wanglab/gogpt-training-data huggingface dataset:
Protein: 2,4,6-trihydroxybenzophenone synthase (GmBPS) (EC 2.3.1.220) (L7NCQ3)
Organism: Garcinia mangostana (Mangosteen)
Function: Type III polyketide synthase involved in the biosynthesis of benzophenones and xanthones. Produces mainly 2,4,6-trihydroxybenzophenone together with minor amounts of tetraketide lactone, triketide lactone and diketide lactone. The preferred substrate is benzoyl-CoA, but can also use acetyl-CoA, phenylacetyl-CoA, hexanoyl-CoA, cinnamoyl-CoA, p-coumaroyl-CoA and salicoyl-CoA.
Interaction partners:
Sequence:
MAPAMDSAQNGHQSRGSANVLAIGTANPPNVILQEDYPDFYFKVTNSEHLTDLKEKFKRICVKSKTRKRHFYLTEQILKENPGIATYGAGSLDSRQKILETEIPKLGKEAAMVAIQEWGQPVSKITHVVFATTSGFMMPGADYSITRLLGLNPNVRRVMIYNQGCFAGGTALRVAKDLAENNKGARVLVVCAENTAMTFHGPNENHLDVLVGQAMFSDGAAALIIGANPNLPEERPVYEMVAAHQTIVPESDGAIVAHFYEMGMSYFLKENVIPLFGNNIEACMEAAFKEYGISDWNSLFYSVHPGGRAIVDGIAEKLGLDEENLKATRHVLSEYGNMGSACVIFILDELRKKSKEEKKLTTGDGKEWGCLIGLGPGLTVETVVLRSVPIA
Protein: G2/mitotic-specific cyclin-A (P14785)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the Cdk1 and Cdk2 protein kinases to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 1
- Cell division control protein
- Dacapo
- Cell division cycle protein 20 homolog
- cyclin-dependent kinase
- S-phase kinase-associated protein 2
- Cyclin-dependent kinases regulatory subunit
- Double parked, isoform A
- Fizzy-related protein homolog
Sequence:
MASFQIHQDMSNKENPGIKIPAGVKNTKQPLAVIGGKAEKNALAPRANFAVLNGNNNVPRPAGKVQVFRDVRNLNVDENVEYGAKKSNVVPVVEQFKTFSVYEDNNDTQVAPSGKSLASLVDKENHDVKFGAGQKELVDYDLDSTPMSVTDVQSPMSVDRSILGVIQSSDISVGTETGVSPTGRVKELPPRNDRQRFLEVVQYQMDILEYFRESEKKHRPKPLYMRRQKDISHNMRSILIDWLVEVSEEYKLDTETLYLSVFYLDRFLSQMAVVRSKLQLVGTAAMYIAAKYEEIYPPEVGEFVFLTDDSYTKAQVLRMEQVILKILSFDLCTPTAYVFINTYAVLCDMPEKLKYMTLYISELSLMEGETYLQYLPSLMSSASVALARHILGMEMWTPRLEEITTYKLEDLKTVVLHLCHTHKTAKELNTQAMREKYNRDTYKKVAMMESVEMSKDDFDQLCEAYNCKQKEDEHQQPDINTKSNVNLFYKF
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q0IGS7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMILRSWDRVKPRSISDFACFLLVAVFVPVTYIFHVTIVMPELFAIGGIWYTLLWLASLFLIFNITSNMLACMLVDTSIRKELLKPPLDAAQLARWHSCQDCQTLVPPRSWHCEVCNVCVLKRDHHCRFTCCCIGHHNYRYFFYYLVYMIIGSLAAAIMESIYLWHLHLDIYWRWSTLFTIFAPVVSLMLSPSWESFYLVIYDLTLLGFAISSLLLVFHWSIFKSGSVTRERGTRKYDRGLRGNLEMVLGKRMHLTWLSPFLRSDLPHDGMNWEPIAAFSPKEE
Protein: At4g28530 (NAC domain containing protein 74) (NAM / CUC2-like protein) (Q8GUJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Expressed protein
- TRM32-like protein
- B3 domain-containing protein REM-like 3
- Transducin/WD40 repeat-like superfamily protein
- PLATZ transcription factor family protein
- Replication protein A 32 kDa subunit B
- DNA replication ATP-dependent helicase/nuclease JHS1
Sequence:
MGLKDIGSKLPPGFRFHPSDEELVCHYLCNKIRAKSDHGDVDDDDDDVDEALKGSTDLVEIDLHICEPWELPDVAKLNAKEWYFFSFRDRKYATGYRTNRATVSGYWKATGKDRTVMDPRTRQLVGMRKTLVFYRNRAPNGIKTTWIMHEFRLECPNIPPKEDWVLCRVFNKGRDSSLQDNNYYNNDNQTQRLEVNDAPDLNYNNQLPPLLSSPPHNHQHEKMKIQVCDQWEQLMKQPSRTTGHPYHHHCHHQTIACGWEQMMIGSLSSPSSHGPDHESLLNLLYVDNNNSVNISGDHHQNYEKILLSSLDMTSLDHDKTCMGSSSDGGMVSDLHMECGGLSFETENILAFQ
Protein: Ras-related protein Rab-43 (Ras-related protein Rab-41) (Q86YS6)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:18664496}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17562788}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:21255211}.
