wanglab/gogpt-training-data huggingface dataset:
Protein: TMEM51 protein (Transmembrane protein 51) (Q9BSA0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMAQSKANGSHYALTAIGLGMLVLGVIMAMWNLVPGFSAAEKPTAQGSNKTEVGGGILKSKTFSVAYVLVGAGVMLLLLSICLSIRDKRKQRQGEDLAHVQHPTGAGPHAQEEDRRKKRRMRRLPQGTMFPATRK
Protein: COP9 signalosome complex subunit 6 (Q567F8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367006}. Nucleus {ECO:0000256|RuleBase:RU367006}.
Interaction partners:
Sequence:
MASGVTGSVSVALHPLVILNISDHWIRIRSQEGRAVQVVGALIGKQEGRNIEVMNSFELLFHTVEDQIHIDKEYYYTKEEQFKQVFKEMEFLGWYTTGGSPDQSDIHIHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIISGEATMLFAELPYTLATEEAERIGVDHVARMTATGTGENSTVAEHLIAQHSAIKMLHSRVKVILEYVKAVQAGEVPFNHEILREANALCHRLPVLNTLKFKTDFYDQCNDVGLMAYLGTITKTCNSMNQFINKFNVLYDRQGIGRRMRGLFF
Protein: Cleavage and polyadenylation specificity factor subunit 2 (Cleavage and polyadenylation specificity factor 100 kDa subunit) (CPSF 100 kDa subunit) (Q9P2I0)
Organism: Homo sapiens (Human)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA 3'-end-processing factor FIP1
- Symplekin
- Cleavage stimulation factor subunit 2
- Pre-mRNA cleavage complex 2 protein Pcf11
- Cleavage stimulation factor subunit 1
- WD repeat-containing protein 82
Sequence:
MTSIIKLTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYATIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDGEEEIVYAVDFNHKREIHLNGCSLEMLSRPSLLITDSFNATYVQPRRKQRDEQLLTNVLETLRGDGNVLIAVDTAGRVLELAQLLDQIWRTKDAGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNPFQFRHLSLCHGLSDLARVPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLIDNPSEKITEIELRKRVKLEGKELEEYLEKEKLKKEAAKKLEQSKEADIDSSDESDIEEDIDQPSAHKTKHDLMMKGEGSRKGSFFKQAKKSYPMFPAPEERIKWDEYGEIIKPEDFLVPELQATEEEKSKLESGLTNGDEPMDQDLSDVPTKCISTTESIEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGKDIKVYMPKLHETVDATSETHIYQVRLKDSLVSSLQFCKAKDAELAWIDGVLDMRVSKVDTGVILEEGELKDDGEDSEMQVEAPSDSSVIAQQKAMKSLFGDDEKETGEESEIIPTLEPLPPHEVPGHQSVFMNEPRLSDFKQVLLREGIQAEFVGGVLVCNNQVAVRRTETGRIGLEGCLCQDFYRIRDLLYEQYAIV
Protein: 5,10-methylenetetrahydromethanopterin reductase (EC 1.5.98.2) (Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase) (Methylene-H(4)MPT reductase) (Q50744)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2379499}.
