ID U2AFL_HUMAN Reviewed; 479 AA. AC Q15695; B2R901; Q13570; Q2M3R8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 24-JAN-2024, entry version 172. DE RecName: Full=U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 {ECO:0000305}; DE AltName: Full=CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1; DE AltName: Full=U2(RNU2) small nuclear RNA auxiliary factor 1-like 1; GN Name=ZRSR2P1 {ECO:0000312|HGNC:HGNC:12456}; GN Synonyms=U2AF1-RS1, U2AF1L1, U2AF1P, U2AF1RS1, U2AFBPL, ZRSR1; 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 [MRNA]. RC TISSUE=Brain; RX PubMed=8586425; DOI=10.1006/geno.1995.9879; RA Kitagawa K., Wang X., Hatada I., Yamaoka T., Nojima H., Inazawa J., Abe T., RA Mitsuya K., Oshimura M., Murata A., Monden M., Mukai T.; RT "Isolation and mapping of human homologues of an imprinted mouse gene RT U2af1-rs1."; RL Genomics 30:257-263(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8630064; DOI=10.1006/bbrc.1996.0716; RA Pearsall R.S., Shibata H., Brozowska A., Yoshino K., Okuda K., Dejong P.J., RA Plass C., Chapman V.M., Hayashizaki Y., Held W.A.; RT "Absence of imprinting in U2AFBPL, a human homologue of the imprinted mouse RT gene U2afbp-rs."; RL Biochem. Biophys. Res. Commun. 222:171-177(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). CC -!- INTERACTION: CC Q15695; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12270264, EBI-10975473; CC Q15695; P55081: MFAP1; NbExp=3; IntAct=EBI-12270264, EBI-1048159; CC Q15695; Q6BDI9: REP15; NbExp=5; IntAct=EBI-12270264, EBI-12048237; CC Q15695; A7MD48: SRRM4; NbExp=3; IntAct=EBI-12270264, EBI-3867173; CC Q15695; P26368-2: U2AF2; NbExp=3; IntAct=EBI-12270264, EBI-11097439; CC Q15695; Q15696: ZRSR2; NbExp=4; IntAct=EBI-12270264, EBI-6657923; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- CAUTION: Defined as a pseudogene by HGNC. However, proteomics data CC suggest the existence of the protein. Appears to have arisen by CC retrotransposition of ZRSR2. It is uncertain if ZRSR2P1 is the ortholog CC of mouse ZRSR1, synteny is not conserved. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D49676; BAA08532.1; -; mRNA. DR EMBL; U51224; AAA98669.1; -; Genomic_DNA. DR EMBL; AK313576; BAG36348.1; -; mRNA. DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; Q15695; -. DR SMR; Q15695; -. DR IntAct; Q15695; 9. DR iPTMnet; Q15695; -. DR PhosphoSitePlus; Q15695; -. DR SwissPalm; Q15695; -. DR BioMuta; ZRSR1; -. DR DMDM; 2833265; -. DR jPOST; Q15695; -. DR MassIVE; Q15695; -. DR MaxQB; Q15695; -. DR PaxDb; 9606-ENSP00000375133; -. DR PeptideAtlas; Q15695; -. DR ProteomicsDB; 60703; -. DR Pumba; Q15695; -. DR UCSC; uc021ycm.2; human. DR AGR; HGNC:12456; -. DR GeneCards; ZRSR2P1; -. DR HGNC; HGNC:12456; ZRSR2P1. DR MIM; 601079; gene. DR neXtProt; NX_Q15695; -. DR eggNOG; KOG2202; Eukaryota. DR HOGENOM; CLU_029117_1_0_1; -. DR InParanoid; Q15695; -. DR PhylomeDB; Q15695; -. DR TreeFam; TF324447; -. DR PathwayCommons; Q15695; -. DR Pharos; Q15695; Tdark. DR PRO; PR:Q15695; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; Q15695; Protein. DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central. DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR CDD; cd12540; RRM_U2AFBPL; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR003954; RRM_dom_euk. DR InterPro; IPR009145; U2AF_small. DR InterPro; IPR000571; Znf_CCCH. DR PANTHER; PTHR12620:SF33; U2 SMALL NUCLEAR RIBONUCLEOPROTEIN AUXILIARY FACTOR 35 KDA SUBUNIT-RELATED PROTEIN 1-RELATED; 1. DR PANTHER; PTHR12620; U2 SNRNP AUXILIARY FACTOR, SMALL SUBUNIT; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF00642; zf-CCCH; 1. DR PRINTS; PR01848; U2AUXFACTOR. DR SMART; SM00361; RRM_1; 1. DR SMART; SM00356; ZnF_C3H1; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS50103; ZF_C3H1; 2. DR Genevisible; Q15695; HS. PE 1: Evidence at protein level; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..479 FT /note="U2 small nuclear ribonucleoprotein auxiliary factor FT 35 kDa subunit-related protein 1" FT /id="PRO_0000081999" FT DOMAIN 203..309 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT ZN_FING 171..199 FT /note="C3H1-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 311..338 FT /note="C3H1-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 1..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..405 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 406..429 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 444..466 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15696" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15696" FT CROSSLNK 67 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15696" FT CONFLICT 135 FT /note="K -> E (in Ref. 3; BAG36348)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="K -> R (in Ref. 3; BAG36348)" FT /evidence="ECO:0000305" SQ SEQUENCE 479 AA; 57643 MW; 96F326694BD4E7C0 CRC64; MAALEKMTFP KKMTFPEKPS HKKYRAALKK EKRKKRRQEL ARLRDSGLSQ EEEEDTFIEE QQLEEEKLLE RERERLHEEW LLREQKAQEE FRIKKEKEEA AKKWLEEQER KLKEQWKEQQ RKEREEEEQK QQEKKEKEEA VQKMLDQAEN DLENSTTWQN PEPPVDFRVM EKDRANCPFY SKTGACRFGD RCSRKHNFPT SSPTLLIKSM FTTFGMEQCR RDDYDPDASL EYSEEETYQQ FLDFYEDVLP EFKNVGKVIQ FKVSCNLEPH LRGNVYVQYQ SEEECQAALS LFNGRWYAGR QLQCEFCPVT RWKMAICGLF EIQQCPRGKH CNFLHVFRNP NNEFWEANRD IYLSSDQTGS SFGKNSERRE KMGHHDHYYS RQRGRRNPSP DHTYKRNGES ERKKSSHRGK KSHKRTSKSR ERHNSPSRGR NRHRSWDQGR RSQSRRSHRS RSQSSSRCRS RGRRKSGNRD RTVQSPQSK //