wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydroorotase (DHOase) (EC 3.5.2.3) (Q727F3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Dihydroorotate dehydrogenase
- Carbamoyl phosphate synthase small chain
- Bifunctional protein PyrR
- Dihydroorotate dehydrogenase, electron transfer subunit
- Orotidine 5'-phosphate decarboxylase
- Orotate phosphoribosyltransferase
- Uracil permease
- Amidohydrolase family protein
Sequence:
MSDILFLRNARLLGTPVDLIARDGVIAAIGEHGTLDTPADATVHDAGGHILFPSFIDAHVHLREPGFEYKEDIASGLAAAAHGGFGAVMCMANTRPVNDDAAVTRHIIETSLRHWPHGPRVYPVGAATVGLKGTELAPMAELAAAGCAAFSNDGAPVPDTEMFRRAVEYAADLGRVVIDHCEDPYLAKGAHMNEGATSGRVGVKGQPDVGEALHVARDILLADYLGLPIHLAHISCRRSVELIAWAKVRGVPVTAETCPHYLILDDTALENYDTNAKVNPPLRTPDDVAALREAVKSGVIDMFVTDHAPHAAHEKETPLDEAPNGISGLDTAVALTWGLVREGLLTEGDLVRLWNREPARVFGLPRNGFEPGDPADFFLFDPDEAWVVSRETMHSKSCNTPFLGHTLTGRVKAHWMGGRRIA
Protein: Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1) (Q8CFI2)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49427}. Nucleus {ECO:0000250|UniProtKB:P49427}. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase. {ECO:0000250|UniProtKB:P49427}.
Interaction partners:
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Ubiquitin-conjugating enzyme E2 R2
- Ubiquitin-like modifier-activating enzyme 1
- Polyubiquitin-C
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like modifier-activating enzyme 6
- Polyubiquitin-B
Sequence:
MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEADSCFGDEEDDSGTEES
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (P12787)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MLAAALRRCTAAAAARGLLHPASAPSPAAAVCSIRCYSHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV
Protein: Cd6 molecule (G3V8U0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- CD166 antigen
- T-cell surface antigen CD2
- T-cell surface glycoprotein CD4
- T-cell surface glycoprotein CD3 epsilon chain
- T-cell surface glycoprotein CD5
- T-cell surface glycoprotein CD3 delta chain
- T-cell surface glycoprotein CD3 zeta chain
- Tyrosine-protein kinase
- T-cell surface glycoprotein CD3 gamma chain
- Lymphocyte cytosolic protein 2
Sequence:
MWLFLGIAGLLTAVLSGLPPPAPSDQHRNGSIPNMSSDPEEQLGIRLVNGSSRCSGFVQVLLESWEPVCAGHWNRAATEAACNALGCGDLGNFTHLAPPTSERPPGATSRNTSSSRNTTWAGAPTVRCHGANWQLCKVEDYECSSDRRLVWVTCAENQAVRLVDGGSRCAGRVEMLQHGEWGTVCDDTWDLDDANVVCKQLKCGWAVKALAGLHFTPGQGPIHRDQVNCSGTEAYLWDCPGRPGDQYCGHKEDAGVVCSEHQSWRLTGGVDSCEGQVEVYFRGVWSTVCDSEWYPSEAKVLCQSLGCGSEVDRPKGLPHSLAGRMYYSCKGEELTLSTCSWRFNNSNLCSQSLAARVVCSGSQRHPNLSTSEVPSRVPVTIESSVPVSVKDKDSQNLTLLIPCIVLGILLLVSLIFIVFLLLKAKGQYALPTSVNHQQLSTANPAGINNYHPVPITIAKEAPMLFIKPRVPEDSDSSSESDYEHYDFSSQPPVALTTFYNSQRHRVTEEEAQQNRFRMPPLEEGLEELHVSNIPAADPRPCVVDAPSLGSQYHTRNNSDSSTSSEEGYCNDPSSKPPPWNSQVFSEKSPLTEQPPNLELAGSQAMFSAGASADDSSSTSSGEWYQNFQPPPQHPPVEQFECPGPPDLQADSIDDDEEDYDDIGAA
Protein: Carbamoylase-1 (EC 3.-.-.-) (Carbamoylase I) (P84783)
Organism: Mactra chinensis (Chinese surf clam)
Function: Hydrolysis of carbamoyl and sulfocarbamoyl esters of paralytic shellfish toxins. Ester hydrolysis is unaffected by the presence or absence of a hydroxyl moiety at the N-1 postion of the substrate toxin but is significantly affected by the stereochemistry of sulfate esters at C-11 of the substrate toxin.