Interaction partners:
- F420-dependent methylenetetrahydromethanopterin dehydrogenase
- F420-dependent glutamate synthase
- Coenzyme F420 hydrogenase subunit beta
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit A 1
- Tetrahydromethanopterin S-methyltransferase subunit A 2
- Acetyl-CoA decarbonylase/synthase complex subunit beta
- F420-reducing hydrogenase, subunit gamma
- Tetrahydromethanopterin S-methyltransferase subunit D
Sequence:
MKFGIEFVPNEPIEKIVKLVKLAEDVGFEYAWITDHYNNKNVYETLALIAEGTETIKLGPGVTNPYVRSPAITASAIATLDELSNGRATLGIGPGDKATFDALGIEWVKPVSTIRDAIAMMRTLLAGEKTESGAQLMGVKAVQEKIPIYMGAQGPMMLKTAGEISDGALINASNPKDFEAAVPLIKEGAEAAGKSIADIDVAAYTCCSIDEDAAAAANAAKIVVAFIAAGSPPPVFERHGLPADTGKKFGELLGKGDFGGAIGAVDDALMEAFSVVGTPDEFIPKIEALGEMGVTQYVAGSPIGPDKEKSIKLLGEVIASF
Protein: Chaperone protein GP96 (Endoplasmin precursor) (Heat shock protein 90, beta (Grp94), member 1) (Q7T3L3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Immunoglobulin binding protein
- Calreticulin
- Protein disulfide isomerase family A, member 6
- Calreticulin
- Calreticulin
- Hypoxia up-regulated protein 1
- DnaJ homolog subfamily B member 11
- Calnexin
- Ankyrin repeat domain-containing protein 45
- Si:ch211-274f20.2.
Sequence:
MRRLWIIGLLCALLAFASVKADDDVDIDGTVEEDLGKSRDGSRTDDEVVQREEEAIQLDGLNTSQLKEIRDKAEKHAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLLSLTNEDALAGNEELTIKIKSDKEKNMLHITDTGIGMTKEELVKNLGTIAKSGTSEFLNKMTEVQDDSQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHMWESDSNQFSVIEDPRGDTLGRGTTITLVMKEEASDYLELETIKNLVKKYSQFINFPIYVWSSKTETVEEPIEDEAEAEKEEATEDEAEVEEEEEDKDKPKTKKVEKTVWDWELMNDIKPIWQRPAKEVEEDEYTAFYKTFSRDTDEPLSHIHFTAEGEVTFKSILFVPASAPRGLFDEYGTKKNDFIKLFVRRVFITDDFHDMMPKYLNFIKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIAEEQYNDKFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQTSHSDTVLSSLEQYVERMKEKQDKIYFMAGTSRKEAESSPFVEKLLKKGYEVVYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESDKAKEKREALEKEFEPLTTWMKDKALKEQIEKAVLSQRLTNSPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTLEINPKHPLIKEMLRRVNEDAEDKTAADLAVVLFETATLRSGYQLQDTKAYGERIERMLRLSMNVDLDAQVEEEPEEEPEEQTEEAEDEEEVQADEAEEESEATSKDEL
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (G8BG57)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTSSNTPSIDHEKGPMDDQVEKISTHGSHPASISEEHKQYLIAKHGTYELDPLPSMSDDDPLNWPDSFKFLQLGMVAFHGFMGTFMASGIVPSFGKYSEILDKPVPRVSYLTSAQIVLIGTFPMFWVPVMQRYGKRLLLIISVLGTMAFSIGAVFSTDYGTLMAMRCLSAVFVSPGLAVGGAIVKETTFSHQRGSRSGVWAISVNLGTMFGAFLMGFVAEYQNPKYVHVVFACTMFVLAVCYLFLGKETSYNPADLSRNETNRFKQLRFKAIFPENKITIFKFLEPLMFLLKPRVFIPAFGYTMMFMHGNIAMNVEIPQVMVHKFELGPQALGLQFLSFVIGTVIGEVGGYLSDRLVQWGHKNNKGPSFRLWVTHPGYITCIVGLIVFGVQIQNIDHYNVTPLIGCAIAAFGLQIGTSPIIAYCIDSDHTKAVQISLFVTFLRQLFAFIGPFYYPKMFDNLGFAEAYGIMAMLVGVLGWILTSCLQFWEQRHGR
