wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 family 8 subfamily B member 1 (G3V8J2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase type 7
- Aldo-keto reductase family 1 member D1
- Sterol 26-hydroxylase, mitochondrial
- Nuclear receptor subfamily 0 group B member 2
- Bile acid receptor
- Bile salt export pump
- Hepatic sodium/bile acid cotransporter
- Bile acid-CoA:amino acid N-acyltransferase
- Nuclear receptor subfamily 5 group A member 2
- Lanosterol synthase
Sequence:
MLWGSVLGALLMAVGCLCLSLLPRHRRPWEPPLDKGFVPWLGHTMAFRKNMFEFLKGMRAKHGDVFTLQLGGQYFTFVMDPLSFGPIIKSTQKVLDFVTYARELVFKVFGYQSMDEDHQMLHIASTKHLMGQGLEDLNRAMLDSLSLVMLGPKGRSLGARSWCEDGLFHFCYSILFKAGFLSLFGCTKDKEQDLDEADELFRKFRRFDLLFPRFVYSLLGPREWVEVSQLQRLFHQRLSVEQNLEKDGISNWLGFMLRFLRERGMASSMQDKFNFMMLWASQGNTGPTCFWALLFLLKHQDAMKAVREEATRVLGEARLEAETSFAFTLSALKCTPVLDSVMEETLRLCATPTLLRVVQEDYVLKMASGQEYQIRRGDKVALFPYLSVHMDPDIHPEPTTFKYNRFLNPDGTRKVDFYKSGKKIHHYNMPWGSGVSICPGRFFALSEMKTFVLLMVMYFDFELVDPDVPVPPIDPRRWGFGTSQPSHEVRFRYRLKPMQ
Protein: WD repeat-containing protein 48 homolog (Q20059)
Organism: Caenorhabditis elegans
Function: Together with wdr-20, binds to and stimulates the activity of the deubiquitinating enzyme usp-46, leading to deubiquitination and stabilization of the glr-1 glutamate receptor.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 46
- WD repeat-containing protein 20 homolog
- FANCI helical domain-containing protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Peptidyl-prolyl cis-trans isomerase
- ubiquitinyl hydrolase 1
- ubiquitinyl hydrolase 1
- ubiquitinyl hydrolase 1
- pre-mRNA 3' end processing protein pfs-2
- FANCD2
Sequence:
MSSCVNTSQTGPKKKISFIIRDEHEYSNRSAVSALQYDAQNGRLFTGGSDTIIRTWSVPHHKDAFSARGGVRSPGKNSPVQYQGSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDNKHGFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVYDINANFKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEKDNPVSLWVGTWKSDIKRWSIRPSAQLSIGGDEDGPSTSNANHSVSASSSPPVTFKYIRVKDQKGQQSTPELVIPGAPAIKKHAMLSDKRHVLTRDSDGNVALYDVLAARKIKDYGKRIFEEVVDENSRQVYIPSWFVVDSKSGMLQITLDELDALSSWLSSKDAGFDDNDRETKLNYGGMMLRSLFERWPPCKMTNVDAADADDVQKATLNFISLPEHTPLIICEGNGRPLYRLLVGDAGKEFEANELAQIAPMWVIDAIERNQLPKFNKMPFYLLPHPSTNPKQPKKDRLSATEMLQVKKVMEHVYEKILSTNDDITVGSIPLNQIHTKMEMYCNDQRLEPDMDLRTVKHLYWKQSGELLLHYKPVK
Protein: Protein SUPPRESSOR OF GENE SILENCING 3 (AtSGS3) (Q9LDX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for post-transcriptional gene silencing and natural virus resistance. May bind nucleic acids and is essential for the biogenesis of trans-acting siRNAs but is not required for silencing induced by IR-PTGS. Involved in the juvenile-to-adult transition regulation. In case of begomoviruses infection, it is targeted by the viral protein V2 leading to suppression of post-transcriptional gene silencing. Involved in the mechanisms necessary for quick response to heat and subsequent heritable transgenerational memory of heat acclimation (global warming) such as early flowering and attenuated immunity; this process includes epigenetic regulation as well as post-transcriptional gene silencing (PTGS). In response to heat, HSFA2 is activated and promotes the expression of REF6 which in turn derepresses HSFA2, thus establishing an heritable feedback loop able to trigger SGIP1 and subsequent SGIP1-mediated SGS3 degradation; this prevents the biosynthesis of trans-acting siRNA (tasiRNA) and leads to the release of HTT5, which drives early flowering but attenuates immunity.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18165314}. Cytoplasmic granule {ECO:0000269|PubMed:30778176}. Note=Accumulates in inclusion bodies in the cell periphery (PubMed:18165314). May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). Co-localizes with SGIP1 in cytoplasmic granules (PubMed:30778176). {ECO:0000250, ECO:0000269|PubMed:18165314, ECO:0000269|PubMed:30778176}.