Interaction partners:
- USP6 N-terminal-like protein
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 3
Sequence:
MAGPGPGPGDPDEQYDFLFKLVLVGDASVGKTCVVQRFKTGAFSERQGSTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFRTITQSYYRSANGAILAYDITKRSSFLSVPHWIEDVRKYAGSNIVQLLIGNKSDLSELREVSLAEAQSLAEHYDILCAIETSAKDSSNVEEAFLRVATELIMRHGGPLFSEKSPDHIQLNSKDIGEGWGCGC
Protein: T-DNA border endonuclease VirD2 (EC 3.1.-.-) (P18592)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Tumor formation by A.tumefaciens involves the transfer and integration of a defined segment (T-DNA) of Ti plasmid DNA into the plant nuclear genome. The virD operon encodes a site-specific endonuclease that cleaves at a unique site within both 24 bp direct repeats flanking the T-DNA.
Interaction partners:
Sequence:
MPDRAQVIIRIVPGGGTKTLQQIINQLEYLSRKGRLELQRSARHLDIPLPPDQIHELARSWVQETGTYDESQPDEERQQELTTHIIVSFPAGTSQVAAYAASREWAAEMFGSGAGGGRYNYLTAFHIDRDHPHLHVVVNRRELLGHGWLKISRRHPQLNYDALRIKMAEISLRHGIALDASRRAERGITERPITYAQYRRLEREQARQIRFEDADLEQSSPQGDHPEFSQPFDTSPFEASAGGPEDMPRPNNRQNESQVHLQEPAGVSNEAGVLVRVALETERLAQPFVSETILADDIGSGSSRVAEGRVESANRTPDIPRAATEAATHTTHDRQRRAKRPHDDDGGPSGAKRVTLEGIAVGPQANAGEQDGSSGPLVRQAGTSRPSPPTATTRASTATDSLSATAHLQQRRGVLSKRPREDDDGEPSERKRERDERSKDGRGGNRR
Protein: Major intrinsically disordered Notch2-binding receptor 1 (Membrane integral NOTCH2-associated receptor 1) (Ubiquitination and mTOR signaling protein) (D3ZJ47)
Organism: Rattus norvegicus (Rat)
Function: Intrinsically disordered protein which may negatively regulate mTOR signaling pathway by stabilizing the mTOR complex component DEPTOR. Negatively regulates angiogenesis (By similarity). Negatively regulates cell growth (By similarity). Negatively regulates neurite outgrowth in hippocampal neurons.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UPX6}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UPX6}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
Sequence:
MEANQEASLFLVKILEELDSKQNTVSYQDLCKSLCAQFDLSQLAKLRSVLFYTACLDPNFPATLFKDKMKCSVNNQQSKKIMVAADIVTIFNLIQMNGGTAKEKLPTSCHKVRKEEASFESCRSDAEVCSPTVCEPLNCELSERPFSRGYPTRQSSKCRKMDCKECPQFVPASEPNFLLGVSKEVKNRAASLDRLQALSPYSVASPQPCEMQRTYFPMNIENESISDQDSLPIGQGIKETFISSEEPFMVQSCVQKRNIFKEDFHNLMTVSPSLVGTTNKAEEDHGEPRSQKELHKPPFFNHSFEMPYHSQYLNPVYSPIPDKRRAKHESLDDLQASTYFGPTPVMGTQDTRRCPGRPSKQTPWPAKSWSLNTEEVPDFERSFFNRNPSEEKLRYPNSGNQTPNFSGPDRHPVYLVPKDQQKVLPAGYAVKPNGLKSKEIPSPVDLEKHEAVKKFKDKSISCTSGQHSSDTSSVGTQTEQHVLDPPKCKDLCSAGQAKYSDRHAMKHSDDDSEIVSDDISDIFRFLDDMSISGSTGVIQSSCYNSTGSLSQLHKSDCDSSPEHNLAKITNGVSGSKGDKCNRPENVHHSEEELKSSVCKLVLRIGEIERKLESLAGVREEISQVLGKLNKLDQKIQQPEKVNVQIDLNSLTSEAPSDDSASPRVFHAHSGSHGPKLENSPDWCCSDVSGSNSESLRVKALKKSLFTRPSSRSLTEENSATESKIASISNSPRDWRTITYTNRMSLNEEEIKDAGPANNKDWHRKSKEADRQYDIPPQHRLPKQPKDGFLVEQVFSPHPYPSSLKAHMKSNPLYTDMRLTELAEVKRGQPSWNIEEYARNTGDKGKLTALDLQTQESLNPNNLEYWMEDIYTPGYDSLLKRKEAEFRRAKVCKIAALITAAACTVILVIVVPICTMKS
Protein: ADP-L-glycero-D-manno-heptose-6-epimerase (EC 5.1.3.20) (ADP-L-glycero-beta-D-manno-heptose-6-epimerase) (ADP-glyceromanno-heptose 6-epimerase) (ADP-hep 6-epimerase) (AGME) (P67910)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Interaction partners:
- Lipopolysaccharide heptosyltransferase 2
- Bifunctional protein HldE
- Lipopolysaccharide heptosyltransferase 1
- Phosphoheptose isomerase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Lipopolysaccharide heptosyltransferase 3
- O-antigen ligase
- Lipopolysaccharide glucosyltransferase WaaG
- Lipopolysaccharide core heptose
- Lipopolysaccharide glucosyltransferase WaaO
Sequence:
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADYMDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKLFEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADATLAYHKKGQIEYIPFPDKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLNRDA
Protein: Late cornified envelope protein 3E (Late envelope protein 17) (Q5T5B0)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 3D
- Small proline-rich protein 2A
- Late cornified envelope protein 2C
- Late cornified envelope protein 2D
- Small proline-rich protein 2G
- Late cornified envelope protein 1C
- Small proline-rich protein 2D
- Small proline-rich protein 2E
- Late cornified envelope protein 2B
- Late cornified envelope protein 1A
Sequence:
MSCQQNQKQCQPPPKCPSPKCPPKNPVQCLPPASSGCAPSSGGCGPSSEGGCFLNHHRRHHRCRRQRSNSCDRGSGQQGGGSGCCHGSGGCC
Protein: Sorbitol dehydrogenase (SDH) (XDH) (EC 1.1.1.14) (EC 1.1.1.9) (L-iditol 2-dehydrogenase) (Polyol dehydrogenase) (Xylitol dehydrogenase) (F7A1C3)
Organism: Equus caballus (Horse)
Subcellular location: Mitochondrion membrane {ECO:0000256|RuleBase:RU369026}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369026}. Cell projection, cilium, flagellum {ECO:0000256|RuleBase:RU369026}. Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. {ECO:0000256|RuleBase:RU369026}.
Interaction partners:
- Aldo-keto reductase family 1 member B1
- Hexokinase 1.