Protein: CRIB domain-containing protein (Q17795)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSVYPPTPTMSMMNGGVDRKRAKRPPNVGSKELNSQENEMLFALVGSEAVCLTAAVVQLLKSDRGAWRVDLPHGVISLVKDYAQRAYFLRIFDILEERIVWDFKLYKAFRAQSFPQCRKLLAFEQMENGEDGVVIGLNFFSEYEAAEFKEHLERRHAQERKSTSTTRPAHPGMPIVVSSGIGSTPTRQFEITQAYGGTIRGPPMAIGGGQGITQMGTMAAAPQSHTHTDGNASSSGSWFRKDKNKKKDKKSKIKKEDISNPTNFQHKAHVGWNQDSGFSNTVYDDDMDEATKNILKAAGLESNNLNEDDKKFVKKFIAKNYDKYVSVGSLDPSQISSPLPPPIQQHPQMNQSWNQTPVRQYKPSFPSSAPIGSGASSYSTPAAPPPPTRVESHGLAPARPPPPPPSSGTRGIAPSRPLPQAPNYGTPENRPHAVPPPPPPPPPQSFGMAPISSAAPPPPPPPPPMGLPAVGAGAPPPPPPPPPSGAGGPASVLAKLPPAQDGRSNLLAEIQAGKQLRSVQQTADSPKSAGGDARGDVMAQIRQGAQLKHVDAAAEQERRKSTTSGAAGMGGLAGALAKALEERRMNMGIDDTSDDDDDEDDKNEWSD
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (G1MWY7)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MSMLTPVLQPPEVKEYLSRGERFIKWDDETASASPVILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYPHSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVQNPLTYNASRYTFLEKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALNACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHFKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSVINIQRGQLSPEGMVWFLCGPENNVIALDKLVLYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAIAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKKQFVSEKRQSSMKKGKNVEPEIIEQPAFTDAEDTVWAGDVAEEEPEEEDDQLGNLDEEEIKKMQSDEGTAGLEVTAYEEMSSLVNYIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPMQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSVDRIDVVVASTVSVTILSGQFLSDRSVKTYVEVELFGLPRDTKRKYRTKLTSTANSINPVWKEEPFVFEKIVMPELASLKIVAFEEGGKFIGHRVIPIIAVHSGYHHVCLRSESNMPLTMPSLFVYLEVKDYVPDAWADLTIALSNPIKFFNLQEKRSVNLKDGSEVERPDMQRNFSFPENNGIPESTRIFSTPFANGPAGAAALVKDGNMKEVTQLPDPQSSSCAAFTQGKLFFKM
Protein: Cofilin/actin-depolymerizing factor homolog 1 (Q8I467)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Not involved in actin polymerisation, instead functions to stimulate nucleotide exchange on monomeric actin and influence turnover of the small amount of cytosolic actin microfilaments. Essential for erythrocytic schizogony (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q03048}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q03048}.
Interaction partners:
- Cyclase-associated protein
- Actin-1
- Profilin
- Actin-related protein
- Actin-like protein, putative
- Actin-related protein, putative
- F-actin-capping protein subunit beta
- Actin-like protein, putative
Sequence:
MISGIRVNDNCVTEFNNMKIRKTCGWIIFVIQNCEIIIHSKGASTTLTELVQSIDKNNEIQCAYVVFDAVSKIHFFMYARESSNSRDRMTYASSKQAILKKIEGVNVLTSVIESAQDVADLK
Protein: Zinc finger protein DPF3 (BRG1-associated factor 45C) (BAF45C) (Zinc finger protein cer-d4) (P58269)
Organism: Mus musculus (Mouse)
Function: Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development (By similarity). Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92784}.
