wanglab/gogpt-training-data huggingface dataset:
Protein: Phytochrome A-associated F-box protein (Empfindlicher im dunkelroten Licht protein 1) (Q8LEA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Negative regulator of the phyA signaling pathway that shifts the responsiveness of the phyA signaling system associated with hypocotyl elongation from red to far-red wavelength.
Subcellular location: Nucleus {ECO:0000269|PubMed:11316788}.
Interaction partners:
- SKP1-like protein 1A
- Nuclear cap-binding protein subunit 2
- EID1-like F-box protein 3
- Nuclear cap-binding protein subunit 1
- EID1-like F-box protein 1
- Small nuclear ribonucleoprotein Sm D2
- EID1-like F-box protein 2
- Transportin MOS14
- 30-kDa cleavage and polyadenylation specificity factor 30
- Phytochrome A
Sequence:
MAESVFSCIPEDVVFNIFFKLQDDPRNWARLACVCTKFSSIVRNVCCKTQCYSAIPTVISDLLPLPPSAAASASSSTAADSSLTPPGGWASLYKLAVCCPGLFHAGILLENSDFGLERELGPDQNLDPKPTTTDLALNDEEVSKPVGSGLETTSFWSLYDDLYTDTIPAPPPEDSIDDQEEEIETSEIRPGRDLPVRKRRKICRSLGSHLASGGWNLSREQGNKLLASRFRGDCLYICNWPGCIHVEEKRNYMLFRGVFKDFKRSRVWRTINDGNRSKTSGLKCAFCLCDETWDLHSSFCLRRVFGFHDDGEPVVRAYVCENGHVSGAWTALPLYT
Protein: Gigas, isoform A (Q9VW83)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- TBC1 domain family member 7
- LD23779p
- GTP-binding protein Rheb homolog
- RAC serine/threonine-protein kinase
- Raptor, isoform B
- GH04846p
- non-specific serine/threonine protein kinase
- Protein charybde
- non-specific serine/threonine protein kinase
- Ribosomal protein S6 kinase
Sequence:
MNSKDKSKFKLFLKSLPAGYVGERTLRPEFERELRPEQPVAQRCRMLKELGDTQLHNFNLDESAITILFNLTNDLIVPNKPAETRQIALSFYKRLIHTQYKNLTIMREKFFLVIQNHEAREDLRHLLELLDTLTDNGKDITNFEEKIGKFMLLWIPAITEANLLTPYLDILVNLIKFNAAHLDKDILVGIVQNACDLSCSVTVNEIGLQCLTILEMVIGYTIFPSEPLPQCITTLCRTVNHAPYCPSSFKIMKNLLGTQLGYHSMKMMCSILNDRALYDDAHLLRGAVFHLNMNIFGSNIIFQVSPMTYATNVLTAFLRALDSRQVIVTFEVILSVRMVITKRQLSEIIWDLICDIMSSIVSNIEYYEEVNINKDRLHHLQINFHENIDCIEKLLQQDRSQILGNVERIYDLIERVADRRPEASVLALIEYRSRRVTATRPDWLQVLAQFVRRYYRMSNVNVRIKTIEALVQIMDQNRACYEEEILSRVVLVHLSHIHLESSVQVRVAVARALSNFATHCDTKRCMDLLDILEALINRPFEHTRHGSSSGEGTLAEVTFGLVNNESEISDIIAAVDGLVKVFAIKLHRLPGIHALKIFNILMDHLELHYERPKIFEHISVVRYKIFAWLLKARANGSYHIGYPEGSTEVVKFSPYLGIDSPLLPQAHPTAISIRRVCKLIVRCLEHDTDYQVFQLVIRELPKVLQNKALVQGNDIEELANTLLKINLVSNNKFKRPTDEFHALVLPAIASLVIYHESLQPQQHYGIITALNSRVLTGIASVCINTMTILILEMPEALMRKLPDVLLQMSKMSDTNALATPVLEFLSLLIHLSKHLFANFTSMHNMYVFAITLPYTKPHRYDHYTVSLAHHVIAGWFLKCKLELRRNCVNYIKSSIQSNAKMLSSDIVNLNSLNEDSSNRKRSTSLTERGSRNNANAWNDLEMRPQMNNGLRNFHAELAETCFDFLARHTYSPCPSMPKRLPAAEFLLKDGVSQTWLVGNNLVTITTSGCPSAPARSGLCERCAQLGKAPSISLNSKSLSDAAPPLSPERERRYTKVSLQHSSGNESAGSTELTSSSSSNSAAAGGHPHRQISNSSTASLDALSRRGSNPEALGSALGEGAHTGSNTSLLGNSLSQSSVSMSPSSGSVVQQPVCVRACTGWAEVLVRRPTGNVSWITRIQNPITNDCFGQELPFNNVVSLFLPTAHGGVFGPDNTIQAPPHTLADPEPEPEAEVNAATAPQASALRSRMVAKARALQRQEEIHSVGGNGNGNGNGNGSGNAPSTGGAAAIPIPRVPASGKRGKEAALCGSVSDGEADDDSLAFEDAQSRARNPVRRVNSSPEMSSSWRQSFLTNKPTPLSQEPVKTTADEPQSLLTLKKKTVQYSTKDMRVSCEAIPEEIAGSTPPSQAAALALQPESGTLPPKQHSADDVSSHVAGGSNLQAGGSTLKLGKPPLSPGQPPLLGTGRVTSFGGTSVPQPGALAKSSSSGSNGTNVGVITSDYDNGNNGNGDMMRGRSKTISVVREVNNGNTRPPPASSFRNFGAAKPPINTKLCMNPSFIFMQLYTTGQLGVTDEPLKVGPENSSAVSLIDLVPPFETHKIGVLYVGQGQCNNEVEILRNSHGSARYVEFLRNIGTLVSLKEAEQNNLFIMLDRNGADGKFAYIWKDDILQVTFHVATLMPTNLQDDPNCNEKKSHIGNDFVKIIYNESGEEYNLNTISGQFNYACVIVEPLDLNSNRVYVKARSEISKFVCHAEYRIVSDRSAPLLARQMALHANLASLVYQSVQKKHPYASNWLERLRKLKRLRSKLIEGLNSQQKSGSASSGIGINASAIGSDMDDQRGDFIKYT
Protein: Proteasome subunit alpha type (A0A1D8PRH6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome subunit beta
- 26S proteasome regulatory subunit 6A
- Proteasome subunit alpha type
- Proteasome regulatory particle lid subunit
- 26S proteasome regulatory subunit 7 homolog
- Proteasome subunit beta
- Proteasome regulatory particle lid subunit
Sequence:
MFRNNYDNDSVTYSPTGRLFQVEYALEAIKQGSAAVGLTSNDYVVLVALKRNAEELGSYQKKIIKIDDHMGVALAGLAPDARVLSNFLRKQAMQCKMVFNRPIQTYKAVLSIADKAQENTQTYGSRPYGVGLLIAGYDETGAHLFEFQPSGSVLEYFGAAIGARSQAARTYLERNLEEIKKCDDVEKLVLHGLYALRDTLSQDVELTFKNTSVSIVGKDQSFVSYDDENVQQWLDKLDSVSNARNRDGDDDEDGDEQEEGNATQAQEGEGTEAPAEDRMETDE
Protein: Eukaryotic translation initiation factor 5, putative (Q38BW8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit 8, putative
- Translation initiation factor, putative
- Elongation initiation factor 2 alpha subunit, putative
- RNA-binding protein, putative
- Translation initiation factor, putative
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit 7-like protein
Sequence:
MTSSMIPVDPDKRDDIYYRYKMPAIQTKVEGSGNGIKTVFPNIHDVCLAINRPEEVLMKYFQSEFGAQRTVSEKDDKFLIMGSHTEERVQEKVYDFIRQFVLCRSCRNPETQLSVERNKKGAPQVSMSCGACGKSMKLEDLGARYVTALATHFAKNPQAALRKGAGTAEARKKDKAQQEEAAAAAAAKLAVPVEKHVIMKSDLQDTREAPQEVLARFMRQCEGDYEEILRHSMELMSTYNLKDKMGPLLVLNAIVIAEKEFMAGLRRHTALLKRFSTLPDSVLYDASADETTKTERQKRKMQLQVAAMEECARICVQHLKPEQLVVALFVLFIEGVLEGESIKNWHNEGKPPSKVDPAVYAEMREAVEPLVVWLDGNKCVAA
Protein: Serine/threonine-protein kinase RAD53 (EC 2.7.12.1) (CHEK2 homolog) (Serine-protein kinase 1) (P22216)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.
