wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleolar protein 56 (Q9SGT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin 1
- rRNA 2'-O-methyltransferase fibrillarin 2
- Uncharacterized protein At3g06530
- Protein SLOW WALKER 1
- U3 small nucleolar RNA-associated protein 18 homolog
- Probable nucleolar protein 5-2
- Nucleolar protein
- Probable nucleolar protein 5-1
- Bystin
- H/ACA ribonucleoprotein complex subunit 4
Sequence:
MAMYVIYESSSGYGLFEVHGLDEIGQNTEAVRTSVSDLSRFGRVVQLTAFHPFESALDALNQVNAVSEGVMTDELRSFLELNLPKVKEGKKPKFSLGLAEPKLGSHIFEATKIPCQSNEFVLELLRGVRQHFDRFIKDLKPGDLEKSQLGLAHSYSRAKVKFNVNRVDNMVIQAIFMLDTLDKDINSFAMRVREWYSWHFPELVKIVNDNYLYARVSKMIDDKSKLTEDHIPMLTEVLGDEDKAKEVIEAGKASMGSDLSPLDLINVQTFAQKVMDLADYRKKLYDYLVTKMSDIAPNLAALIGEMVGARLISHAGSLTNLAKCPSSTLQILGAEKALFRALKTRGNTPKYGLIFHSSFIGRASAKNKGRIARYLANKCSIASRIDCFADGATTAFGEKLREQVEERLEFYDKGVAPRKNVDVMKEVIENLKQEEEGKEPVDASVKKSKKKKAKGEEEEEVVAMEEDKSEKKKKKEKRKMETAEENEKSEKKKTKKSKAGGEEETDDGHSTKKKKKKSKSAE
Protein: KIN17 protein (O76926)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGRAEVGTPKYLANKMKSKGLQKLRWYCQMCEKQCRDENGFKCHTMSESHQRQLLLFADNPGKFLHSFSKEFSDGYMELLRRRFGTKRTSANKIYQEYIAHKEHIHMNATRWLTLSDYVKWLGGLGKCIADETEKGWFVTYIDRSPEAMERQAKXDRKEKMEKDDEERMADFIEQQIKNAKAKDGEEDEGQEKFTELKREENEPLKLDIRLEKKFQPDTVLGKSALAKRPAPEAEEKVFKKPKS
Protein: RNA exonuclease 2 (H0YGR4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGRFGARGVREGGAAMAAGESMAQRMVWVDLEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTITLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKIDEKKRKIIENGENEKTVS
Protein: CCCH-type zinc finger protein oma-2 (Maturation oocyte expansion protein 2) (Oocyte maturation defective protein 2) (Q23359)
Organism: Caenorhabditis elegans
Function: Zinc-finger RNA-binding protein that binds to 5'-UA[AU]-3' motifs in the 3'-UTR of maternal mRNAs to suppress translation in oocytes and embryos. Acts redundantly with oma-1 to control the temporal expression and distribution of maternal proteins and thereby promote meiotic progression, oocyte maturation, fertilization and embryonic development. Also, together with oma-1, is involved in P-granule distribution during embryonic development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:16611242}. Cytoplasmic granule {ECO:0000269|PubMed:12296824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12296824}. Note=Expressed in cytoplasmic P-granules following fertilization and in developing oocytes. Expression ceases in P-granules in 2-cell stage embryos. Expressed in the centrosome after the 2-cell stage of embryogenesis, during the early cleavage stage, and also at later blastula stages. {ECO:0000269|PubMed:12296824}.
