HNRC2_HUMAN
ID HNRC2_HUMAN Reviewed; 293 AA.
AC B2RXH8; B7ZW41;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein C-like 2;
DE Short=hnRNP C-like-2;
GN Name=HNRNPCL2; Synonyms=HNRNPCP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in nucleosome assembly by neutralizing basic
CC proteins such as A and B core hnRNPs. {ECO:0000250}.
CC -!- INTERACTION:
CC B2RXH8; P07910: HNRNPC; NbExp=3; IntAct=EBI-9512317, EBI-357966;
CC B2RXH8; O60812: HNRNPCL1; NbExp=3; IntAct=EBI-9512317, EBI-1046507;
CC B2RXH8; B2RXH8: HNRNPCL2; NbExp=3; IntAct=EBI-9512317, EBI-9512317;
CC B2RXH8; O75864: PPP1R37; NbExp=3; IntAct=EBI-9512317, EBI-5235692;
CC B2RXH8; Q53GL6: RALY; NbExp=3; IntAct=EBI-9512317, EBI-9512693;
CC B2RXH8; Q86SE5-3: RALYL; NbExp=3; IntAct=EBI-9512317, EBI-11526555;
CC B2RXH8; P78317: RNF4; NbExp=3; IntAct=EBI-9512317, EBI-2340927;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC ribonucleosomes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
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DR EMBL; BX640550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC144551; AAI44552.1; -; mRNA.
DR EMBL; BC157858; AAI57859.1; -; mRNA.
DR EMBL; BC171863; AAI71863.1; -; mRNA.
DR CCDS; CCDS76105.1; -.
DR RefSeq; NP_001130033.3; NM_001136561.3.
DR AlphaFoldDB; B2RXH8; -.
DR SMR; B2RXH8; -.
DR BioGRID; 136689; 297.
DR IntAct; B2RXH8; 36.
DR MINT; B2RXH8; -.
DR STRING; 9606.ENSP00000479203; -.
DR GlyGen; B2RXH8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; B2RXH8; -.
DR PhosphoSitePlus; B2RXH8; -.
DR BioMuta; HNRNPCL2; -.
DR jPOST; B2RXH8; -.
DR MassIVE; B2RXH8; -.
DR PeptideAtlas; B2RXH8; -.
DR PRIDE; B2RXH8; -.
DR DNASU; 440563; -.
DR Ensembl; ENST00000621994.3; ENSP00000479203.2; ENSG00000275774.3.
DR Ensembl; ENST00000633387.3; ENSP00000488781.2; ENSG00000283370.2.
DR Ensembl; ENST00000633810.2; ENSP00000488742.1; ENSG00000282530.2.
DR GeneID; 440563; -.
DR KEGG; hsa:440563; -.
DR MANE-Select; ENST00000621994.3; ENSP00000479203.2; NM_001136561.3; NP_001130033.3.
DR UCSC; uc010obg.3; human.
DR CTD; 440563; -.
DR GeneCards; HNRNPCL2; -.
DR HGNC; HGNC:48813; HNRNPCL2.
DR HPA; ENSG00000275774; Not detected.
DR neXtProt; NX_B2RXH8; -.
DR OpenTargets; ENSG00000275774; -.
DR VEuPathDB; HostDB:ENSG00000275774; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153402; -.
DR HOGENOM; CLU_079090_0_0_1; -.
DR OMA; RPAGDMY; -.
DR OrthoDB; 1022166at2759; -.
DR PathwayCommons; B2RXH8; -.
DR SignaLink; B2RXH8; -.
DR BioGRID-ORCS; 440563; 13 hits in 194 CRISPR screens.
DR GenomeRNAi; 440563; -.
DR Pharos; B2RXH8; Tdark.
DR PRO; PR:B2RXH8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; B2RXH8; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..293
FT /note="Heterogeneous nuclear ribonucleoprotein C-like 2"
FT /id="PRO_0000430276"
FT DOMAIN 16..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 140..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..225
FT /evidence="ECO:0000255"
FT COMPBIAS 145..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 247
FT /note="S -> P (in Ref. 2; AAI71863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32072 MW; 6D748EFD8FEE28DD CRC64;
MASNVTNKMD PHSVNSRVFI GNLNTLVVKK SDVEAIFSKY GKIAGCSVHK GFAFVQYDKE
KNARAAVAGE DGRMIASQVA VINLAAEPKV NRGNAGVKRS AAEMYGSSFD LDYGFQRDYY
DGMYSFPARV PPPPPIALAV VPSKRQRISG NTSRRGKSGF NSKSGKRGSS KSGKLKGDDL
QAIKQELTQI KQKVDSLLEN LEKIEKEQSK QEVEVKNAKS EEEQSSSSMK KDETHVKMES
EGGAEDSAEE GDPLDDDDNE DQGDNQLHLI KNNEKDAEEG EDNRDSTNGQ DDS