Subcellular location: Nucleus {ECO:0000269|PubMed:8355715}.
Interaction partners:
- Serine/threonine-protein kinase MEC1
- Mediator of replication checkpoint protein 1
- Histone chaperone ASF1
- DNA repair protein RAD9
- Cell division control protein 7
- Securin
- Mitosis inhibitor protein kinase SWE1
- S-phase entry cyclin-5
- G2/mitotic-specific cyclin-2
- DNA damage response protein kinase DUN1
Sequence:
MENITQPTQQSTQATQRFLIEKFSQEQIGENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFINDKFKQCLEQNKVDRIRSNLKNTSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFAVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITDFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQMEQQLQEQDQEDQDGKIQGFKIPAHAPIRYTQPKSIEAETREQKLLHSNNTENVKSSKKKGNGRFLTLKPLPDSIIQESLEIQQGVNPFFIGRSEDCNCKIEDNRLSRVHCFIFKKRHAVGKSMYESPAQGLDDIWYCHTGTNVSYLNNNRMIQGTKFLLQDGDEIKIIWDKNNKFVIGFKVEINDTTGLFNEGLGMLQEQRVVLKQTAEEKDLVKKLTQMMAAQRANQPSASSSSMSAKKPPVSDTNNNGNNSVLNDLVESPINANTGNILKRIHSVSLSQSQIDPSKKVKRAKLDQTSKGPENLQFS
Protein: Eukaryotic translation initiation factor 3 subunit D-1 (eIF3d-1) (Eukaryotic translation initiation factor 3 subunit 7-1) (Eukaryotic translation initiation factor 3 subunit p66) (Q9VCK0)
Organism: Drosophila melanogaster (Fruit fly)
Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit G-1
- Eukaryotic translation initiation factor 3 subunit K
Sequence:
MSETINTAAQFPSFEKPTVQFNEKGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTNTSNNDKKYQNKYASSFGTGIQYSYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRNSRSGRGRNARGGLNTHGMTTLSGKNVKARDPRHGRGMGKKFGHRGPPPKMRESSVAVRADWASIEEMDFPRLIKLSLPNIKEGVDIVTCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTVGNVFATDAILATIMCSTRSNYSWDIVIEKVGDKVFMDKRDHTEFDLLTVNESSVEPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEPKYKFEESNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGEPQFMTIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGILRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDEGFQQVYNYAHNKI
Protein: GPN-loop GTPase QQT2 (EC 3.6.5.-) (Protein QUATRE QUART 2) (Q8W586)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17419841}. Nucleus {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:17419841}. Note=During interphase, mainly expressed in the cytoplasm and weakly in the nucleus. Associated with microtubules during cell division. {ECO:0000269|PubMed:17419841}.