Interaction partners:
- C-type lectin domain-containing protein 87
- Embryonic mRna
- glutamine--fructose-6-phosphate transaminase
- Chondroitin proteoglycan 1
- G2/mitotic-specific cyclin-B
- Protein mom-2
- Uncharacterized protein EEED8.3
- C-type lectin domain-containing protein 91
- Pumilio domain-containing protein 5
- CCCH-type zinc finger protein oma-1
Sequence:
MDMLKENVIQNNEARTESSVEPSHPDMMETVPEEQQKPISHIDDLLSETANLMAVKEQLLKEIAENEHIHSMQMRALQNLPQEAILPLQYHADPRRRHRMQKPESYKTVICQAWLESKTCAFAENCRFAHGEEELRPSLIEARQNNKYRTKLCDKYTTTGLCPYGKRCLFIHPDNGPNAYIRADKLFEVSQRHALADLRDQMEHHIMNGGRSTAGPQQFDMFARPCTPDEPAANMPLGPTPVSIRGPRYELPSKKPLETEEAGNRPPSSWPLDPSTFFALDSLNMATRPISPFESMLIGAAGNMQYSMLGKQSTPGGVSGYSSSGSTPSQDSDSSPLTAASAAADAACQANSESAQSILLKSINNPMIGNETTLPIPGLDQLAMDIAKHLELW
Protein: CUGBP Elav-like family member 3 (CELF-3) (Bruno-like protein 1) (CAG repeat protein 4) (CUG-BP- and ETR-3-like factor 3) (ELAV-type RNA-binding protein 1) (ETR-1) (Expanded repeat domain protein CAG/CTG 4) (RNA-binding protein BRUNOL-1) (Trinucleotide repeat-containing gene 4 protein) (Q5SZQ8)
Organism: Homo sapiens (Human)
Function: RNA-binding protein involved in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- CCAAT/enhancer-binding protein delta
- Ribonucleoside-diphosphate reductase subunit M2
- Troponin T, cardiac muscle
- Ribonucleoside-diphosphate reductase large subunit
Sequence:
MKEPDAIKLFVGQIPRHLEEKDLKPIFEQFGRIFELTVIKDKYTGLHKGCAFLTYCARDSALKAQSALHEQKTLPGMNRPIQVKPADSESRGEDRKLFVGMLGKQQTDEDVRKMFEPFGTIDECTVLRGPDGTSKGCAFVKFQTHAEAQAAINTLHSSRTLPGASSSLVVKFADTEKERGLRRMQQVATQLGMFSPIALQFGAYSAYTQALMQQQAALVAAHSAYLSPMATMAAVQMQHMAAINANGLIATPITPSSGTSTPPAIAATPVSAIPAALGVNGYSPVPTQPTGQPAPDALYPNGVHPYPAQSPAAPVDPLQQAYAGMQHYTAAYPAAYSLVAPAFPQPPALVAQQPPPPPQQQQQQQQQQQQQQQREGPDGCNIFIYHLPQEFTDSEILQMFVPFGHVISAKVFVDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: Solute carrier family 17 member 3 (A0A0G2JY28)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MATVVELSPTSEQCEFVLGLPVNKKTPPRKVPSLCSMRYSIAFIAHICNFTLIAQNSIISITMVAMVNNTDQPSHLNSSTEWFPDGLNGDQHEASKHLSIKGAGYGGQFALWQKWAPPNERSRLCSIAMSGMILGIFAVLLVGGIISEALGWPFVFYIFGSIGVVCCLLWLILVYDDPVSHPWISSPEKEYILSSLDQQFNSEEQPLPIKAMLKSLPLWSMCLCSMTHQWLVNTLIIYTPTYISSVFKVNIRDNGLLSSLPFFVAWVIGILGGLLADFLLSKNFRLITVRKIITILGNTPPAALVVALPYVQSSYIATTTFLTLSCGLSPLCQSGVYINALDIAPRYASLLMGTSRGLAHSSAVMVPIVAGFFLNQDSEFGWRNFFFVLFAINLFGLIIYLVFAKADIQEWARERKLTRL
Protein: Phytyl ester synthase 1, chloroplastic (EC 2.3.1.-) (Q9ZVN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyltransferase involved in fatty acid phytyl ester synthesis in chloroplasts, a process required for the maintenance of the photosynthetic membrane integrity during abiotic stress and senescence. Exhibits phytyl ester synthesis and diacylglycerol acyltransferase activities with broad substrate specificities, and can employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl donors.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653, ECO:0000269|PubMed:22623494}.
