PABP5_HUMAN
ID PABP5_HUMAN Reviewed; 382 AA.
AC Q96DU9; A8K240; Q5JQF4; Q6P529; Q9UFE5;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Polyadenylate-binding protein 5;
DE Short=PABP-5;
DE Short=Poly(A)-binding protein 5;
GN Name=PABPC5; Synonyms=PABP5;
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 [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=11374897; DOI=10.1006/geno.2001.6530;
RA Blanco P., Sargent C.A., Boucher C.A., Howell G., Ross M., Affara N.A.;
RT "A novel poly(A)-binding protein gene (PABPC5) maps to an X-specific
RT subinterval in the Xq21.3/Yp11.2 homology block of the human sex
RT chromosomes.";
RL Genomics 74:1-11(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-382.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP ALTERNATIVE INITIATION (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=23275553; DOI=10.1093/nar/gks1347;
RA Kazak L., Reyes A., Duncan A.L., Rorbach J., Wood S.R., Brea-Calvo G.,
RA Gammage P.A., Robinson A.J., Minczuk M., Holt I.J.;
RT "Alternative translation initiation augments the human mitochondrial
RT proteome.";
RL Nucleic Acids Res. 41:2354-2369(2013).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. May be involved in
CC cytoplasmic regulatory processes of mRNA metabolism. Can probably bind
CC to cytoplasmic RNA sequences other than poly(A) in vivo (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96DU9; Q9BPZ3: PAIP2; NbExp=3; IntAct=EBI-2880076, EBI-2957445;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix
CC {ECO:0000269|PubMed:23275553}. Note=Co-fractionates with mtDNA and co-
CC immunoprecipitates with the mitochondrial poly(A) polymerase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DU9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DU9-2; Sequence=VSP_047456;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain and in a range of adult
CC tissues.
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DR EMBL; AJ278963; CAC42826.1; -; Genomic_DNA.
DR EMBL; AK290105; BAF82794.1; -; mRNA.
DR EMBL; AL662874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471115; EAX02776.1; -; Genomic_DNA.
DR EMBL; BC063113; AAH63113.1; -; mRNA.
DR EMBL; AL122118; CAB59276.1; -; mRNA.
DR CCDS; CCDS14460.1; -. [Q96DU9-1]
DR PIR; T34543; T34543.
DR RefSeq; NP_543022.1; NM_080832.2. [Q96DU9-1]
DR AlphaFoldDB; Q96DU9; -.
DR SMR; Q96DU9; -.
DR BioGRID; 126753; 137.
DR IntAct; Q96DU9; 4.
DR STRING; 9606.ENSP00000308012; -.
DR iPTMnet; Q96DU9; -.
DR PhosphoSitePlus; Q96DU9; -.
DR BioMuta; PABPC5; -.
DR DMDM; 28201851; -.
DR EPD; Q96DU9; -.
DR jPOST; Q96DU9; -.
DR MassIVE; Q96DU9; -.
DR MaxQB; Q96DU9; -.
DR PaxDb; Q96DU9; -.
DR PeptideAtlas; Q96DU9; -.
DR PRIDE; Q96DU9; -.
DR ProteomicsDB; 76329; -. [Q96DU9-1]
DR Antibodypedia; 398; 97 antibodies from 20 providers.
DR DNASU; 140886; -.
DR Ensembl; ENST00000312600.4; ENSP00000308012.3; ENSG00000174740.8. [Q96DU9-1]
DR GeneID; 140886; -.
DR KEGG; hsa:140886; -.
DR MANE-Select; ENST00000312600.4; ENSP00000308012.3; NM_080832.3; NP_543022.1.
DR UCSC; uc004efg.4; human. [Q96DU9-1]
DR CTD; 140886; -.
DR GeneCards; PABPC5; -.
DR HGNC; HGNC:13629; PABPC5.
DR HPA; ENSG00000174740; Tissue enhanced (adrenal gland, ovary).
DR MIM; 300407; gene.
DR neXtProt; NX_Q96DU9; -.
DR OpenTargets; ENSG00000174740; -.
DR PharmGKB; PA32884; -.
DR VEuPathDB; HostDB:ENSG00000174740; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000162668; -.
DR HOGENOM; CLU_012062_22_6_1; -.
DR InParanoid; Q96DU9; -.
DR OMA; KCIDNRA; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; Q96DU9; -.
DR TreeFam; TF300458; -.
DR PathwayCommons; Q96DU9; -.
DR SignaLink; Q96DU9; -.
DR BioGRID-ORCS; 140886; 10 hits in 693 CRISPR screens.
DR ChiTaRS; PABPC5; human.
DR GenomeRNAi; 140886; -.
DR Pharos; Q96DU9; Tdark.
DR PRO; PR:Q96DU9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96DU9; protein.
DR Bgee; ENSG00000174740; Expressed in adrenal tissue and 101 other tissues.
DR ExpressionAtlas; Q96DU9; baseline and differential.
DR Genevisible; Q96DU9; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; Mitochondrion; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..382
FT /note="Polyadenylate-binding protein 5"
FT /id="PRO_0000081705"
FT DOMAIN 18..96
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 106..182
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 199..276
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 302..378
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047456"
FT VARIANT 314
FT /note="N -> S (in dbSNP:rs7050077)"
FT /id="VAR_054049"
SQ SEQUENCE 382 AA; 43331 MW; 23B34751780C602B CRC64;
MGSGEPNPAG KKKKYLKAAL YVGDLDPDVT EDMLYKKFRP AGPLRFTRIC RDPVTRSPLG
YGYVNFRFPA DAEWALNTMN FDLINGKPFR LMWSQPDDRL RKSGVGNIFI KNLDKSIDNR
ALFYLFSAFG NILSCKVVCD DNGSKGYAYV HFDSLAAANR AIWHMNGVRL NNRQVYVGRF
KFPEERAAEV RTRDRATFTN VFVKNIGDDI DDEKLKELFC EYGPTESVKV IRDASGKSKG
FGFVRYETHE AAQKAVLDLH GKSIDGKVLY VGRAQKKIER LAELRRRFER LRLKEKSRPP
GVPIYIKNLD ETINDEKLKE EFSSFGSISR AKVMMEVGQG KGFGVVCFSS FEEATKAVDE
MNGRIVGSKP LHVTLGQARR RC