Interaction partners:
- Transcriptional elongation regulator MINIYO
- GPN-loop GTPase QQT1
- GPN-loop GTPase 3
- Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog
- DNA-directed RNA polymerase II subunit 2
- DNA-directed RNA polymerase V subunit 5A
- U11/U12 small nuclear ribonucleoprotein 31 kDa protein
- tRNA-specific adenosine deaminase TAD3
- tRNA-specific adenosine deaminase TAD2
- Tubulin-folding cofactor E
Sequence:
MDPMESSSEQDIVEESQKLVDSLDKLRVSAASSSSNFKKKPIIIIVVGMAGSGKTSFLHRLVCHTFDSKSHGYVVNLDPAVMSLPFGANIDIRDTVKYKEVMKQYNLGPNGGILTSLNLFATKFDEVVSVIEKRADQLDYVLVDTPGQIEIFTWSASGAIITEAFASTFPTVVTYVVDTPRSSSPITFMSNMLYACSILYKTRLPLVLAFNKTDVADHKFALEWMEDFEVFQAAIQSDNSYTATLANSLSLSLYEFYRNIRSVGVSAISGAGMDGFFKAIEASAEEYMETYKADLDMRKADKERLEEERKKHEMEKLRKDMESSQGGTVVLNTGLKDRDATEKMMLEEDDEDFQVEDEEDSDDAIDEDDEDDETKHYYL
Protein: Protein misato homolog 1 (Q9BUK6)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of mitochondrial distribution and morphology. Required for mitochondrial fusion and mitochondrial network formation.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:17349998, ECO:0000269|PubMed:28554942}. Cytoplasm {ECO:0000269|PubMed:28544275, ECO:0000269|PubMed:28554942}.
Interaction partners:
Sequence:
MAGGAREVLTLQLGHFAGFVGAHWWNQQDAALGRATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGLYRDKQLDAAIAWQGKLTTHKEELYPKNPYLQDFLSAEGVLSSDGVWRVKSIPNGKGSSPLPTATTPKPLIPTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGFSGVGAKAAELLQDEYSGRGIITWGLLPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPVSFPYLHYDATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSLPDSLMQFGGATPWTPLSACGEPSGTRCFAQSVVLRGIDRACHTSQLTPGTPPPSALHACTTGEEILAQYLQQQQPGVMSSSHLLLTPCRVAPPYPHLFSSCSPPGMVLDGSPKGAAVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAGVEHDDVAELLQELQSLAQCYQGGDSLVD
Protein: U6 snRNA-associated Sm-like protein LSm3 (Q8IMX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365046}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm8
- Protein associated with topo II related - 1, isoform A
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm4
- Probable small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein G
Sequence:
MADETEQLSQVILPVKEPLDLIRLSLDEKVYVKMRNERELRGRLHAFDQHLNMVLGDAEETVTTVEIDEETYEEVYKTAKRTIPMLFVRGDGVILVSPPMRVG
Protein: Protein psiK (Q54DV5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Latrophilin receptor-like protein A
Sequence:
MKKTFIFLYCVVLFISTTLAVEMKKTQDFNLRIFDQHPKYNNNFEPENGVLTVNLVKSILNETTGIPELTTMSNLTTVNKQGRIYSPELFKYFFADNSDAPDRNNSGKNYPLDITLTMNLDDKSNYFYDNQEFFPIDGRGFDVDQQFRNYYDDESKANPKPYHNYHFCAKITNSRFTYKGFETFRFVGDDDVWVFIDRKLVVDLGGLHIAQEKTIDLTKLGLVVNKLYVIDFFYCERHTSRSTIRIETTIELQCPWYDFCGVCTGNGLSCCNVTRDCDDGNPCTIDLCPEPTAVFDLKDISANCRHQDRTPTDWSVTDKCNTGKCNVSTGIFVTNITKCIPQNSCKAEDHCDSGLGCIFKNLCTDVCSTGACVDGKCETKNSKICIDELDKGVEDKCYEYSCDPNVGCTKKPRCLQKSENYNPCLNSFCEVSTGECKNTTIPPNLCDCQCDGKLNKCQIKSCNADGSCKPLPSLEIDDKNPCTIDACDETTGVITHTLSNKCGGCSICNGVTGDCDPVDKKCDDGNRCTTEVCLLDKATNNGNCSSKPTTECDKGDVCMVYSCDTEKGCVETPRVCPSKGKCQVGKCVPGVGCKYEPRVCKADAFCLVAECDEIVGCIQFEKKCAADNGRCQAGICKNATATEEGTCESVDFDPKPFICKTAAVVSVGVAVGVAVGGAIALGVFIFAGKKGYDYWKASQGVTMATSNANPLYESNPSGGENPIYTSPN