Interaction partners:
- Tocopherol cyclase, chloroplastic
- Alternative NAD
- Probable plastid-lipid-associated protein 1, chloroplastic
- Acyl carrier protein 1, mitochondrial
- Probable plastid-lipid-associated protein 3, chloroplastic
- F16N3.9 protein
- Phytol kinase 1, chloroplastic
- Probable plastid-lipid-associated protein 4, chloroplastic
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MATCSSSLLVLPNLRLSSNQRRNFKVRAQISGENKKATSLEPVNNNGSVSLSTTVQNQKGANEVNGKGKSKRKIVSDEIELLWDDGYGSKSVKDYFAAAKEILKADGGPPRWFSPVDCGRPVEDAPTLLFLPGMDGTGMGLVPHHKALGKAFHVSCLHIPVLDRTPFEGLLKVVEDVLRQEQATRPNKPIYLVGDSFGGCLALAVAARNRSLDLVLILVNPATSFDRSPLQPLLPILEMVPEELHFTVPYALSFIMGDPIKMATLGIDNQLPTGVKIEKLRQRLTKTMLPLLSELGGIIPRETLLWKLKLLRSGCAYANSRIHAVQAEVLVLASGKDMMLPSQEEAKRLHGLLKNCSVRCFKDNGHTLLLEDSISLLTVIKGTGKYRRSWRYDLVSDFLPPSKGELAYALDEVLGFLRNAVGSVFFSTMEDGKIVKGLAGVPDKGPVLLVGYHMLMGLELGPMSEAFIKEKNILFRGMAHPVLYSDNDPAKAFDYGDWIKVFGAYPVTATNLFKLLDSKSHVLLFPGGAREALHNRGEQYKLIWPEQQEFVRMAARFGATIVPFGTVGEDDIAELVLDYNDLMKIPILNDYITEVTRDTKQFKLREESEGEVANQPLYLPGLIPKVPGRFYYLFGKPIETKGRPELVKDKEEANQVYLEVKAEVENSIAYLLKKREEDPYRSVLDRLNYSLTHTTATHVPSFEP
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 2 (EC 1.1.1.44) (Q9FWA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Required for guided growth of the male gametophytes and interaction between the pollen tube and the ovule.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26941195}. Peroxisome {ECO:0000269|PubMed:26941195}.
Interaction partners:
- Probable 6-phosphogluconolactonase 4
- Probable 6-phosphogluconolactonase 5
- 6-phosphogluconolactonase 3, chloroplastic
- Probable 6-phosphogluconolactonase 2
- Probable 6-phosphogluconolactonase 1
- Ribulose-5-phosphate-3-epimerase, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Probable ribose-5-phosphate isomerase 2
- Ribulose-phosphate 3-epimerase
- Ribulose-phosphate 3-epimerase
Sequence:
MAVQPTRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLPLYGFHDPESFVKSIQKPRVIIMLVKAGSPVDQTIKTLSAYLEKGDCIVDGGNEWYENTERREKAVAENGFLYLGMGVSGGEEGARNGPSMMPGGSYEAYKNIEDIVLKVAAQVRDSGPCVTYIGKGGSGNFVKMVHNGIEYGDMQLIAEAYDVLKSVGKLSNEELHSVFSDWNKGELESFLVEITADIFGIKDDKGDGHLVDKVLDKTGMKGTGKWTVQQAAELSVPAPTIESSLDARFLSGLKDERVQAAKVFKAGGFGDILTDQKVDKKQLVDDVRKALYASKICSYAQGMNLIRAKSIEKGWGLKLGELARIWKGGCIIRAIFLDRIKQAYDRNAELANLLVDPEFAKEIIERQSAWRRVVCLAINSGISTPGMSASLAYFDSYRRERLPANLVQAQRDYFGAHTYERTDVEGSFHTEWFKIARQSKI
Protein: Probable pectinesterase/pectinesterase inhibitor 34 [Includes: Pectinesterase inhibitor 34 (Pectin methylesterase inhibitor 34); Pectinesterase 34 (PE 34) (EC 3.1.1.11) (Pectin methylesterase 34) (AtPME34)] (Q9M3B0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Serine carboxypeptidase-like 41
- Probable pectate lyase 20
Sequence:
MGYERLGPSGATGSVTTSTTTAPILNQVSTSEQPENNNRRSKKKLVVSSIVLAISLILAAAIFAGVRSRLKLNQSVPGLARKPSQAISKACELTRFPELCVDSLMDFPGSLAASSSKDLIHVTVNMTLHHFSHALYSSASLSFVDMPPRARSAYDSCVELLDDSVDALSRALSSVVSSSAKPQDVTTWLSAALTNHDTCTEGFDGVDDGGVKDHMTAALQNLSELVSNCLAIFSASHDGDDFAGVPIQNRRLLGVEEREEKFPRWMRPKEREILEMPVSQIQADIIVSKDGNGTCKTISEAIKKAPQNSTRRIIIYVKAGRYEENNLKVGRKKINLMFVGDGKGKTVISGGKSIFDNITTFHTASFAATGAGFIARDITFENWAGPAKHQAVALRIGADHAVIYRCNIIGYQDTLYVHSNRQFFRECDIYGTVDFIFGNAAVVLQNCSIYARKPMDFQKNTITAQNRKDPNQNTGISIHASRVLAASDLQATNGSTQTYLGRPWKLFSRTVYMMSYIGGHVHTRGWLEWNTTFALDTLYYGEYLNSGPGSGLGQRVSWPGYRVINSTAEANRFTVAEFIYGSSWLPSTGVSFLAGLSI