- Xylulose kinase
- hexokinase
- Hexokinase-3
- Ketohexokinase
- Hexokinase-2
- L-xylulose reductase
- Hydroxyacid-oxoacid transhydrogenase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MAAAKSENLSVVVHGPGDLRLENYLIPEPGPNEVLLKMHSVGICGSDVHYWEHGRIGHFVVKKPMVLGHEASATVVKVGSLVQHLKPGDRVAIEPGAPRETDEFCKIGRYNLSPSIFFCATPPDDGNLCRFYKHNASFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGNKVFVCGAGPIGLVTLLVAKAMGAAQVVVTDLSASRLSKAKELGADFILHISKESPQEIASKVEDLLGCKPEVTIECTGAEAAIQAGIYATRSGGTLVLVGLGSEMTTVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVTHRFPLEKALEAFETSKKGLGLKVMLKCDPDDQNP
Protein: Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2) (Q9N0Y2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against vesicular stomatitis virus (VSV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15767791}. Nucleus {ECO:0000250}.
Interaction partners:
- ISG15 ubiquitin like modifier.
- Ubiquitin carboxyl-terminal hydrolase
- Interferon-induced, double-stranded RNA-activated protein kinase
- Radical S-adenosyl methionine domain containing 2.
- Interferon induced protein with tetratricopeptide repeats 1.
- 2'-5'-oligoadenylate synthetase 1.
- Signal transducer and activator of transcription.
- 2'-5'-oligoadenylate synthetase 2.
- DExD/H-box helicase 58.
- Intersectin 2.
Sequence:
MSKAHGSRPYRRHNVVIPRQQPEKEMNFVQQQPPPSDAAARQMMYPPNCQVGVQDPVYLAKEFNLLTLNPQQLEGSRHQQMAKGPEKSLYSQYEQKVRPCIDLVDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKRDPHKAWRGRISYRKTELQFQDPSQVEKEIRQAQNIIAGQGLGISHELISLEITSPEVPDLTLIDLPGITRVAVGNQPQDIGVQIKALIKNYIQKQETINLVVVPCNVDIATTEALSMAQEVDPNGDRTIGVLTKPDLVDRGTEKTVVNVAQNLTYHLQKGYMIVRCRGQEEITNQLSLAEATEKERMFFQTHPYFRALLEEGKATVPCLAERLTKELILHINKSLPLLEKQIRESHQRATDELHQCGDSIPSNEADKMFFLIEKIKLFNQDIDKLIEGEEIVKKNETRLYNKIREEFEHWALVLTANTQKVKNIVSEEVSVYEKQYRGKELLGFVNYKTFETIVHQYIEQLVEPALTMLRKTIEIVWQAFTDTAKKHFSVFSNLSQTIQNKIEDIKTRQAETAENLIRLQFRMEQLVYCQDQIYSVVLRKVRKEVFNPAGKAAQDLQLKFPFPKDLPSMSSNDEIGVHLNAYFLETSKRLANQIPFIIQYFVLQENGSCLQKAMMQILQEREQYSWLLQEHADTSAKRRFLKEKIYRLAQARRALYMFFS
Protein: Aldo-keto reductase family 1 member A1 (EC 1.1.1.2) (EC 1.1.1.372) (EC 1.1.1.54) (Alcohol dehydrogenase [NADP(+)]) (Aldehyde reductase) (Glucuronate reductase) (EC 1.1.1.19) (Glucuronolactone reductase) (EC 1.1.1.20) (S-nitroso-CoA reductase) (ScorR) (EC 1.6.-.-) (P14550)
Organism: Homo sapiens (Human)
Function: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde. Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). Displays no reductase activity towards retinoids (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6}.
Interaction partners:
- Inositol oxygenase
- Aldehyde dehydrogenase family 3 member A2
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member B1
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member B2
- Glycerol kinase
Sequence:
MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY
Protein: Vanadium-binding protein 2 (EC 1.13.-.-) (Q86BW2)
Organism: Ascidia sydneiensis samea (Vanadium-rich ascidian)
Function: Acts as a vanadium reductase which may form an electron transfer cascade in conjunction with NADPH and glutathione through thiol disulfide exchange reactions. Partial cleavage of its disulfide bonds results in the reduction of V(5+) to V(4+). Binds up to 24 V(4+) ions per protein at pH 7.5. Also binds Fe(3+) and Cu(2+) and, to a lesser extent, Co(2+), Zn(2+) and Ni(2+).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17116994}.