Protein: Type VII secretion system accessory factor EsaA (P0C049)
Organism: Staphylococcus aureus (strain Newman)
Function: Component of the type VII secretion system (Ess). Provides together with EssB and other components such as EssC and EssE a secretion platform across the cytoplasmic membrane in the host.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q2G188}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKKKNWIYALIVTLIIIIAIVSMIFFVQTKYGDQSEKGSQSVSNKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKTPSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPINDFPELFTDTLVNSISANKDITKWFQTYNKSLLSANSDTFRVNTDYNVSTLIEKQNSLFDEHNTAMDKMLQDYKSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKEEYKQTVKENLDKLREIIQSQESPFSKGMIEDYRKQLTESLQDELANNKDLQDALNSIKMNNAQFAENLEKQLHDDIVKEPDTDTTFIYNMSKQDFIAAGLNEGEANKYEAIVKEAKRYKNEYNLKKPLAEHINLTDYDNQVAQDTSSLINDGVKVQRTETIKSNDINQLTVATDPHFNFEGDIKINGKKYDIKDQSVQLDTSNKEYKVEVNGVAKLKKDAEKDFLKDKTMHLQLLFGQANRQDEPNDKKATSVVDVTLNHNLDGRLSKDALSQQLSALSRFDAHYKMYTDTKGREDKPFDNKRLIDMMVDQVINDMESFKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQLENVKKTFAEEPQEPKIDKGKNDEFNTMSSNLDKEISRISEKSTQLLSDTQESKSIADSVSGQLNQVDNNVNKLHATGRALGVRANDLNRQMAKNDKDNELFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSYERAKGQMNFIKDDYSSKNHLWNNVITSGVIGTTGLVEGLIVGLIAMNKFHVLAGYRAKFILMVILTMMVFVLINTYLLRQVKSIGMFLMIAALGLYFVAMNNLKAAGQGVTNKISPLSYIDNMFFNYLNAEHPIGLVLVILTVLVIIGFVLNMFIKHFKKERLI
Protein: Sideroflexin-3 (Q9BWM7)
Organism: Homo sapiens (Human)
Function: Mitochondrial serine transporter that mediates transport of serine into mitochondria, an important step of the one-carbon metabolism pathway. Mitochondrial serine is converted to glycine and formate, which then exits to the cytosol where it is used to generate the charged folates that serve as one-carbon donors.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:30442778, ECO:0000269|Ref.4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGELPLDINIQEPRWDQSTFLGRARHFFTVTDPRNLLLSGAQLEASRNIVQNYRAGVVTPGITEDQLWRAKYVYDSAFHPDTGEKVVLIGRMSAQVPMNMTITGCMLTFYRKTPTVVFWQWVNQSFNAIVNYSNRSGDTPITVRQLGTAYVSATTGAVATALGLKSLTKHLPPLVGRFVPFAAVAAANCINIPLMRQRELQVGIPVADEAGQRLGYSVTAAKQGIFQVVISRICMAIPAMAIPPLIMDTLEKKDFLKRRPWLGAPLQVGLVGFCLVFATPLCCALFPQKSSIHISNLEPELRAQIHEQNPSVEVVYYNKGL
Protein: Homocysteine S-methyltransferase 1 (BoHMT1) (EC 2.1.1.10) (A4ZGQ8)
Organism: Brassica oleracea var. italica (Broccoli)
Function: Catalyzes methyl transfer from S-methylmethionine to homocysteine. The highest preference is for DL-homocysteine >> DL-cysteine. Has no selenocysteine methyltransferase activity.