Interaction partners:
- RNA-dependent RNA polymerase 6
- T10F20.8 protein
- Protein argonaute 1
- Putative nuclear RNA export factor SDE5
- Double-stranded RNA-binding protein 1
- Protein argonaute 7
- Regulator of nonsense transcripts 1 homolog
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 2
- Endoribonuclease Dicer homolog 1
Sequence:
MSSRAGPMSKEKNVQGGYRPEVEQLVQGLAGTRLASSQDDGGEWEVISKKNKNKPGNTSGKTWVSQNSNPPRAWGGQQQGRGSNVSGRGNNVSGRGNGNGRGIQANISGRGRALSRKYDNNFVAPPPVSRPPLEGGWNWQARGGSAQHTAVQEFPDVEDDVDNASEEENDSDALDDSDDDLASDDYDSDVSQKSHGSRKQNKWFKKFFGSLDSLSIEQINEPQRQWHCPACQNGPGAIDWYNLHPLLAHARTKGARRVKLHRELAEVLEKDLQMRGASVIPCGEIYGQWKGLGEDEKDYEIVWPPMVIIMNTRLDKDDNDKWLGMGNQELLEYFDKYEALRARHSYGPQGHRGMSVLMFESSATGYLEAERLHRELAEMGLDRIAWGQKRSMFSGGVRQLYGFLATKQDLDIFNQHSQGKTRLKFELKSYQEMVVKELRQISEDNQQLNYFKNKLSKQNKHAKVLEESLEIMSEKLRRTAEDNRIVRQRTKMQHEQNREEMDAHDRFFMDSIKQIHERRDAKEENFEMLQQQERAKVVGQQQQNINPSSNDDCRKRAEEVSSFIEFQEKEMEEFVEEREMLIKDQEKKMEDMKKRHHEEIFDLEKEFDEALEQLMYKHGLHNEDD
Protein: Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2 3) (PDC-E2 3) (PDCE2 3) (Q5M729)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
Sequence:
MAYASRIINHSKKLKDVSTLLRRENAATIRYYSNTNRAPLNREDTFNSRLGYPPLERISICSTSTLPVSIIFSTTRSNLSSAMGRPIFGKEFSCLMQSARGFSSGSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGYLAKIVKAEGSKEIQVGEVIAITVEDEEDIGKFKDYTPSSTADAAPTKAEPTPAPPKEEKVKQPSSPPEPKASKPSTPPTGDRVFASPLARKLAEDNNVPLSDIEGTGPEGRIVKADIDEYLASSGKGATAKPSKSTDSKAPALDYVDIPHSQIRKVTASRLAFSKQTIPHYYLTVDTCVDKLMALRSQLNSFKEASGGKRISVNDLVVKAAALALRKVPQCNSSWTDDYIRQFKNVNINVAVQTENGLYVPVVKDADRKGLSTIGEEVRLLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVVNPPQAAILAVGSAEKRVVPGNGPDQFNFASYMPVTLSCDHRVVDGAIGAEWLKAFKGYIENPKSMLL
Protein: Uncharacterized protein Rv2000 (P9WLN7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv2001
- Cation-transporting P-type ATPase B
Sequence:
MRPGFVGLGFGQWPVYVVRWPKLHLTPRQRKRVLHRRRLLTDRPISLSQIPIRTGGPMNDPWPRPTQGPAKTIETDYLVIGAGAMGMAFTDTLITESGARVVMIDRACQPGGHWTTAYPFVRLHQPSAYYGVNSRALGNNTIDLVGWNQGLNELAPVGEICAYFDAVLQQQLLPTGRVDYFPMSEYLGDGRFRTLAGTEYVVTVNRRIVDATYLRAVVPSMRPAPYSVAPGVDCVAPNELPKLGTRDRYVVVGAGKTGMDVCLWLLRNDVCPDKLTWIMPRDSWLIDRATLQPGPTFVRQFRESYGATLEAIGAATSTDDLFDRLETAGTLLRIDPSVRPSMYRCATVSHLELEQLRRIRDIVRMGHVQRIEPTTIVLDGGSVPATPTALYIDCTADGAPQRPAKPVFDADHLTLQAVRGCQQVFSAAFIAHVEFAYEDDAVKNELCTPIPHPDCDLDWMRLMHSDLGNFQRWLNDPDLTDWLSSARLNLLADLLPPLSHKPRVRERVVSMFQKRLGTAGDQLAKLLDAATATTEQR
Protein: Protein SLC31A2 (Copper transporter 2) (CTR2) (Solute carrier family 31 member 2) (Q9CPU9)
Organism: Mus musculus (Mouse)
Function: Involved in low-affinity copper uptake.
