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HNRC1_HUMAN
ID   HNRC1_HUMAN             Reviewed;         293 AA.
AC   O60812; B2RP44;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 179.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein C-like 1;
DE            Short=hnRNP C-like-1;
DE   AltName: Full=hnRNP core protein C-like 1;
GN   Name=HNRNPCL1; Synonyms=HNRPCL1;
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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       O60812; A1L168: C20orf202; NbExp=3; IntAct=EBI-1046507, EBI-18396958;
CC       O60812; P07910: HNRNPC; NbExp=3; IntAct=EBI-1046507, EBI-357966;
CC       O60812; O60812: HNRNPCL1; NbExp=3; IntAct=EBI-1046507, EBI-1046507;
CC       O60812; B2RXH8: HNRNPCL2; NbExp=3; IntAct=EBI-1046507, EBI-9512317;
CC       O60812; O75928-2: PIAS2; NbExp=3; IntAct=EBI-1046507, EBI-348567;
CC       O60812; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-1046507, EBI-948156;
CC       O60812; Q53GL6: RALY; NbExp=3; IntAct=EBI-1046507, EBI-9512693;
CC       O60812; Q86SE5-3: RALYL; NbExp=3; IntAct=EBI-1046507, EBI-11526555;
CC       O60812; P78317: RNF4; NbExp=3; IntAct=EBI-1046507, EBI-2340927;
CC       O60812; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1046507, EBI-10180829;
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; AL022101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71752.1; -; Genomic_DNA.
DR   EMBL; BC137258; AAI37259.1; -; mRNA.
DR   EMBL; BC171866; AAI71866.1; -; mRNA.
DR   CCDS; CCDS30591.1; -.
DR   RefSeq; NP_001013653.1; NM_001013631.2.
DR   AlphaFoldDB; O60812; -.
DR   SMR; O60812; -.
DR   BioGRID; 131227; 174.
DR   IntAct; O60812; 63.
DR   MINT; O60812; -.
DR   STRING; 9606.ENSP00000479365; -.
DR   GlyGen; O60812; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60812; -.
DR   PhosphoSitePlus; O60812; -.
DR   SwissPalm; O60812; -.
DR   BioMuta; HNRNPCL1; -.
DR   EPD; O60812; -.
DR   jPOST; O60812; -.
DR   MassIVE; O60812; -.
DR   MaxQB; O60812; -.
DR   PaxDb; O60812; -.
DR   PeptideAtlas; O60812; -.
DR   PRIDE; O60812; -.
DR   ProteomicsDB; 49605; -.
DR   Antibodypedia; 65448; 114 antibodies from 18 providers.
DR   DNASU; 343069; -.
DR   Ensembl; ENST00000317869.7; ENSP00000365370.4; ENSG00000179172.10.
DR   Ensembl; ENST00000634171.3; ENSP00000488130.1; ENSG00000282175.4.
DR   GeneID; 343069; -.
DR   KEGG; hsa:343069; -.
DR   MANE-Select; ENST00000317869.7; ENSP00000365370.4; NM_001013631.3; NP_001013653.1.
DR   UCSC; uc010obf.2; human.
DR   CTD; 343069; -.
DR   GeneCards; HNRNPCL1; -.
DR   HGNC; HGNC:29295; HNRNPCL1.
DR   HPA; ENSG00000179172; Not detected.
DR   neXtProt; NX_O60812; -.
DR   OpenTargets; ENSG00000179172; -.
DR   PharmGKB; PA162391240; -.
DR   VEuPathDB; HostDB:ENSG00000179172; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000153402; -.
DR   HOGENOM; CLU_079090_0_0_1; -.
DR   InParanoid; O60812; -.
DR   OMA; MECEGGA; -.
DR   OrthoDB; 1315388at2759; -.
DR   PhylomeDB; O60812; -.
DR   TreeFam; TF330974; -.
DR   PathwayCommons; O60812; -.
DR   SignaLink; O60812; -.
DR   BioGRID-ORCS; 343069; 101 hits in 986 CRISPR screens.
DR   GenomeRNAi; 343069; -.
DR   Pharos; O60812; Tdark.
DR   PRO; PR:O60812; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O60812; protein.
DR   Bgee; ENSG00000179172; Expressed in skeletal muscle tissue of biceps brachii and 24 other tissues.
DR   Genevisible; O60812; HS.
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; HDA:UniProtKB.
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 1"
FT                   /id="PRO_0000081848"
FT   DOMAIN          16..87
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          137..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..263
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..293
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         81
FT                   /note="D -> V (in dbSNP:rs2982092)"
FT                   /id="VAR_059824"
FT   VARIANT         208
FT                   /note="Q -> H (in dbSNP:rs6702447)"
FT                   /id="VAR_052225"
FT   VARIANT         258
FT                   /note="V -> D (in dbSNP:rs2076063)"
FT                   /id="VAR_033723"
SQ   SEQUENCE   293 AA;  32142 MW;  C87938AE3189D8E2 CRC64;
     MASNVTNKMD PHSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIAGCSVHK GFAFVQYDKE
     KNARAAVAGE DGRMIASQVV DINLAAEPKV NRGNAGVKRS AAEMYGSSFD LDYGFQRDYY
     DGMYSFPARV PPPPPIALAV VPSKRQRLSG NTSRRGKSGF NSKSGKRGSS KSGKLKGDDL
     QAIKQELTQI KQKVDSLLEN LEKIEKEQSK QEVEVKNAKS EEEQSSSSMK KDETHVKMES
     EGGAEDSAEE GDPLDDDVNE DQGDDQLELI KDDEKEAEEG EDDRDSTNGQ DDS
 
 
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