Protein: Sorulation-regulated protein 2 (Q12282)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Spore wall {ECO:0000305|PubMed:3323843}. Secreted, cell wall {ECO:0000305|PubMed:10383953, ECO:0000305|PubMed:9613572}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MLGLYLSSLFFAFFMAQVFATKYSITFTSDEYEEDETGQNEPGPLVFHLDKNSLPPALLNQMEFNPYLVLADLPEEPRAVDSQEHTDTVLASKSVIDFLLEDPLTIVEHKKFSQIESILHEIMEDSIQKKVGADEVFEEIPKPKIYAYEDILVTNMSIINNSEMPTSTATLTSTISYLSSTTSLALSTGVTSVEIFPTITPGNITTIGGYENSSSSLMPSMGILSFLFGLYLLLHP
Protein: 3-isopropylmalate dehydrogenase 2, chloroplastic (3-IPM-DH 2) (AtIMDH2) (AtIMDH3) (IMDH 2) (EC 1.1.1.85) (Beta-IPM dehydrogenase 2) (Isopropylmalate dehydrogenase 2) (AtIMD2) (P93832)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in leucine biosynthesis; catalyzes the oxidative decarboxylation step in leucine biosynthesis (primary metabolism). Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate, 3-IPM) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Required during pollen development and involved in embryo sac development.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9FMT1}.
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 1
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 3-isopropylmalate dehydratase small subunit 2
- Acetolactate synthase, chloroplastic
- Acetolactate synthase small subunit 1, chloroplastic
- Acetolactate synthase small subunit 2, chloroplastic
- Threonine dehydratase biosynthetic, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
Sequence:
MAAALQTNIRTVKVPATFRAVSKQSLAPFRVRCAVASPGKKRYTITLLPGDGIGPEVVSIAKNVLQQAGSLEGVEFNFREMPIGGAALDLVGVPLPEETISAAKESDAVLLGAIGGYKWDNNEKHLRPEKGLLQIRAALKVFANLRPATVLPQLVDASTLKREVAEGVDLMVVRELTGGIYFGEPRGIKTNENGEEVGFNTEVYAAHEIDRIARVAFETARKRRGKLCSVDKANVLEASILWRKRVTALASEYPDVELSHMYVDNAAMQLVRDPKQFDTIVTNNIFGDILSDEASMITGSIGMLPSASLSDSGPGLFEPIHGSAPDIAGQDKANPLATILSAAMLLKYGLGEEKAAKRIEDAVLVALNNGFRTGDIYSAGTKLVGCKEMGEEVLKSVDSQVPASV
Protein: Nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) (EC 2.7.7.18) (A0A8I5ZK56)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRDNNIGIRGLHLDQQLQLLPMDSSKKTEVVLLACGSFNPITNMHLRLFELAKDYLNATGEYKVIKGIISPVGDAYKKKGLIPAHHRIIMAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKLATGSRSHPQSSPVLERPGRKRKWADQKQDSSPQKPQEPKPTGVPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIRRALRRGQSIRYLVPDLVQEYIEEHDLYNSESEDRNAGVTLAPLQRNTSEAKHNHSTR
Protein: L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) (P42123)
Organism: Rattus norvegicus (Rat)
Function: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+).
Subcellular location: Cytoplasm. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07195}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- L-lactate dehydrogenase A chain
- Aspartate aminotransferase, cytoplasmic
- Pyruvate kinase PKM
- Aspartate aminotransferase, mitochondrial
- Pyruvate kinase PKLR
- Pyruvate carboxylase, mitochondrial
- L-lactate dehydrogenase C chain
- D-lactate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Malic enzyme
Sequence:
MATLKEKLIAPVADDETAVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCTIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVDSAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLRKSADTLWDIQKDLKDL
Protein: Imidazole glycerol phosphate synthase subunit HisF (EC 4.3.2.10) (IGP synthase cyclase subunit) (IGP synthase subunit HisF) (ImGP synthase subunit HisF) (IGPS subunit HisF) (P62450)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}.