Interaction partners:
Sequence:
MSKVIFALVLVVVLVACINATYVEFEEAYAPVDCKGQCTTPCEPLTACKEKCAESCETSADKKTCRRNCKKADCEPQDKVCDACRMKCHKACRAANCASECPKHEHKSDTCRACMKTNCK
Protein: Dishevelled segment polarity protein 3a (Segment polarity protein dishevelled homolog DVL-3a) (B8JMI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Axin-1
- Vang-like protein 2
- Vang-like protein
- Axin-2
- Dishevelled-associated activator of morphogenesis 1a.
- Protein naked cuticle homolog 1
- Protein naked cuticle homolog 2-like
- Glycogen synthase kinase-3 beta
- Disheveled-associated activator of morphogenesis 1b
- Glycogen synthase kinase-3 beta
Sequence:
MGETKVIYHLDDQETPYLVKLPIPAERVTLLDLKNALKKPNYKFFFKSMDDDFGVVKEEITDDNAKLPCYNGRVICWLVSSDGSHSDGCSVAESQSERPPSHERSQGIGDSRPPSFHPKAAGSRHGVDDETETDSVVSHRRDRDRDRSRRKHSHEHSGGKQNGYSRGGRGMDLGGYDICDSRSSLMSSELESSSCFDSDDGSTSRFSSVTEQSGSSKLMTKKPRRRRRKTRAQQMERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDINFENMCNDDAVRVLREIVHKPGPVSLTVAKCWDPNPNSCFALPRSEPIRPIDPAAWVSHTAAMTGVYPPYGMSPSMSTVTSTSSSISSSIPETERFDDYHLSVHSDMATVAKAMACPDSGLEVRDRMWLKITIANAFIGSDVVDWLFHHVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLSGNMAHLSLQDHDGSSGASDQDTLAPLLHPAEAPWPAAFPYQYPAAHSHLEEAGGGSAGSQQSEGSSGSNCSWSRTEGKTAAGDFRLGGGSEMGDAHEFDFRRDRAPSERSGVPPSEGSVRSSRSHSYSLKQGSARGGPGSPSGRHLAHIPPELTGSRRSCNTANGEFFVDIM
Protein: Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Q5ZI23)
Organism: Gallus gallus (Chicken)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: [Isoform 1]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16775}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q16775}.
Interaction partners:
- Lactoylglutathione lyase
- RING-type E3 ubiquitin transferase
- Uncharacterized protein.
- Uncharacterized protein.
- NSF attachment protein alpha
- Fibrinogen-like protein 1-like protein
Sequence:
MLGGGWRSLGTALVALGAGALLRAGPAQLRAVFLHTEHEQRKSKTVAQANMKVEVLPALTDNYMYLLIDEETKEAAIVDPVQPQKVLDAVKKHGVKLTSVLTTHHHWDHAGGNEKLVKLETGLRVYGGDSRVGALTQKVSHLTSLKVGSLNVKCLCTPCHTSGHICYYVTKPNSSEPPAVFTGDTLFVAGCGKFFEGTPEEMYRALIEILGSLDPETRVYCGHEYTINNLKFARHVEPNNVSIQEKLAWAKAKYDSGEPTIPSTIAEEFTYNPFMRVREKTVQEHAGETDPIRTMGAIRKEKDNFRVPKD
Protein: Peptidyl-prolyl cis-trans isomerase CYP20-1 (PPIase CYP20-1) (EC 5.2.1.8) (Cyclophilin of 20 kDa 1) (Rotamase CYP20-1) (Rotamase cyclophilin-7) (Q9SP02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Seems to be involved in root development.