Interaction partners:
Sequence:
VRTPVTVQTKVDNIKXY
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (A0A8I6AM39)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MTSSLQRPFRVPWLLWAVLLVSTTAELLNILSLQRAGITASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSSNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSVSMMEAAAAEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERLTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNGGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEVFMRCTDLFPGESVPDYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTSGLTPSTGMTTISEMPYPDETHLHATNVAQSLGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEVTGQQDFTQAANGQACLIPDVPPAQLYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGNKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRSHNVNSHAATTQYANGVVPSGQAANIVAHRAQEMLQNQFNGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVPTQGVTSTAADPGPAKPRRAQRPNSLDLSATNILDGSSMQIGESTQDGKSGSGEKIKRRVKTPYSLKRWRPSTWVISTEPLDCEVNNNGSDRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL
Protein: Serpentine receptor class r-10 (Odorant response abnormal protein 10) (Olfactory receptor 10) (Q18807)
Organism: Caenorhabditis elegans
Function: An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:26150102, ECO:0000269|PubMed:8601313}; Multi-pass membrane protein {ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:8601313}.
Interaction partners:
- Serpentine Receptor, class I
- Ion transport domain-containing protein
- Guanine nucleotide-binding protein alpha-17 subunit
- Odorant response abnormal protein 4
- Serpentine Receptor, class H
- Nuclear hormone receptor family member odr-7
- E3 ubiquitin-protein ligase makorin
Sequence:
MSGELWITLVDTADIVGVTLTFCVNIVLLGLLKTRGKNLGTYKYLMAFFSVFSIFYAIIEFILRPIMHIENTTFFLISRKRFNYSTKLGKINSAFYCACFATSFVVSGVHFVYRYFATCKPNLLRLFNLPTLLLWPLGCSVPVTMWASVSYFLYPDTEYTEAAVTNVLNNHYNWIKKENVSYIAYVYYQYENGVRHIYLKNLLGCFVHYFVMSMTFVVMFYCGYATWKTMNEHKDVSDRTRALQKQLFKALVLQTLIPTIFMYAPTGVMFIAPFFDVNLNANANFIVFCSFLYPGLDPLILILIIRDFRRTIFNFLCGKKNSVDESRSTTRANLSQVPT
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (EC 7.1.1.2) (Complex I-20kD) (CI-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) (Q9DC70)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
Sequence:
MAALAAPGLLSVRILGLRTAQVQLRRVHQSVATEGPSPSPSPSLSSTQSAVSKAGAGAVVPKLSHLPRSRAEYVVTKLDDLINWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQADVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIKREQKLKIWYRR
Protein: Meiotically up-regulated gene 170 protein (Q9UU84)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and the barrier septum.
Interaction partners:
- Arrestin family protein 1
- Arrestin domain-containing protein C584.15c
- Arrestin domain-containing protein C31A2.12
- Putative arrestin-related trafficking adapter C2D10.04
- Uncharacterized protein C18H10.20c
Sequence:
MTEELFSNSETCSLSDPLTSKTLSSIENPFDDPYILSEESEILTIKTDVLRPNILNRKSSFYPEADAPVRKSNLQVKKIFENQVLNCDGIKVAITIPDTSLIAGSLLHGNIWLSYEGAKNVETGVWIKEMFLDFYGILNFKGHSEPFYSISEKYSFCNLKTSALILSKAASASIGNKGLFLKCSCKVGFPFSFIVPLDIGPGTYHSSKLELLYYISSTLTLTSLDQNIRCTRCTIPKRVITSMHNNIAELYNPISCIKSLPYLSLEEAKTTLEVHTDRSLFFSGQIIDFTICYTHNHHRRIHNIKARLLETHIFHPNTQNHYGGYCMNQAEETFASCGYLKRYQKTKTKTRAKSTWKIANKSVYSNLAPTLKNTIHAQIKIPEFCRSVNLKDQLKIDYTLEVCFSAFFKPRILSIQIPITILHSWN
Protein: Uncharacterized HTH-type transcriptional regulator YciT (P76034)
Organism: Escherichia coli (strain K12)
Interaction partners:
- UPF0509 protein YciZ
Sequence:
MNSRQQTILQMVIDQGQVSVTDLAKATGVSEVTIRQDLNTLEKLSYLRRAHGFAVSLDSDDVETRMMSNYTLKRELAEFAASLVQPGETIFIENGSSNALLARTLGEQKKNVTIITVSSYIAHLLKDAPCEVILLGGVYQKKSESMVGPLTRQCIQQVHFSKAFIGIDGWQPETGFTGRDMMRTDVVNAVLEKECEAIVLTDSSKFGAVHSYSIGPVERFNRVITDSKIRASDLMHLEHSKLTIHVVDI
Protein: Dynein light chain Tctex-type 1 (Activator of G-protein signaling 2) (AGS2) (T-complex testis-specific protein 1 homolog) (Q9Z336)
Organism: Rattus norvegicus (Rat)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to mitotic spindles. {ECO:0000250}.
Interaction partners:
- Dynein light chain roadblock-type 1
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain roadblock
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light chain 2, cytoplasmic
- Dynein light chain LC8-type 1 like 2
- Dynein light chain LC8-type 1 like 1
- Dynein light chain
- Cytoplasmic dynein 1 light intermediate chain 2
Sequence:
MEDFQASEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI
Protein: Myosin-5 (Actin-dependent myosin-I MYO5) (Class I unconventional myosin MYO5) (Type I myosin MYO5) (Q04439)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:16478726, ECO:0000269|PubMed:17522383, ECO:0000269|PubMed:8682864, ECO:0000269|PubMed:9628892}. Note=Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.
Interaction partners:
- Verprolin
- Proline-rich protein LAS17
- Protein BZZ1
- Calmodulin
- Reduced viability upon starvation protein 167
- Actin-binding protein
- Actin
- Myosin tail region-interacting protein MTI1
- Actin cytoskeleton-regulatory complex protein SLA1
- Actin cytoskeleton-regulatory complex protein PAN1
Sequence:
MAILKRGARKKVHQEPAKRSANIKKATFDSSKKKEVGVSDLTLLSKISDEAINENLKKRFLNATIYTYIGHVLISVNPFRDLGIYTDAVMNEYKGKNRLEVPPHVFAIAESMYYNMKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASSTHTESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNNQFEPCAGNITNYLLEKQRVVSQIKNERNFHIFYQFTKGASDAYRQTFGVQKPEQYVYTAAAGCISAETIDDLQDYQETLKAMRVIGLGQEEQDQIFRMLAAILWIGNVSFIENEEGNAQVRDTSVTDFVAYLLQIDSQLLIKSLVERIMETNHGMKRGSVYHVPLNIVQADAVRDALAKAIYNNLFDWIVSRVNKSLQAFPGAEKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKSEQETYEREKIQWTPIKYFDNKVVCDLIEARRPPGIFAAMNDSVATAHADSNAADQAFAQRLNLFTTNPHFDLRSNKFVIKHYAGDVTYDIDGITDKNKDQLQKDLVELIGTTTNTFLATIFPDTVDRESKRRPPTAGDKIIKSANDLVETLSKAQPSYIRTIKPNETKSPNDYDDRQVLHQIKYLGLQENVRIRRAGFAYRQVFEKFVERFYLLSPHCSYAGDYTWQGDTLDAVKYILQDSSIPQQEYQLGVTSVFIKTPETLFALEHMRDRYWHNMAARIQRAWRRFLQRRIDAATKIQRTIRERKEGNKYEKLRDYGTKVLGGRKERRSMSLLGYRAFMGDYLSCNESKSKGAYIKRQVSIKEKVIFSIHGEALHTKFGRSAQRLKKTFLLTPTTLYIVGQTLVQNAMTYTQDYKIDVRNIQAVSLTNLQDDWVAIKLASSGQPDPLINTYFKTELITHLKRLNDKIQIKIGSAIEYQKKPGKLHSVKCQINESAPKYGDIYKSSTISVRRGNPPNSQVHKKPRKKSSISSGYHASSSQATRRPVSIAAAQHVPTAPASRHSKKPAPPPPGMQNKAATRRSVPNPASTLTASQSNARPSPPTAATRATPAATPAAAAMGSGRQANIPPPPPPPPPSSKPKEPMFEAAYDFPGSGSPSELPLKKGDVIYITREEPSGWSLGKLLDGSKEGWVPTAYMKPHSGNNNIPTPPQNRDVPKPVLNSVQHDNTSANVIPAAAQASLGDGLANALAARANKMRLESDDEEANEDEEEDDW
Protein: Protein SYM1 (Stress-inducible yeast MPV17 protein 1) (Q06563)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cellular response to stress. Required to maintain mitochondrial DNA (mtDNA) integrity and stability. Required for ethanol metabolism and tolerance during heat shock.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:15189984}; Multi-pass membrane protein {ECO:0000269|PubMed:15189984}.
Interaction partners:
Sequence:
MKLLHLYEASLKRRPKTTNAIMTGALFGIGDVSAQLLFPTSKVNKGYDYKRTARAVIYGSLIFSFIGDKWYKILNNKIYMRNRPQYHWSNMVLRVAVDQLAFAPLGLPFYFTCMSIMEGRSFDVAKLKIKEQWWPTLLTNWAVWPLFQAINFSVVPLQHRLLAVNVVAIFWNTYLSYKNSKVMEKDKVPVHYPPVVE
Protein: RNA-binding region-containing protein 3 (RNA-binding protein 40) (F1Q8J0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprise less than 1% of all non-coding sequences.