Interaction partners:
- 1-
- Phosphoribosyl-AMP cyclohydrolase
- Imidazole glycerol phosphate synthase subunit HisH
- Imidazoleglycerol-phosphate dehydratase
- Histidinol dehydrogenase
- ATP phosphoribosyltransferase
- Histidinol-phosphate aminotransferase
- Aminotransferase, putative
- Cytidine/deoxycytidylate deaminase family protein
- Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative
Sequence:
MLSKRIIPCLDVRAGRLTKGVKFEGNVDIGDPVATARRYYEEGADEIVFYDITASHEDRGIFLDVVERVASEIFIPFSVGGGINTVDDMRAVLMAGAEKVSVNSGAVKTPDIISQGAAAFGSQAIVVGMDVKQVEKSATIPSGYEIVIHGGRKYMGMDAIEWAKTCESLGAGELCVNSIDADGTKDGYELTLTRMISDAVTIPVIASGGAGSPEHMYDALTRGGASAALIASIVHYGTYTIPDLKRRISGMGAKMRMVW
Protein: Limb region 1 protein (Q9JIT0)
Organism: Mus musculus (Mouse)
Function: Putative membrane receptor.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- RING finger protein 32
- Sonic hedgehog protein
Sequence:
MEGQDEVSAREQHFHSQVRESTICFLLFAILYIVSYFIIIRYKRKSDEQEDEDAVVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLAFPHNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLLLLALLILGMVWVASALIDSDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPAILEDLDEQIYMITLEEEALQRRLHGLSSSVEYNVMELEQELENVKILKTKLERRKKASAWERNLVYPAVMVLLLIETSISVLLVACNILCLLVDETAMPKGTRGPGIGSASLSTFGFVGAALEIILIFYLMVSSVVGFYSLRFFGNFTPKKDDTTMTKIIGNCVSILVLSSALPVMSRTLGITRFDLLGDFGRFNWLGNFYIVLSYNLLFAIMTTLCLIRKFTSAVREELFKALGLHKLHLSDTSRDSETTKPSANGHQKAL
Protein: Damage-inducible mutagenesis protein (Q92ZJ8)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MSAAVATSNPVLHELRGKIASLEGAGSRNRSILPFGVPELDAQLPGGGLAFGALHEVAGGGNGSIDGAAAALFIGGIAARTTGKVVWCLTRFDLFFPALAKVGLHPDRVIFVECYKEETVLASFEEALRYGGLGAVVAELVRLPMTASRRLQLAAEKSGTLGLVIRRWRRQTEASDFGMPTAAATRWRISVLPSEPLPVPGVGRARWLAELMRVRAGEGGEFIIGACDGQGRICLSSETANGPDQAGRSFAIGRKAAGGHRQERFEAMDFGS
Protein: 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.14.139) (7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase) (CYPVIIIB1) (Cytochrome P450 8B1) (Sterol 12-alpha-hydroxylase) (O02766)
Organism: Oryctolagus cuniculus (Rabbit)
Function: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis. Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1400444}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:1400444}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVLWGLLGALLMVMVGWLCLPGLLRQRRPQEPPLDKGSIPWLGHAMTFRKNMLEFLKHMRSKHGDVFTVQLGGQYFTFVMDPVSFGPILKDGQRKLDFVEYAKGLVLKVFGYQSIEGDHRMIHLASTKHLMGHGLEELNKAMLDSLSLVMLGPEGRSPDASRWHEDGLFHFCYGVMFKAGYLSLFGHTSDKRQDLLQAEEIFIKFRRFDLLFPRFVYSLLGPREWREVGRLQQLFHELLSVKHNPEKDGMSNWIGHMLQYLSEQGVAPAMQDKFNFMMLWASQGNTGPASFWALIYLLKHPEAMRAVKEEATRVLGEPRLEAKQSFTVQLSALQHIPVLDSVMEETLRLGAAPTLYRVVQKDILLKMASGQECLLRQGDIVTLFPYLSVHMDPDIHPEPTTFKYDRFLNPNGSRKVDFYKAGQKIHHYTMPWGSGVSICPGRFFALSEMKLFVLLMVQYFDLELVDPNTPVPPIDPRRWGFGTMQPTHDVRIRYRLKPLE
Protein: RNA-binding protein, putative (Q389L2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVDPSVLLAYCPTHDFQRIEAVVREWPGVEAVGSLRTKEGKENTTSVFIKFSDKEAARDATSRIDAVPGLVRKIEEPKAKQRMRKMGKNMLIDPAMEIFSFGATDKGDVTFNERKREGNRRRHPSVIGPGSGSERTSNKGNNAIRHHPFTPPARASVALVDNVPFNMTNDQVARLFSPFGELIDLSRYETMAMVFYRSPDSVLKCIQQLNGKTVKGKIITVSSGAITIPGLLAAVVGVQVHN