Interaction partners:
- Actin-like protein 6B
- Zinc finger protein neuro-d4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- AT-rich interactive domain-containing protein 1A
- AT-rich interactive domain-containing protein 1B
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- Calcium-responsive transactivator
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
Sequence:
MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDVPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA
Protein: Arrestin domain-containing protein 3 (TBP-2-like inducible membrane protein) (TLIMP) (Q96B67)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays a role in regulating cell-surface expression of adrenergic receptors and probably also other G protein-coupled receptors. Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation. May recruit NEDD4 to ADRB2. Alternatively, may function as adapter protein that does not play a major role in recruiting NEDD4 to ADRB2, but rather plays a role in a targeting ADRB2 to endosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}. Cell membrane {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}; Peripheral membrane protein {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325}; Cytoplasmic side {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325}. Lysosome {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}. Endosome {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}. Early endosome {ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}. Note=Associated with plasma membrane, as well as with endosomes and lysosomes during endocytosis (PubMed:16269462, PubMed:20559325, PubMed:23208550). {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
- NEDD4-like E3 ubiquitin-protein ligase WWP2
- Beta-2 adrenergic receptor
- NEDD4-like E3 ubiquitin-protein ligase WWP1
- E3 ubiquitin-protein ligase NEDD4-like
- Beta-arrestin-1
- E3 ubiquitin-protein ligase Itchy homolog
- Beta-arrestin-2
- S-arrestin
Sequence:
MVLGKVKSLTISFDCLNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERDDDNSEEGFHTIHSGRHEYAFSFELPQTPLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDINTPSLLSPQAGTKEKTLCCWFCTSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVPKAAIYQTQAFYAKGKMKEVKQLVANLRGESLSSGKTETWNGKLLKIPPVSPSILDCSIIRVEYSLMVYVDIPGAMDLFLNLPLVIGTIPLHPFGSRTSSVSSQCSMNMNWLSLSLPERPEAPPSYAEVVTEEQRRNNLAPVSACDDFERALQGPLFAYIQEFRFLPPPLYSEIDPNPDQSADDRPSCPSR
Protein: Follistatin-related protein 1 (Follistatin-like protein 1) (Q12841)
Organism: Homo sapiens (Human)
