Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heterogeneous nuclear ribonucleoprotein L-like

Gene

Hnrnpll

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding protein that functions as regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein L-like
Gene namesi
Name:Hnrnpll
Synonyms:Hnrpll
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1919942. Hnrnpll.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi136 – 1361V → D: Alters RRM 1 stability. Abolishes regulation of alternative splicing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Heterogeneous nuclear ribonucleoprotein L-likePRO_0000081610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei48 – 481PhosphothreonineBy similarity
Modified residuei107 – 1071PhosphoserineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei124 – 1241PhosphoserineBy similarity

Post-translational modificationi

Isoform 3 is phosphorylated at 'Ser-64'.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ921F4.
MaxQBiQ921F4.
PaxDbiQ921F4.
PeptideAtlasiQ921F4.
PRIDEiQ921F4.

PTM databases

iPTMnetiQ921F4.
PhosphoSiteiQ921F4.

Expressioni

Inductioni

Up-regulated in stimulated T-cells.1 Publication

Gene expression databases

BgeeiQ921F4.
CleanExiMM_HNRPLL.
ExpressionAtlasiQ921F4. baseline and differential.
GenevisibleiQ921F4. MM.

Interactioni

Subunit structurei

Interacts with HNRNPL.By similarity

Protein-protein interaction databases

BioGridi215518. 2 interactions.
STRINGi10090.ENSMUSP00000058308.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi125 – 1317Combined sources
Helixi138 – 1458Combined sources
Turni146 – 1483Combined sources
Beta strandi151 – 1577Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 1698Combined sources
Helixi170 – 18213Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi216 – 2249Combined sources
Helixi231 – 2388Combined sources
Turni239 – 2413Combined sources
Beta strandi244 – 26320Combined sources
Helixi264 – 27411Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi302 – 3098Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEXNMR-A117-207[»]
2E5INMR-A200-316[»]
ProteinModelPortaliQ921F4.
SMRiQ921F4. Positions 118-316, 385-585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ921F4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 19975RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini215 – 29379RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini384 – 45875RRM 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 87Poly-Ser
Compositional biasi58 – 11659Gly-richAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1456. Eukaryota.
ENOG410XQHN. LUCA.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
InParanoidiQ921F4.
KOiK13159.
OMAiQIRIPNG.
OrthoDBiEOG7HMS2K.
PhylomeDBiQ921F4.
TreeFamiTF354318.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR006536. HnRNP-L/PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q921F4-1) [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
MSSSSSSSPK EETYEEDREF ESQAKRLKTE EGEIVYSAEE SENRQEATPQ
60 70 80 90 100
AGSDSDSGGG DGGDGDGGSG GGGDGEEGEG GEEGDEGDGD EGGSGGDEGG
110 120 130 140 150
SGGGPRSMPL STEGGGSHHK VSVSPVVHVR GLCESVVEAD LVEALEKFGT
160 170 180 190 200
ICYVMMMPFK RQALVEFENI DSAKECVTFA ADVPVYIAGQ QAFFNYSTSK
210 220 230 240 250
RITRPGNTDD PSGGNKVLLL SIQNPLYPIT VDVLYTVCNP VGKVQRIVIF
260 270 280 290 300
KRNGIQAMVE FESVLCAQKA KAALNGADIY AGCCTLKIEY ARPTRLNVIR
310 320 330 340 350
NDNDSWDYTK PYLGRRDRGK GRQRQAILGD HPSSFRHDGY GSHGPLLPLP
360 370 380 390 400
SRYRMGSRDT PELVAYPLPQ ASSSYMHGGS PSGSVVMVSG LHQLKMNCSR
410 420 430 440 450
VFNLFCLYGN IEKVKFMKTI PGTALVEMGD EYAVERAVTH LNNVKLFGKR
460 470 480 490 500
LNVCVSKQHS VVPSQIFELE DGTSSYKDFA MSKNNRFTSA GQASKNIIQP
510 520 530 540 550
PSCVLHYYNV PLCVTEETFT KLCNDHEVLP FIKYKVFDAK ASAKTLSGLL
560 570 580 590
EWKCKTDAVE ALTALNHYQI RVPNGSNPYT LKLCFSTSSH L
Length:591
Mass (Da):64,125
Last modified:March 29, 2005 - v3
Checksum:i431C0167DF619FB7
GO
Isoform 2 (identifier: Q921F4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     317-326: DRGKGRQRQA → GRYFTNFRMY
     327-591: Missing.