Subcellular location: Membrane {ECO:0000250|UniProtKB:O15432}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O15432}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000305|PubMed:24167251}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O15432}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000305|PubMed:24167251}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is partial (By similarity). Localizes in endosomes recycling from and to the plasma membrane, as well as in late endosomes trafficking to the trans-Golgi network (TGN) (PubMed:24167251). {ECO:0000250|UniProtKB:O15432, ECO:0000269|PubMed:24167251}.
Interaction partners:
- Copper-transporting ATPase 2
- Copper transport protein ATOX1
- Copper-transporting ATPase 1
- Cytochrome c oxidase copper chaperone
- Copper chaperone for superoxide dismutase
Sequence:
MPMHFIFSDEAVLLFDFWRVHSPTGMALSVLVVLLLAVLYEGIKVGKAKLLHKTLESLPATNSQQFILGPDQDSTGSRSTSDNRTRLRWFLCYFGQSLVHVIQVVIGYFVMLAVMSYNTWIFLGVVLGSAVGYYLAYPLLNMT
Protein: Magnesium transporter MgtE (Q9I544)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362011}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362011}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTEVEAKKPQESLQDRLAQVVELLHRHKVVEDLTHRQEGQHHDRVENLVHRQNLVELQRKLEELHPADIAHILESLPLDDRLTVWQLVKSEDDGDILLEVSDAVRETLIADMDDHEIIAATKDLDADELADLAPELPRDVVHELMESLDAQQRERVRSALSYEEDQVGALMDFEMVTIREDVSLEVVLRYLRRLKELPGHTDKLFVVDYDGVLKGVLPIKRLLVNDPDKQVLEVMATDPVTFHPDEDGYDAAQAFERYDLISAPVVDKGGKLIGRLTIDEMVDLIREESESEVLNMAGLREEEDIFASVWKSVRNRWAWLATNLITAFVASRVIGLFEGSIEKLVALAALMPIVAGIGGNSGNQTITMIVRAIALDQVQPTSNSRNRLLRKELGVALVNGLAWGGVIGVVAFYLYGNWELGVVMTAAMTLNLLLAAMMGVLIPMTLHRFGRDPAMGSSVMITAMTDSGGFFIFLGLATIFLM
Protein: L-glyceraldehyde 3-phosphate reductase (GAP reductase) (EC 1.1.1.-) (Q46851)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Interaction partners:
- Methylglyoxal reductase DkgB
- Multiple antibiotic resistance protein MarR
- Multiple antibiotic resistance protein MarA
- Methylglyoxal reductase DkgA
- Penicillin-insensitive murein endopeptidase
Sequence:
MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELAQIDQHIADGELNLWQASSDK
Protein: ribose-phosphate diphosphokinase (EC 2.7.6.1) (M0RBK1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ribokinase
- transketolase
- Transketolase
- Ribose-5-phosphate isomerase
- Amidophosphoribosyltransferase
- transketolase
- Phosphoglucomutase-1
- Uridine monophosphate synthetase, isoform CRA_a.
