000473132 ; ENSG00000105323 . [Q9BUJ2-4 ]
ENST00000602130 ; ENSP00000470687 ; ENSG00000105323 . [Q9BUJ2-2 ]
GeneIDi 11100.
KEGGi hsa:11100.
UCSCi uc002opz.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

CTDi 11100.
GeneCardsi GC19P041768.
HGNCi HGNC:17011. HNRNPUL1.
HPAi CAB046477.
HPA046290.
HPA049475.
MIMi 605800. gene.
neXtProti NX_Q9BUJ2.
PharmGKBi PA162391519.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297571.
HOVERGENi HBG061101.
InParanoidi Q9BUJ2.
KOi K15047.
OMAi SGPDGHY.
OrthoDBi EOG79CZ07.
PhylomeDBi Q9BUJ2.
TreeFami TF317301.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPUL1. human.
GeneWikii HNRPUL1.
GenomeRNAii 11100.
NextBioi 42198.
PROi Q9BUJ2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BUJ2.
Bgeei Q9BUJ2.
CleanExi HS_HNRNPUL1.
Genevestigatori Q9BUJ2.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR001870. 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 ]
PANTHERi PTHR12381:SF41. PTHR12381:SF41. 1 hit.
Pfami PF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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. 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].

Entry informationi

Entry nameiHNRL1_HUMAN
AccessioniPrimary (citable) accession number: Q9BUJ2
Secondary accession number(s): B3KMW7
, O76022, Q6ZSZ0, Q7L8P4, Q8N6Z4, Q96G37, Q9HAL3, Q9UG75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: September 3, 2014
This is version 130 of the entry and version 2 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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