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Protein

Heterogeneous nuclear ribonucleoprotein U-like protein 1

Gene

Hnrnpul1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein U-like protein 1
Gene namesi
Name:Hnrnpul1
Synonyms:Hnrpul1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2443517. Hnrnpul1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Heterogeneous nuclear ribonucleoprotein U-like protein 1PRO_0000227556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki117 – 117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei195 – 1951PhosphoserineCombined sources
Modified residuei210 – 2101PhosphothreonineCombined sources
Modified residuei513 – 5131PhosphoserineBy similarity
Modified residuei721 – 7211PhosphoserineBy similarity

Post-translational modificationi

Methylated.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VDM6.
MaxQBiQ8VDM6.
PaxDbiQ8VDM6.
PRIDEiQ8VDM6.

PTM databases

iPTMnetiQ8VDM6.
PhosphoSiteiQ8VDM6.

Expressioni

Gene expression databases

BgeeiQ8VDM6.
GenevisibleiQ8VDM6. MM.

Interactioni

Subunit structurei

Interacts with BRD7, PRMT2, TP53 and NXF1. Associates with histones and BRD7 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231344. 2 interactions.
IntActiQ8VDM6. 3 interactions.
MINTiMINT-4119866.
STRINGi10090.ENSMUSP00000037268.

Structurei

3D structure databases

ProteinModelPortaliQ8VDM6.
SMRiQ8VDM6. Positions 1-37, 210-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 3735SAPPROSITE-ProRule annotationAdd
BLAST
Domaini192 – 389198B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Repeati613 – 61531-1
Repeati620 – 62231-2
Repeati639 – 64131-3
Repeati645 – 64731-4
Repeati659 – 66131-5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 103103Necessary for interaction with HRMT1L1By similarityAdd
BLAST
Regioni214 – 859646Necessary for interaction with TP53By similarityAdd
BLAST
Regioni457 – 595139Necessary for interaction with BRD7 and transcriptional activationBy similarityAdd
BLAST
Regioni613 – 661495 X 3 AA repeats of R-G-GAdd
BLAST
Regioni613 – 66149Necessary for transcription repressionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi614 – 66956Gly-richAdd
BLAST
Compositional biasi671 – 69222Asn-richAdd
BLAST
Compositional biasi695 – 814120Pro-richAdd
BLAST
Compositional biasi760 – 84889Tyr-richAdd
BLAST
Compositional biasi809 – 83527Gln-richAdd
BLAST

Domaini

The RGG-box domain is methylated.By similarity

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
ENOG410XSBV. LUCA.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
HOVERGENiHBG061101.
InParanoidiQ8VDM6.
KOiK15047.
OMAiGYERRPL.
OrthoDBiEOG79CZ07.
PhylomeDBiQ8VDM6.
TreeFamiTF317301.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR027025. hnRNP_U-like_1.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR12381:SF41. PTHR12381:SF41. 2 hits.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VDM6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLLAALEAE EPEDERELEA
60 70 80 90 100
DDDPGLPGHN NEEVETEGGS ELEGTAQPPP PGLQPHPEPG GYSGPDGHYV
110 120 130 140 150
MDNITRQNQF YETPVIKQEN ESSYDRRPLD MEPQQQVYHP ELKTEMKQEA
160 170 180 190 200
PPSFLPPEAS QLKTDRPQFQ NRKRPFEENR GRGYFEHRED RRGRSPQPPA
210 220 230 240 250
EEDEDDFDDT LVAIDTYNCD LHFKVARDRS SGYPLTIEGF AYLWSGARAS
260 270 280 290 300
YGVRRGRVCF EMKINEEISV KHLPSTEPDP HVVRIGWSLD SCSTQLGEEP
310 320 330 340 350
FSYGYGGTGK KSTNSRFENY GDKFAENDVI GCFADFECGN DVELSFTKNG
360 370 380 390 400
KWMGIAFRIQ KEALGGQALY PHVLVKNCAV EFNFGQRAEP YCSVLPGFTF
410 420 430 440 450
IQHLPLSERI RGTIGPKSKA ECEILMMVGL PAAGKTTWAI KHAASNPSKK
460 470 480 490 500
YNILGTNAIM DKMRVMGLRR QRNYAGRWDV LIQQATQCLN RLIQIAARKK
510 520 530 540 550
RNYILDQTNV YGSAQRRKMR PFEGFQRKAI VICPTDEDLK DRTVKRTDEE
560 570 580 590 600
GKDVPDHAVL EMKANFTLPD VGDFLDEVLF IELQREEADK LVRQYNEEGR
610 620 630 640 650
KAGPPPEKRF DSRGGGFRGR GGGGGFQRYD NRGPPGGNRG GFQNRGGGGG
660 670 680 690 700
SGGGGGNYRG GFNRSGGGGY NQNRWGNNNR DNNNSNNRGN YNRAPQQQPP
710 720 730 740 750
PQQPPPPQPP PQQPPPPPSY SPARNPPGAS SYNKNSNIPG SSANTSTPTV
760 770 780 790 800
SSYTPPQPSY SQPPYNQGGY TQGYTAPPPP PPPPPAYNYG SYGPYNPAPY
810 820 830 840 850
TPPPPPTAQT YPQPSYNQYQ QYAQQWSQYY QNQSQWPPYY GNYDYGGYSG

STQGGTSTQ
Length:859
Mass (Da):96,002
Last modified:March 1, 2002 - v1
Checksum:i197328B681DF260E
GO
Isoform 2 (identifier: Q8VDM6-2) [UniParc]FASTAAdd to basket

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

Show »
Length:759
Mass (Da):85,046
Checksum:i7DB36055FFEE4BF0
GO
Isoform 3 (identifier: Q8VDM6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     335-340: DFECGN → VLELQV
     341-859: Missing.