- ADP-sugar pyrophosphatase
- ADP-ribose pyrophosphatase, mitochondrial
Sequence:
MPNIKIFSGSSHQDLSQKITERLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPMSAKLIANMLSIAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENISDWRNCTIVSPDAGGAKRVTSIADHLNVDFALIHKERKKANEVDRMVLVGDVKERVAILVDDMADTCGTICYAADKLLSEGATRVYAILTHGIFSGPAIARINGACFEAVVVTNTIPQEDKMKQCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
Protein: Dimethyladenosine transferase 2, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 2) (Mitochondrial transcription factor B2) (mTFB2M) (mtTFB2) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2) (Q3TL26)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent rRNA methyltransferase which may methylate two specific adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA (By similarity). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Stimulates transcription independently of the methyltransferase activity (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Transcription factor A, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- Ubiquitin-like protein FUBI
- Bystin
- Pre-rRNA-processing protein TSR1 homolog
- Periodic tryptophan protein 2 homolog
- U3 small nucleolar ribonucleoprotein protein IMP4
- Protein LTV1 homolog
- WD repeat-containing protein 3
- WD repeat domain 36
Sequence:
MRGPAMRLPPRIALSALARGPSCILGSGAATRKDWQTRNRRGFSDFNIEPLPDSDLEESSPWTSRNRSEPTRHIACKKAARNLVRDLLEHQNPSRQIILECNPGPGILTGALLKAGARVVAFESEKTFIPHLEPLQRNMDGELQVVHCDFFKMDPRYQEVVRPDVSSQAIFQNLGIKAVPWSAGVPIKVFGILPYKHERRILWKILFDLYSCESIYRYGRVELNMFVSEKEFRKLIATPKRPDLYQVMAVLWQVACDVKFLHMEPWSSFSVHTENGHLEKSKHGESVNLLKQNLYLVRMTPRRTLFTENLSPLNYDIFFHLVKHCFGKRNAPIIRHLRSLSTVDPINILRQIRKNPGDTAARMYPHDFKKLFETIEQSEDSVFKWIYDYCPEDMEF
Protein: DnaJ homolog subfamily C member 3 (Interferon-induced, double-stranded RNA-activated protein kinase inhibitor) (Protein kinase inhibitor of 58 kDa) (Protein kinase inhibitor p58) (Q9R0T3)
Organism: Rattus norvegicus (Rat)
Function: Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Interferon-induced, double-stranded RNA-activated protein kinase
- DnaJ heat shock protein family
- Endoplasmic reticulum chaperone BiP
- Endoplasmin
- Protein disulfide-isomerase A6
- Hypoxia up-regulated protein 1
- X-box-binding protein 1
- Translocation protein SEC63 homolog
- Protein disulfide-isomerase A4
- DnaJ homolog subfamily B member 11
Sequence:
MVAPGSVRSRLGAVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTRVIELKMDFTAARLQRGHLLLKQGRLAEAEDDFKKVLKSNPSENEEKEAQSQLVKADEMQRLRAQALDAFDSADYTAAITFLDEILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKNDNTEAFYKISILYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIGSAEELIRDGRYTDATSKYESVMKAEPSVAEYTVRSKERICHCFSKDEKPVEAIKICSEVLQLEPDNVNALKDRAEAYLIEEMYDEAIQDYEAAQEQNENDQQIREGLEKAQRLLKQSQKRDYYKILGVKRNAKKQEIIKAYRKLALQWHPDNFQSEEEKKKAEKKFIDIAAAKEVLSDPEMRRKFDDGEDPLDAETQQGGGSNPFHRSWDSWQGFNPFSSGGPFRFKFHFN
Protein: Proteasome subunit alpha type-5 (Proteasome subunit alpha 5) (Q95008)
Organism: Caenorhabditis elegans
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome regulatory subunit 7
- Proteasome subunit beta type-3
- Proteasome subunit beta
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit pbs-5
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-3
Sequence:
MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAVKLGSTSIGIKTSEGVLLAAEKRSTSKLMVNDAIEKISKVDQHIGVTFAGLIADSRTLVERAQIEAQNFWFTYNRKIRVEDVTQSVANLALQFGDDDVKASMSRPFGVAMLFAGVDQEGAKLFHLDPSGTFIDCKAKSIGAASDGAEQNLKEQYHDALTIKEGLKMALAILKQVMEEKLNSANVEVVVIKPTVDAKGRPIGEFTRVSNEELDQVITSL
Protein: Epididymal secretory protein E3-beta (Human epididymis-specific protein 3-beta) (HE3-beta) (P56851)
Organism: Homo sapiens (Human)
Function: Possible function in sperm maturation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MASSLKIWGTLLALLCILCTLLVQSKEVSWREFMKQHYLSPSREFREYKCDVLMRENEALKDKSSHMFIYISWYKIEHICTSDNWMDRFRNAYVWVQNPLKVLKCHQENSKNSYTESRSFNYIEFHCSMDGYVDSIEDLKMVEPIGN
Protein: Alcohol dehydrogenase 4 (EC 1.1.1.1) (Alcohol dehydrogenase IV) (Q09669)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in ethanol oxidation in mitochondria.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16999687}.