Subcellular location: Nucleus {ECO:0000305|PubMed:24516132}.
Interaction partners:
- Small nuclear ribonucleoprotein 48
- Small nuclear ribonucleoprotein E
- Zinc finger matrin-type protein 5
- Splicing factor 3B subunit 6
- Zinc finger
- Zinc finger CCHC-type and RNA-binding motif-containing protein 1
- Small nuclear ribonucleoprotein G
- Splicing factor 3B subunit 1
- Small nuclear ribonucleoprotein polypeptide F.
- Splicing factor 3B subunit 4
Sequence:
MAETDEADVQTKKSKTLIIRHLPRELSRDEKEDLLKYFGASSVRVLSEKGPLKHMAFATFSSETSASKALNRLHQLRILGRTLVVEFAKDQDSASILKDPPVSDRTAAAVAEKEKKEKQQPSVPLMDTSIAPSLGLKFQTNPTLKYLYPPPSSGILTNITHTLLSVPKFYVQVLHLMNKMNLPSPFRPVTAPPPMFEMPSGPLPPPFPPENPPLPEHDESGSEEESEYESEDEEERERMIRLMGLVNQPCKRPLRTKTSSKRKKPKLKDLLFIPKPDSHGPSGPVLQPADVFEQPHALGQKKIEFHISSEVSAILEGPGQNQKLPFADATEDTPDMEVSAQETTEGFGKIYPSAQVPRQEEEQEEDEDIPSEFISRRELERGRLSRDEIKKLSVFKKYEPGEPTCRLYVKNVAKHVEEKDLKFIYGRYIDISSEEERNMFDIVLMKEGRMKGQAFIGLPSERSAQKALKETNGYVLKDKPLVVQFARSAKPKQESADPKKGGRKH
Protein: Major prion protein (Q53YK7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG
Protein: ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (F1T0B3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MAAFSVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (A0A1D8PFS4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Gluconokinase
- Transketolase
- 6-phosphogluconolactonase-like protein
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase
- Glucosamine/galactosamine-6-phosphate isomerase domain-containing protein
- Phosphoglycerate kinase
- Enolase 1
Sequence:
MSSAPKGDIGLIGLAVMGQNLILNMADHGYTVVAYNRTTAKVDRFLENEAKGKSILGAHSIKELVDQLKRPRRIMLLVKAGAPVDEFINQLLPYLEEGDIIIDGGNSHFPDSNRRYEELAKKGILFVGSGVSGGEEGARTGPSLMPGGNEKAWPHIKDIFQDVAAKSDGEPCCDWVGDAGAGHYVKMVHNGIEYGDMQLICEAYDLMKRVGKFEDKEIGDVFATWNKGVLDSFLIEITRDILYYNDPTDGKPLVEKILDTAGQKGTGKWTAVNALDLGIPVTLIGEAVFSRCLSAMKAERVEASKALKGPQVTGESPITDKKQFIDDLEQALYASKIISYTQGFMLMNQAAKDYGWKLNNAGIALMWRGGCIIRSVFLAEITAAYRKKPDLENLLLYPFFNDAITKAQSGWRASVGKAIQYGIPTPAFSTALAFYDGLRSERLPANLLQAQRDYFGAHTFKVLPGQENELLKKDEWIHINWTGRGGDVSSTTYDA
Protein: Putative defective protein IntQ (Putative lambdoid prophage Qin defective integrase) (P76168)
Organism: Escherichia coli (strain K12)
Function: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome (By similarity).
Interaction partners:
Sequence:
MITDVWKYRGKSTGELRSSVCYAIKTGVFDYAKQFPSSRNLEKFGEARQDLTIKELAEKFLALKETEVAKTSLNTYRAVIKNILSIIGEKNLASSINKEKLLEVRKELLTGYQIPKSNYIVTQPGRSAVTVNNYMTNLNAVFQFGVDNGYLADNPFKGISPLKESRTIPDPLSREEFIRLIDACRNQQAKNLWCVSVYTGVRPGELCALGWEDIDLKNGTMMIRRNLAKDRFTVPKTQAGTNRVIHLIKPAIDALRSQMTLTRLSKEHIIDVHFREYGRTEKQKCTFVFQPEVSARVKNYGDHFTVDSIRQMWDAAIKRAGLRHRKSYQSRHTYACWSLTAGANPAFIANQMGHADAQMVFQVYGKWMSENNNAQVALLNTQLSEFAPTMPHNEAMKN