Interaction partners:
Sequence:
MGLEKKSALLEDLIEKCGGCAVVDGGFATQLEIHGAAINDPLWSAVSLIKDPELIKRVHMEYLEAGADVVVTSSYQATIPGFLSRGLSMEESESLLQKSVKLAVEARDRFWDKVSKTSGHSYNRALVAASIGSYGAYLADGSEYSGSYGEDVSLDKLKDFHRRRIQVLVEASPDLLAFETIPNKLEAQACVELLEEENVQIPAWICFTSVDGENAPSGESFQECLETLNKSNNICAVGINCAPPQFMDNLIRKFSKLTQKAIVVYPNSGEVWDGKAKKWLPSQCFGDAEFEMFATKWRDLGAKLIGGCCRTTPSTIKAISRDLKRR
Protein: Inhibin beta A chain (Activin beta-A chain) (Q04998)
Organism: Mus musculus (Mouse)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P08476}.
Interaction partners:
- Follistatin
- Activin receptor type-2A
- Activin receptor type-1B
- Activin receptor type-2B
- Inhibin beta B chain
- Inhibin alpha chain
- Activin receptor type-1C
- Follistatin-related protein 3
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-1 proprotein
Sequence:
MPLLWLRGFLLASCWIIVRSSPTPGSEGHGSAPDCPSCALATLPKDGPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGDEAEEMGLKGERSELLLSEKVVDARKSTWHIFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEVDGDGKKKDGSDGGLEEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
Protein: Phosphoacetylglucosamine mutase (PAGM) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Phosphoglucomutase-3) (PGM 3) (Q9CYR6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
Interaction partners:
- UDP-N-acetylhexosamine pyrophosphorylase
- Glucosamine 6-phosphate N-acetyltransferase
- N-acetyl-D-glucosamine kinase
- UDP-N-acetylhexosamine pyrophosphorylase-like protein 1
- N-acetylglucosamine-6-phosphate deacetylase
- Glutamine--fructose-6-phosphate aminotransferase 1
- UTP--glucose-1-phosphate uridylyltransferase
- Phosphoglucomutase-1
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Outer mitochondrial transmembrane helix translocase
Sequence:
MDLEAVCKRSALHAKPQGLILQYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQDVRQVLAAIVEKEAVDLTQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNSGGRYGQATVEGYCQKLSKAFVDLTNQVSCSGDVKRSVKVDCANGIGALKLREMEHYFSRGLSVLLFNDGTQGRLNHLCGADFVKSQQKPPQGIEMKSGERCCSFDGDADRIVYYYCDADGHFHLIDGDKIATLISSFLKELLLEIGESVNLGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSEAVEVKIKRLAQELDDGKGKAARTLASIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDAIYVDLPNRQLKVKVADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLVFQLAGGIGERPQPTF
Protein: Uncharacterized protein C216.01c (Q9Y7J8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative serine/threonine-protein phosphatase C26H8.05c
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase 2A activator 2
- Putative serine/threonine-protein phosphatase C22H10.04
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Uncharacterized protein C63.05
- Protein phosphatase PP2A regulatory subunit A
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Transcription elongation factor spt5
Sequence:
MDSTKEEEDLNNNIDEISDGENEEEELDEAIAAALQKIEVPSIPRRVKVYEMEDENWVDCGTGYCDGKIEGPLAYFIVRSEADNETILLKTQLIAEDIYSRQEETLIVWQELNGTDLALSFQESSGCIDMWMFLANVQKAISSVTRSYSNDDILTDEGALNENYLNTVDLPAPELANLKEIEEAVYGYMQSIQSRDSLVRYVSNENYIDRLIELFPLCEDLENTDDLHRLCSIIKSFVQLNDAPLLESLFSNDEKLMCVAGILEYDPEFPNIKANHREYLMDSKKFKQVVPIQDPRILAKIHQTFKLQYLRDVVVSRIVDEPSFSVLNSFIFFNQADIIQYLQTNEKFLHELFSIYVNEGEDDQRKQDGIFFIQQVCNIAKGLQFQSCSALFATFVKFNLLKALDYAMSHENNSVRNAGSDILVSIIDHEPAIVWQKFDQDRKDASSSLSNAHVSQHSLLSNLINILHKESNPGVLAQISEAFKMLLSLPGSYAYNNPYRNADGNVRNKTDNIIGINFIENFYDNSFNMLAAPLLELENVSSLDVKKLDMYMHLCELFCYFFRIHDYWSRRFDTYKTLTSKVALLLYSDRKYVVLSALRFIRSCLAARQSEMSLIMLETDTYGKVLDLMLKVKDQTNLVNSAALEFFEFLRSEGSEDTLDYLNKNYRPQLESLNNLSTFSELLNIIDGLSSDSRSPKTVGTHESNSYEFDGASNNNQRVGDDVSKDWEIQQDFSIENDTELSEKVGQRTVLDSIAPAELNIEDSCEQPKQPILEDRYFLESAVYDTSAESSGINVSNTRYSKRKSDFQVDDQQADDESPKKRLSIDSSSAQNGYAS
Protein: MAGE (RE25453p) (Q9I7L4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosomes element 4
- SD25546p
- E3 SUMO-protein ligase NSE2
- E3 SUMO-protein ligase NSE2
- Dysfusion, isoform D
- E3 SUMO-protein ligase NSE2
- E3 SUMO-protein ligase NSE2
Sequence:
MASTSRAARSQNAIPSQEAQQPVDVVDAKVRAILNYILDHTAQKIPIKDKDLIAVAGDKSELKKRLPLVTNLLAETFGIILTPLDATTKTFICTAEEPVASIHELTPAQRPQFTLLYIILMYIFLRGNRIEDSKLYVMLEMLNIYPDEEHGYFGPNLRKQIEETFVKQQYLKRERSQLSAYDDSKTFFLWGPRAKAEFTFEQMVQFASKLLNQHPKVFGHHLSMAQEGVNAE
Protein: Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (PHK-gamma-LT) (PHK-gamma-T) (EC 2.7.11.19) (PSK-C3) (Phosphorylase kinase subunit gamma-2) (P15735)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity).
Interaction partners:
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Phosphorylase b kinase regulatory subunit beta
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-1
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Glycogen phosphorylase, liver form
Sequence:
MTLDVGPEDELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVTAERLSPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSSTVKDLISRLLQVDPEARLTAEQALQHPFFERCEGSQPWNLTPRQRFRVAVWTVLAAGRVALSTHRVRPLTKNALLRDPYALRSVRHLIDNCAFRLYGHWVKKGEQQNRAALFQHRPPGPFPIMGPEEEGDSAAITEDEAVLVLG
Protein: Myb domain protein 55 (T15B16.4 protein) (Q9ZSI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRHSCCYKQKLRKGLWSPEEDEKLLRYITKYGHGCWSSVPKQAGTFLFIQIHLLFGLQRCGKSCRLRWINYLRPDLKRGAFSQDEENLIIELHAVLGNRWSQIAAQLPGRTDNEIKNLWNSCLKKKLRLRGIDPVTHKLLTEIETGTDDKTKPVEKSQQTYLVETDGSSSTTTCSTNQNNNTDHLYTGNFGFQRLSLENGSRIAAGSDLGIWIPQTGRNHHHHVDETIPSAVVLPGSMFSSGLTGYRSSNLGLIELENSFSTGPMMTEHQQIQESNYNNSTFFGNGNLNWGLTMEENQNPFTISNHSNSSLYSDIKSETNFFGTEATNVGMWPCNQLQPQQHAYGHI
Protein: EH domain binding protein 1 (B5MC86)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASVWKRLQRVGKHASKFQFVASYQELMVECTKKWQPDKLVVVWTRRSRRKSSKAHSWQPGIKNPYRGVVVWPVPENIEITVTLFKDPHAEEFEDKEWTFVIENESPSGRRKALATSSINMKQYASPMPTQTDVKLKFKPLSKKVVSAALQFSLSCIFLREGKATDEDMQSLASLMSMKQADIGNLDDFEEDNEDDDENRVNQEEKAAKITELINKLNFLDEAEKDLATVNSNPFDDPDAAELNPFGDPDSEEPITETASPRKTEDSFYNNSYNPFKEVQTPQYLNPFDEPEAFVTIKDSPPQSTKRKNI