Function: Secreted glycoprotein that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation. Plays a role in the development of the central nervous system, skeletal system, lungs, and ureter (By similarity). Promotes endothelial cell survival, migration and differentiation into network structures in an AKT-dependent manner. Also promotes survival of cardiac myocytes (By similarity). Initiates various signaling cascades by activating different receptors on the cell surface such as DIP2A, TLR4 or BMP receptors.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Toll-like receptor 2
- Toll-like receptor 6
- Disco-interacting protein 2 homolog A
- Bone morphogenetic protein 2
- Toll-like receptor 1
- SPARC
- Toll-like receptor 4
- Bone morphogenetic protein 4
- Transforming growth factor beta-1 proprotein
- Toll-like receptor 5
Sequence:
MWKRWLALALALVAVAWVRAEEELRSKSKICANVFCGAGRECAVTEKGEPTCLCIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHCKEKKSVSPSASPVVCYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKLLRGLCVDALIELSDENADWKLSFQEFLKCLNPSFNPPEKKCALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKNQKGAQTQTEEEMTRYVQELQKHQETAEKTKRVSTKEI
Protein: AHNAK nucleoprotein (A0A494B8Y7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEKEEETTRELLLPNWQGSGSHGLTIAQRDDGVFVQEVMQNSPAARTGVVKEGDQIVGATIYFDNLQSGEVTQLLNTMGHHTVGLKLHRKGDRSPEPGQTWTHEVFSSRSSEVVLNTVQPSSLDCNDQNKPKEAINKAGAASDSTPDAGSAFQPQGSPGLQICLSTLTSSCLALSA
Protein: ZZ-type domain-containing protein (Q9N3Z0)
Organism: Caenorhabditis elegans
Interaction partners:
- Glutaminyl-peptide cyclotransferase
- Protein lgg-1
Sequence:
MSSIRYRRPPIIERRYERTPSYSTIPRDIHVSFYHNNYHRSKILYLNKFNAMEKLIEAAHELYPSNGVYRLFSDSTIGAQNELNDSVQVMECVQNPDHILPHLHIRLEDYRPRSISRNYHEVNVPIIRTPSQHSIHQSVRFNDNKRHHHHHHHDSIRNFVHHDTPCRNCFRIIVGSRYHCLQCPDYDICGDCEKDLVHYEHALLRIVTPRVTSIPDYVTVNAPSYIFPEHRYDIKREHYHWF
Protein: alcohol dehydrogenase (EC 1.1.1.1) (Q9UAT1)
Organism: Caenorhabditis elegans
Interaction partners:
- Alcohol dehydrogenase class-3
- Dehydrogenase/reductase SDR family member 4
- DeHydrogenases, Short chain
- Hydroxyacid-oxoacid transhydrogenase, mitochondrial
- O-acyltransferase
- Alcohol dehydrogenase 2
- Alcohol dehydrogenase 1
- PNPLA domain-containing protein
- Probable aldehyde oxidase gad-3
- Putative aldehyde dehydrogenase family 7 member A1 homolog
Sequence:
MVSSDVPKTQRALIFESYGGPLEIKQLPIPQPNEDELLVKMEYSGICHSDVHTWLGDFHYVSKCPMIGGHEGAGSVISVGSKVKNWQIGDKVGIKLVQGNCLNCEYCQTGHEPLCPHVWNIGVQKYGTFQEYATIRDVDAIKIPKSMNMAAAAPVLCGGVTAYKALKESEVKSGQIVAVTGAGGGLGSFAIQYARAMGMRVVAIDHPSKEAHCKSLGAEWFVDAFGTEDIVAHIREITDGGAHGVVNFAAAKVPMEKALEYVRKRGTVVFVGLAKDSKILVDTIPLIFNAVKIKGSIVGSRLDVNEAMDFVARGAVNVPLELVKLEDVAEVYTKMHDGKINSRVVVDFSL
Protein: EKC/KEOPS complex subunit CGI121 (Q8I3Y9)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- non-specific serine/threonine protein kinase
- N
- tRNA N6-adenosine threonylcarbamoyltransferase
- tRNA N6-adenosine threonylcarbamoyltransferase