Show »
Length:340
Mass (Da):38,733
Checksum:i78013360382D09E2
GO

Sequence cautioni

The sequence AAH27844.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti657 – 6571N → Y in BAE33342 (PubMed:16141072).Curated
Sequence conflicti665 – 6651S → T in BAE33342 (PubMed:16141072).Curated
Sequence conflicti672 – 6721Q → L in BAE33342 (PubMed:16141072).Curated
Sequence conflicti686 – 6861N → Y in BAE33342 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_017553Add
BLAST
Alternative sequencei335 – 3406DFECGN → VLELQV in isoform 3. 1 PublicationVSP_017554
Alternative sequencei341 – 859519Missing in isoform 3. 1 PublicationVSP_017555Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042090 mRNA. Translation: BAC31161.1.
AK143666 mRNA. Translation: BAE25486.1.
AK155604 mRNA. Translation: BAE33342.1.
BC021506 mRNA. Translation: AAH21506.1.
BC027844 mRNA. Translation: AAH27844.1. Different initiation.
BC078642 mRNA. Translation: AAH78642.1.
CCDSiCCDS20995.1. [Q8VDM6-1]
CCDS39841.1. [Q8VDM6-3]
RefSeqiNP_659171.1. NM_144922.2. [Q8VDM6-1]
NP_835190.1. NM_178089.2. [Q8VDM6-3]
XP_006539918.1. XM_006539855.2. [Q8VDM6-2]
XP_006539919.1. XM_006539856.1. [Q8VDM6-2]
UniGeneiMm.254223.

Genome annotation databases

EnsembliENSMUST00000043765; ENSMUSP00000037268; ENSMUSG00000040725. [Q8VDM6-2]
ENSMUST00000108401; ENSMUSP00000104038; ENSMUSG00000040725. [Q8VDM6-3]
ENSMUST00000206832; ENSMUSP00000146263; ENSMUSG00000040725. [Q8VDM6-1]
GeneIDi232989.
KEGGimmu:232989.
UCSCiuc009ftu.1. mouse. [Q8VDM6-1]
uc009ftw.1. mouse. [Q8VDM6-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042090 mRNA. Translation: BAC31161.1.
AK143666 mRNA. Translation: BAE25486.1.
AK155604 mRNA. Translation: BAE33342.1.
BC021506 mRNA. Translation: AAH21506.1.
BC027844 mRNA. Translation: AAH27844.1. Different initiation.
BC078642 mRNA. Translation: AAH78642.1.
CCDSiCCDS20995.1. [Q8VDM6-1]
CCDS39841.1. [Q8VDM6-3]
RefSeqiNP_659171.1. NM_144922.2. [Q8VDM6-1]
NP_835190.1. NM_178089.2. [Q8VDM6-3]
XP_006539918.1. XM_006539855.2. [Q8VDM6-2]
XP_006539919.1. XM_006539856.1. [Q8VDM6-2]
UniGeneiMm.254223.

3D structure databases

ProteinModelPortaliQ8VDM6.
SMRiQ8VDM6. Positions 1-37, 210-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231344. 2 interactions.
IntActiQ8VDM6. 3 interactions.
MINTiMINT-4119866.
STRINGi10090.ENSMUSP00000037268.

PTM databases

iPTMnetiQ8VDM6.
PhosphoSiteiQ8VDM6.

Proteomic databases

EPDiQ8VDM6.
MaxQBiQ8VDM6.
PaxDbiQ8VDM6.
PRIDEiQ8VDM6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043765; ENSMUSP00000037268; ENSMUSG00000040725. [Q8VDM6-2]
ENSMUST00000108401; ENSMUSP00000104038; ENSMUSG00000040725. [Q8VDM6-3]
ENSMUST00000206832; ENSMUSP00000146263; ENSMUSG00000040725. [Q8VDM6-1]
GeneIDi232989.
KEGGimmu:232989.
UCSCiuc009ftu.1. mouse. [Q8VDM6-1]
uc009ftw.1. mouse. [Q8VDM6-3]

Organism-specific databases

CTDi11100.
MGIiMGI:2443517. Hnrnpul1.

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
ENOG410XSBV. LUCA.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
HOVERGENiHBG061101.
InParanoidiQ8VDM6.
KOiK15047.
OMAiGYERRPL.
OrthoDBiEOG79CZ07.
PhylomeDBiQ8VDM6.
TreeFamiTF317301.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

PROiQ8VDM6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDM6.
GenevisibleiQ8VDM6. MM.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR027025. hnRNP_U-like_1.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR12381:SF41. PTHR12381:SF41. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Spleen and Thymus.
  2. "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 AND 2).
    Strain: FVB/N.
    Tissue: Embryo and Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND THR-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiHNRL1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDM6
Secondary accession number(s): Q3U201
, Q3UPB0, Q6AZA7, Q8BY45, Q8K365
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.