Interaction partners:
- Alcohol dehydrogenase
- Putative S-
- Probable S-
- Probable pyruvate decarboxylase Pdc101
- Probable pyruvate decarboxylase C186.09
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative pyruvate decarboxylase C13A11.06
- Putative pyruvate decarboxylase C3G9.11c
- Uncharacterized oxidoreductase C26F1.07
Sequence:
MSILRSPFRLIRSPARFFPSLFHSSCNQSFTNGLKHQSTSSKAMPVSAFYIPSFNLFGKGCLAEAAKQIKMSGFKNTLIVTDPGIIKVGLYDKVKALLEEQSITVHLYDGVQPNPTVGNVNQGLEIVKKENCDSMVSIGGGSAHDCAKGIALLATNGGKIADYEGVDKSSKPQLPLIAINTTAGTASEMTRFAIITEETRHIKMAIIDKHTMPILSVNDPETMYGLPPSLTAATGMDALTHAVEAYVSTAANPITDACAVKCIELVNKYLKRAVDNGKDEEARDNMAYAEFLGGMAFNNASLGYVHAMAHQLGGFYGIPHGVCNAVLLAHVQKFNSRDPRANARLGDIAFHLGCEEHTAEAALDRISQLVLEVKIRPHLVDLGVKEKDFDVLVDHAMKDACGATNPIQPTHDEVKAIFKSAM
Protein: Probable 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) (O74455)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase gcd1
- Probable gluconokinase
- Glucose-6-phosphate 1-dehydrogenase
- Probable glucose-6-phosphate 1-dehydrogenase C7.13c
- 6-phosphogluconate dehydrogenase, decarboxylating
- Dihydroxy-acid dehydratase, mitochondrial
- Meiotically up-regulated gene 96 protein
- ATP-dependent 6-phosphofructokinase
- Transaldolase
- Glucose-6-phosphate isomerase
Sequence:
MSVYSFSDVSLVAKALGAFVKEKSEASIKRHGVFTLALSGGSLPKVLAEGLAQQRGIEFSKWEVFFADERIVPLDDENSNYALCKKLIFDKFEGFDPKKIHTINPELLKENPIDPQNVADEYEKQLVHVFANSSTVKVPVFDLLLLGCGPDGHTCSLFPDHEVLQEDVAWVAPVTDSPKPPKDRITLTLPVVTHAQAIAFVTTGAGKKDILPIVIEDFTSKLPSALITRNNLTRTSWFVDDEASANLERSSLKVFPQ
Protein: Chemokine C-C motif ligand 4 (Chemokine K203) (Q9I8E0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MKLSAVVLALLIASFCSRASSAPVGPDVPTCCTTYITHKIPRNLIQRHYSTSTSCSKPAIIFITKKEREVCANPSDPWVQRYLQSVKRD
Protein: HCG2029799, isoform CRA_b (Plasminogen) (Q5TEH5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPR
Protein: Alpha-xylosidase XylQ (EC 3.2.1.177) (P96793)
Organism: Lactiplantibacillus pentosus (Lactobacillus pentosus)
Function: Involved in the metabolism of isoprimeverose. Hydrolyzes isoprimeverose into equimolar amounts of glucose and xylose. In vitro, can also use p-nitrophenyl-alpha-D-xylopyranoside (alpha-p-NPX).
Subcellular location: Cell membrane {ECO:0000269|PubMed:9573180}; Peripheral membrane protein {ECO:0000269|PubMed:9573180}; Cytoplasmic side {ECO:0000269|PubMed:9573180}.
Interaction partners:
- Isoprimeverose transporter
- Xylose repressor
- Xylose isomerase
- Xylulose kinase
- Unannotated protein.