Protein: Cleavage stimulation factor subunit 2 (CF-1 64 kDa subunit) (Cleavage stimulation factor 64 kDa subunit) (CSTF 64 kDa subunit) (CstF-64) (P33240)
Organism: Homo sapiens (Human)
Function: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11598190, ECO:0000269|PubMed:32816001}. Note=Localized with DDX1 in cleavage bodies. {ECO:0000269|PubMed:11598190}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage stimulation factor subunit 3
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulation factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 6
- Pre-mRNA cleavage complex 2 protein Pcf11
- Pre-mRNA 3'-end-processing factor FIP1
Sequence:
MAGLTVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGETISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLIAGNPQPVHGAGPGSGSNVSMNQQNPQAPQAQSLGGMHVNGAPPLMQASMQGGVPAPGQMPAAVTGPGPGSLAPGGGMQAQVGMPGSGPVSMERGQVPMQDPRAAMQRGSLPANVPTPRGLLGDAPNDPRGGTLLSVTGEVEPRGYLGPPHQGPPMHHVPGHESRGPPPHELRGGPLPEPRPLMAEPRGPMLDQRGPPLDGRGGRDPRGIDARGMEARAMEARGLDARGLEARAMEARAMEARAMEARAMEARAMEVRGMEARGMDTRGPVPGPRGPIPSGMQGPSPINMGAVVPQGSRQVPVMQGTGMQGASIQGGSQPGGFSPGQNQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (FP) (SDH1b) (P47052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable minor catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q00711}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00711}; Matrix side {ECO:0000250|UniProtKB:Q00711}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH4
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MLSLKKGITKSYILQRTFTSSSVVRQIGEVKSESKPPAKYHIIDHEYDCVVVGAGGAGLRAAFGLAEAGYKTACLSKLFPTRSHTVAAQGGINAALGNMHPDDWKSHMYDTVKGSDWLGDQDAIHYMTREAPKSVIELEHYGMPFSRTEDGRIYQRAFGGQSKDFGKGGQAYRTCAVADRTGHAMLHTLYGQALKNNTHFFIEYFAMDLLTHNGEVVGVIAYNQEDGTIHRFRAHKTVIATGGYGRAYFSCTSAHTCTGDGNAMVSRAGFPLEDLEFVQFHPSGIYGSGCLITEGARGEGGFLLNSEGERFMERYAPTAKDLASRDVVSRAITMEIRAGRGVGKNKDHILLQLSHLPPEVLKERLPGISETAAVFAGVDVTQEPIPVLPTVHYNMGGIPTKWTGEALTIDEETGEDKVIPGLMACGEAACVSVHGANRLGANSLLDLVVFGRAVANTIADTLQPGLPHKPLASNIGHESIANLDKVRNARGSLKTSQIRLNMQRTMQKDVSVFRTQDTLDEGVRNITEVDKTFEDVHVSDKSMIWNSDLVETLELQNLLTCATQTAVSASKRKESRGAHAREDYAKRDDVNWRKHTLSWQKGTSTPVKIKYRNVIAHTLDENECAPVPPAVRSY
Protein: Vitronectin (VN) (S-protein) (Serum-spreading factor) (P29788)
Organism: Mus musculus (Mouse)
Function: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Integrin alpha-V
- Plasminogen activator inhibitor 1
- Urokinase plasminogen activator surface receptor
- Integrin beta-3
- Fibronectin
- Integrin alpha-IIb
- Integrin beta-1
- Urokinase-type plasminogen activator
- Nidogen-1
- Plasminogen
Sequence:
MAPLRPFFILALVAWVSLADQESCKGRCTQGFMASKKCQCDELCTYYQSCCADYMEQCKPQVTRGDVFTMPEDDYWSYDYVEEPKNNTNTGVQPENTSPPGDLNPRTDGTLKPTAFLDPEEQPSTPAPKVEQQEEILRPDTTDQGTPEFPEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPGYPRNISEGFSGIPDNVDAAFALPAHRYSGRERVYFFKGKQYWEYEFQQQPSQEECEGSSLSAVFEHFALLQRDSWENIFELLFWGRSSDGAREPQFISRNWHGVPGKVDAAMAGRIYVTGSLSHSAQAKKQKSKRRSRKRYRSRRGRGHRRSQSSNSRRSSRSIWFSLFSSEESGLGTYNNYDYDMDWLVPATCEPIQSVYFFSGDKYYRVNLRTRRVDSVNPPYPRSIAQYWLGCPTSEK