Sequence:
MSTTKLHILDQQLDITLILFKNVVNSKDLLESYTKSMNDNICYINDFFLLLDSNLVYNENHILHSIYRAHHNFQSKKRITKNIFLEILFLLSPHENINECVKQYQIKNDSSSVIYVGINISKDQVDMFIKSVQGDQADFNELSFLHDKKKILENFKCDNMDNLERFIYHNIASKKINLS
Protein: Rac-like GTP-binding protein 3 (OsRac3) (Q6Z808)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the membrane when activated.
Interaction partners:
- Os10g0372500 protein
- Expressed protein
- Os05g0392050 protein
- Os05g0392000 protein
- Dol-P-Glc:Glc
- Uncharacterized protein Os04g0629400
- Protein LOL5
- Os02g0719000 protein
- Os01g0913600 protein
- Os06g0318300 protein
Sequence:
MASSASRFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVVVDSTTVNLGLWDTAGQEDYNRLRPLSYRGADVFVLAFSLVSRASYENIMKKWIPELQHYAPGVPIVLVGTKLDLREDKHYLLDHPGMIPVTTAQGEELRKQIGAAYYIECSSKTQQNVKGVFDAAIKVVIQPPTKQREKKKKKSRQGCSMMNMFRGRKMSCFKS
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 6 (EC 2.4.1.109) (P42934)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial oxaloacetate transport protein
Sequence:
MSKAKGTGFSSIDTEDENLRERYVNQPKANASDIQDEQLDCFEQLEEKHRTKKNEEYTALKILRDVIGPLLLTITSFYLRFQHIDQNNYVVWDEAHFGKFGSYYIKHEYYHDVHPPLGKMLIALSEWMAGFDGQFDFSSNNAYPENVNFKLMRQFNATFGALCTPVAFFTAKWMGFNYFTVYLIATMVTLEHSYIVLSKFILLDSMLLFFSMTTFACMIKLYTLRKQQMTKKWSLWMLLTGLSIGCVCSVKWVGLFITVVVGLYTCIELFLLYCDKELPRIKYYKHWLIRIINLIVIPFLIYLYCFKIHFVLLYKSGTGDSTTNTLFQINLEGTQIEAGPRDVAFGSELTIRSHGLSPNLLHSHIQVYPEGSGQRQITGYGFADSNNVWKFEFSRSSGLELDQNGTLNGKIIPITDGVEVRLSHKNTGSNLHSHDVPSHVSRGNYEVSGYGSQSVGDEKDDWIVEIVKQMDSPNPVYSNENSTILHPVSTFFRLRHKVLGCYLASTGLTYPAWGFKQAEIVCKDSWSRRDKSTWWNVEDHWNHNLETAEDYVPPKSNFWTDFILTNFAMASSNNALVPDEDKYDSLSSDAWEWPTLHKGLRMCSWAGYITRYYLMGSPFNTWISTVSLIIFPFIILFILYRWRRQTLYLSDDQIWQITIQGIFPFISWMTHYLPFAMMGRVTYVHHYVPALYFAMLVFGFVLDFTLTRVHWMVKYPIYLSLFGGCIYIYNLFAPICQGMHGDKAEYLPLQWLSTWDIAP
Protein: GTP-binding nuclear protein Ran-1 (Ras-related nuclear protein 1) (P41916)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Exportin-T
- Protein EXPORTIN 1A
- Protein EXPORTIN 1B
- Protein HASTY 1
- Ran-binding protein 1 homolog a
- Importin subunit beta-1
- Elongation factor 1-alpha 1
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- Importin beta-like SAD2 homolog
Sequence:
MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNFEKPFLYLARKLAGDQNLHFVETPALAPPEVHIDIADQQKNEAELLQAAAQPLPDDDDDIFE
Protein: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1) (Iron-sulfur subunit of complex II) (Ip) (P21911)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Iron-sulfur protein (IP) 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).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome B subunit
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- WW domain-containing protein C2F3.14c
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Probable citrate synthase, mitochondrial