Sequence:
MKFTNGYWLNREEYDVNSPKETYDAQQNGKTITAFAPYTRIMSRGDQLNLGTTTITLTSPVENVIGVKLEHFDTNEHGPEFKINNLDPEVAIEVNDQVASLQSGDLKVTLPLRTDFEMKFTANGQLVTQSETKPQATIWNHDTKVNYMREQLSMGIDEKIYGLGERFTNFVKNGQVVDTWNQDGGTGSEQAYKNIPFYISSNGYGVFVDESQRVSFEIGSENVDRVQFSTEGQSLQYYVIYGPTPKEVLHRYTQLTGAIKLPPAWSFGLWLTTSFTTDYSEETVLKFIDGMQEHHIPLDVFHFDCFWQKGFEWCTLEWDKEQFPDPEGLLKKIHDRGIKVCVWLNPYIAQKSPLFKEAKDKGYLLTRENGDIWQWDLWQAGNGFVDFTNPAAVKWYQDKLKVLLDMGVDSFKTDFGERIPAEDVKFFDGSNPQQEHNYYTLQYNRAVYEVIQQEKGADEAVLFARSQRLVHNPIQYTGAATISRSTAQCVIQLRGGLSFLLSGFGFWSHDIGGFEDGPGTPTADLYKRWSQFGLLSSHSRYHGSDVYRVPWNFDDEAVENTRKYVNKLSLMPYIYTEAAHAAAAYGNPLMRPMFLEFGDDDNVYDNATQYMFGSKILVAPIFNDQGKAHFYLPSGKWTSILDGKVYQAPRTGEWVNEVFDELDLPVLVRQNSIIVRNEKAVDAAYDYTKDVDIHLYQIQDGNVSSKVVDEHGQDTAEIKVERANGRIVINTVGLTGDSTVYVHENNDTIKLSLVDGKAEVTL
Protein: LDL receptor repeat-containing protein egg-1 (Egg sterile protein 1) (Q09967)
Organism: Caenorhabditis elegans
Function: Probable receptor which is required for the oocyte-to-zygote transition although its exact function is controversial. Redundantly with egg-2, seems to be required for fertilization probably by promoting the interaction or fusion between sperm and oocyte. Conversely, shown to be dispensable for fertilization but required together with egg-2 for the formation of a continuous and cohesive eggshell chitin layer by maintaining a homogenous distribution of chitin synthase chs-1 at the unfertilized oocyte cell membrane. Appears to recruit or maintain together to the unfertilized oocyte cortex several proteins including chs-1, kinase mbk-2 and pseudophosphatases egg-3, and possibly egg-4 and egg-5.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16360684, ECO:0000269|PubMed:20971008}; Single-pass type II membrane protein {ECO:0000269|PubMed:16360684}. Endosome membrane {ECO:0000269|PubMed:20971008}; Single-pass type II membrane protein {ECO:0000269|PubMed:16360684}. Note=Localizes to the cell membrane of developing oocytes (PubMed:16360684, PubMed:20971008). Plasma membrane localization requires extracellular matrix protein cbd-1 (PubMed:20971008). After fertilization, localizes to endosomes in zygotes (PubMed:20971008). {ECO:0000269|PubMed:16360684, ECO:0000269|PubMed:20971008}.
Interaction partners:
- Inactive protein-tyrosine phosphatase egg-5
- RNA-binding protein pos-1
- Chondroitin proteoglycan 4 domain-containing protein
- Chitin-binding domain protein cbd-1
- Zinc finger protein mex-5
- glutamine synthetase
- PUM-HD domain-containing protein
- C-type lectin domain-containing protein 87
- Chondroitin proteoglycan 1
- glutamine--fructose-6-phosphate transaminase
Sequence:
MSQQPGSARRVNFPEEPMTLGEKFSHRMDQLKEIIADGGCSRAAKCVSITVCLVLLVLIFGGAIVYLVMSLTSSAQKMSADSMDISPQAIRHPKFWPPTDKIRFDDLNGIPMTSLFPQNVSTCSGFGFACTGAVHMVIPSSKRCDGRRDCEDGSDEENCKECQSVFSCKLRPEEESKKKGRSTVQPTLICLTAQHLCDNVENCPDGSDEAVCKSSCSKDQFKCPGSNACLPLSAKCDGINDCADASDEKNCSKCQNNAHKCGKQCIKASHVCDGVAQCADGSDEQQCDCQRCSGTDKALCDDGTCIMRTQVCDGKKDCTDGMDEEDCPGSCTIESFSPKLKMVTCSDGKQYTEAEACSGSFESCDHDCPNSKCHPKLAFTCPASKEARKMCISRRKVCDGTPDCDDGADEINCTPIKECGIAKNTQFKCDHKCLDSSRRCDGVWDCEDKSDEKGCDKCPSGTIKCAADKKCLPAFTRCNGVADCSDGSDELKCSCQECLGVHSNTYMCNESNRCLKRDEVCSPYSMCPNATYTDKAFCAALFLKKSGTSPF