Note: No experimental confirmation available.
Show »
Length:326
Mass (Da):34,938
Checksum:iC0EC9B1EE165C671
GO
Isoform 3 (identifier: Q921F4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.
     522-591: LCNDHEVLPF...KLCFSTSSHL → VGTEESSVRM...RLVVLDGFLC

Show »
Length:100
Mass (Da):11,485
Checksum:i912DB4EB7D70EDE3
GO

Sequence cautioni

The sequence BAE27500.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41S → T in AAH12849 (PubMed:15489334).Curated
Sequence conflicti101 – 1011S → SGGG in AAH12849 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 480480Missing in isoform 3. 1 PublicationVSP_026132Add
BLAST
Alternative sequencei317 – 32610DRGKGRQRQA → GRYFTNFRMY in isoform 2. 1 PublicationVSP_013290
Alternative sequencei327 – 591265Missing in isoform 2. 1 PublicationVSP_013291Add
BLAST
Alternative sequencei522 – 59170LCNDH…TSSHL → VGTEESSVRMLRFVFYVYVV FHSSASFENFSKILLFVVSL VWVCVRRAYRLVVLDGFLC in isoform 3. 1 PublicationVSP_026133Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034860 mRNA. Translation: BAC28858.1.
AK146879 mRNA. Translation: BAE27500.1. Different initiation.
BC004763 mRNA. Translation: AAH04763.1.
BC012849 mRNA. Translation: AAH12849.2.
BC071184 mRNA. Translation: AAH71184.1.
CCDSiCCDS70845.1. [Q921F4-1]
RefSeqiNP_659051.3. NM_144802.4. [Q921F4-1]
UniGeneiMm.64579.

Genome annotation databases

EnsembliENSMUST00000061331; ENSMUSP00000058308; ENSMUSG00000024095. [Q921F4-1]
ENSMUST00000184635; ENSMUSP00000139372; ENSMUSG00000024095. [Q921F4-1]
GeneIDi72692.
KEGGimmu:72692.
UCSCiuc008dqk.2. mouse. [Q921F4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034860 mRNA. Translation: BAC28858.1.
AK146879 mRNA. Translation: BAE27500.1. Different initiation.
BC004763 mRNA. Translation: AAH04763.1.
BC012849 mRNA. Translation: AAH12849.2.
BC071184 mRNA. Translation: AAH71184.1.
CCDSiCCDS70845.1. [Q921F4-1]
RefSeqiNP_659051.3. NM_144802.4. [Q921F4-1]
UniGeneiMm.64579.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEXNMR-A117-207[»]
2E5INMR-A200-316[»]
ProteinModelPortaliQ921F4.
SMRiQ921F4. Positions 118-316, 385-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215518. 2 interactions.
STRINGi10090.ENSMUSP00000058308.

PTM databases

iPTMnetiQ921F4.
PhosphoSiteiQ921F4.

Proteomic databases

EPDiQ921F4.
MaxQBiQ921F4.
PaxDbiQ921F4.
PeptideAtlasiQ921F4.
PRIDEiQ921F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061331; ENSMUSP00000058308; ENSMUSG00000024095. [Q921F4-1]
ENSMUST00000184635; ENSMUSP00000139372; ENSMUSG00000024095. [Q921F4-1]
GeneIDi72692.
KEGGimmu:72692.
UCSCiuc008dqk.2. mouse. [Q921F4-1]

Organism-specific databases

CTDi92906.
MGIiMGI:1919942. Hnrnpll.

Phylogenomic databases

eggNOGiKOG1456. Eukaryota.
ENOG410XQHN. LUCA.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
InParanoidiQ921F4.
KOiK13159.
OMAiQIRIPNG.
OrthoDBiEOG7HMS2K.
PhylomeDBiQ921F4.
TreeFamiTF354318.

Miscellaneous databases

EvolutionaryTraceiQ921F4.
PROiQ921F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ921F4.
CleanExiMM_HNRPLL.
ExpressionAtlasiQ921F4. baseline and differential.
GenevisibleiQ921F4. MM.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR006536. HnRNP-L/PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Embryonic heart.
  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 3).
    Strain: C57BL/6J and Czech II.
    Tissue: Embryonic germ cell and Mammary gland.
  3. "Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL."
    Wu Z., Jia X., de la Cruz L., Su X.-C., Marzolf B., Troisch P., Zak D., Hamilton A., Whittle B., Yu D., Sheahan D., Bertram E., Aderem A., Otting G., Goodnow C.C., Hoyne G.F.
    Immunity 29:863-875(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-136, INDUCTION, STRUCTURE BY NMR OF RRM 1.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Solution structure of RNA binding domains in heterogeneous nuclear ribonucleoprotein L-like."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 119-316.

Entry informationi

Entry nameiHNRLL_MOUSE
AccessioniPrimary (citable) accession number: Q921F4
Secondary accession number(s): Q3UIK6
, Q6IR44, Q8BIP6, Q91W02, Q99J40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: July 6, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.