Sequence:
MFSRRIQVLSPFLKHFVNRNARMMATEANISATSANPQSQGENLKTFEIYRWNPEKPEVKPKLQKYTVDLTKCGPMVLDALIKIKNEQDPTLTFRRSCREGICGSCAMNINGSNTLACICNIKKDNKPTKIYPLPHCFIVKDLVPDLTYFYKQYKSIEPWLQNDNIPKDKEFYQSRADRAKLDGLYECILCACCSTSCPSYWWNSEEYLGPAVLMQAYRWIIDSRDQATAKRLDVMQNSMSVYRCHTIMNCARTCPKGLNPGLAIAKVKALMATA
Protein: holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) (F4J6B1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRIRVMSQLQRSLSIELPSLVPLQLPSRMETHLWFIRPDEVKSTSLLKHYSQLLSPTEKEKVLQMRGDELKKNALLARTLVRTTIARCMTNNEVDPKALMFKKNMYGKPEVDWQNYTNCNNPPLHFNISHTDSLIACGVTVHVPVGIDVEDKERKIKHDILAFAERFYSADEVKFLSTLPDPEVQRKEFIKLWTLKEAYVKALGKGFSAAPFNTFTIQSKVGTKGEYNLCKVCFDLNLHSGIE
Protein: Stathmin-3 (A0A0J9YW36)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XHRCGLGDHPLRRPRHLLWPEKPLPFAPRGLDGGGATAIPKPSGDQRAPPLPPLHLPRGGPTAFEAYKEKMKELSVLSLICSCFYTQPHPNTVYQYGDMEVKQLDKRASGQSFEVILKSPSDLSPESPMLSSPPKKKDTSLEELQKRLEAAEERRKTQEAQVLKQLAERREHEREVLHKALEENNNFSRQAEEKLNYKMELSKEIREAHLAALRERLREKELHAAEVRRNKEQREEMSG
Protein: Rearranged L-myc fusion sequence variant (Q59GL0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFYHDLLFYRELTLFWSKLQRRIDPSLDTFLERCRQFGVIAKTQQHLFCLIRVIQTEAQDAGLGVSILLCVRALQLRSSEDEEMKASVCKTIACLLPEDLEVRRACQLTEFLIEPSLDGFNMLEELYLQPDQKFDEENAPVPNSLRCELLLALKAHWPFDPEFWDWKTLKRHCHQLLGQEASDSDDDLSGYEMSINDTDVLESFLSDYDEGKEDKQYRRRDLTDQHKEKRDKKPIGSSERYQRWLQYKFFCLLCKRECIEARILHHSKMHMEDGIYTCPVCIKKFKRKEMFVPHVMEHVKMPPSRRDRSKKKLLLKGSQKGICPKSPSAIPEQNHSLNDQAKGESHEYVTFSKLEDCHLQDRDLYPCPGTDCSRVFKQFKYLSVHLKAEHQNNDENAKHYLDMKNRREKCTYCRRHFMSAFHLREHEQVHCGPQPYMCVSIDCYARFGSVNELLNHKQKHDDLRYKCELNGCNIVFSDLGQLYHHEAQHFRDASYTCNFLGCKKFYYSKIEYQNHLSMHNVENSNGDIKKSVKLEESATGEKQDCINQPHLLNQTDKSHLPEDLFCAESANSQIDTETAENLKENSDSNSSDQLSHSSSASMNEELIDTLDHSETMQDVLLSNEKVFGPSSLKEKCSSMAVCFDGTKFTCGFDGCGSTYKNARGMQKHLRKVHPYHFKPKKIKTKDLFPSLGNEHNQTTEKLDAEPKPCSDTNSDSPDEGLDHNIHIKCKREHQGYSSESSICASKRPCTEDTMLELLLRLKHLSLKNSITHGSFSGSLQGYPSSGAKSLQSVSSISDLNFQNQDENMPSQYLAQLAAKPFFCELQGCKYEFVTREALLMHYLKKHNYSKEKVLQLTMFQHRYSPFQCHICQRSFTRKTHLRIHYKNKHQIGSDRATHKLLDNEKCDHEGPCSVDRLKGDCSAELGGDPSSNSEKPHCHPKKDECSSETDLESSCEETESKTSDISSPIGSHREEQEGREGRGSRRTVAKGNLCYILNKYHKPFHCIHKTCNSSFTNLKGLIRHYRTVHQYNKEQLCLEKDKARTKRELVKCKKIFACKYKECNKRFLCSKALAKHCSDSHNLDHIEEPKVLSEAGSAARFSCNQPQCPAVFYTFNKLKHHLMEQHNIEGEIHSDYEIHCDLNGCGQIFTHRSNYSQHVYYRHKDYYDDLFRSQKVANERLLRSEKVCQTADTQGHEHQTTRRSFNAKSKKCGLIKEKKAPISFKTRAEALHMCVEHSEHTQYPCMVQGCLSVVKLESSIVRHYKRTHQMSSAYLEQQMENLVVCVKYGTKIKEEPPSEADPCIKKEENRSCESERTEHSHSPGDSSAPIQNTDCCHSSERDGGQKGCIESSSVFDADTLLYRGTLKCNHSSKTTSLEQCNIVQPPPPCKIENSIPNPNGTESGTYFTSFQLPLPRIKESETRQHSSGQENTVKNPTHVPKENFRKHSQPRSFDLKTYKPMGFESSFLKFIQESEEKEDDFDDWEPSEHLTLSNSSQSSNDLTGNVVANNMVNDSEPEVDIPHSSSDSTIHENLTAIPPLIVAETTTVPSLENLRVVLDKALTDCGELALKQLHYLRPVVVLERSKFSTPILDLFPTKKTDELCVGSS