Subcellular location: Endoplasmic reticulum {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- Vesicle-associated protein 2-2
- At4g10270
- At1g09850
- Cysteine proteinase RD21A
- Probable cysteine protease RD21C
- Probable cysteine protease RD21B
- Small ribosomal subunit protein uS19u
- Tetratricopeptide repeat
- Pre-mRNA-splicing factor SYF2
Sequence:
MASSVTLLLWSLLLLGTLSAIQAKKSKENLKEITHKVYFDVEIDGKAAGRIVMGLFGKTVPKTVENFRALCTGEKGIGKNGKALHYKGSSFHRIIPSFMLQGGDFTHGNGMGGESIYGEKFADENFKLKHTGPGFLSMANAGQDTNGSQFFITTVTTSWLDGRHVVFGKVVTGMDVVYKVEAEGNQSGTPKSKVVIVDSGELPL
Protein: Stac-like, isoform J (A0A0B4KEV7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein unc-13 homolog 4B
- Voltage-dependent calcium channel type D subunit alpha-1
- Uncharacterized protein
- HDC09916
Sequence:
MGISAHAAPASFWNHPRRIRRTPTSDRDGVDQCRPWICRRKDRRPAHPAANRPPESRVCGPSSTFRWDDWAAPAPRTRERATDCARMCMCTSRIPYSVARICARTTSMHSSRPASRSSSFIRRPLTRRQRMAVGGVTRRLWRTMRVYTIHQGRGVRRARAAQAVAAYLRDRRARIGKGWPAQGHGVRISATEQWADKPVVRRPGDPTRRVAAGAVPVLAERLPKVTGSSVKSSSGRRSRRRRIFGWRGPRGGSLSPQGGSMASYNGVLKDYSHSSLNEAFKSQNNVNFKLIKTVSDFSETLSRLYEEHATALQVAVSNYRKKNAELRKERPACHLAIFQAWETFLQEVETDSQACNDVASVLSRQVSRPMLDKSFHRKVQSRKIFTHRESFETIIAKTEEKLSKCRVDYKQCHLAHRQNPSQHSLTEYIDAHNAYVQQLHATNGMLEAYHTDTLPQQMQELEEIHNDLVAIVSDSLMQGAEVIAGKANDQAKRYNSLSNQCAAVSPQQDLVNFVRLLAQPSQAQKIPRRLFASPQAEVGEEAGDHNEMTPCLRNELVFDRHSTLSQRSALESLKREAIELELQIRQLQDSIEALNRTQTRGIEGQLYNKVNELQEDLSMKKFDLRAKQIHLAAIRAQKDLFVSKVEPTSPRNERKFSAATAPSMKTKWLKAFKSLKPAGSGSAQQADSQPPRQNQMYHAVSTVLTLRRNGASSTASEPLRPNLDGSHHLQEYTYKKITACDVCSQILRGHTRQGLRCRICKLNAHGDCAPNLPRCQPKQKLLRRQKSTSELENRVDIEEETGADKSVQAKQMDGSVAGGSALPVPVLSERELGRAPPPDIPIVSVSELALQEQQQQQQQQQQQHQQQQRSLASVAQAAAVRAGRGVRPPPVAMPILGVQLQQQELQQQRGGLPVPSQDISSSSAPHSPRRQKLNLRMKSLSLDSPESSELHGQFRRRTQLPGTGASTSAGSGYYHGGSGGHLEHSTPPSNNSRLHSPSSPSHPGRKLLYATRGMRGGSVDLPDEMEKSQSSASTSPCLSPKTHRLLPTNLYVIIYNFKARHADELDLKAGYKVTVIDNSDPDWWKGKVLGRVGYFPSKYCVRLNANEKPLQVTHNLQVSDSERGENLTLLRDQIVIQTGDEVNGMVMIRAAEHGQGYCPIKYLQEVXQPEEDEPPSDERDRPHKSSMQTSSSRTADKTKRRIRIVVSENHNVAASSVAPAPPTTAFNTTTHHQIPRESDIETKRLNIDYGDEGSADWDKDREVLILSGRRNKNDKNWENWERIREQKLEKMKGICFESYRQSKRDKLLQAKPRPKQLDSTWYTDNIYSNRSDDMDEDYVPDCLKYGPFRTLRDIHELDEKSGVTEERRVEGEGSPGYGLHRSKSCKEFQYPKSQSWCFEGNVFEAGGGVASGSGSSSGAPPPTTSILKNRAGVPKSYSFSATTKTMPFDIIDYELPPVSNTRREKKEALRRNMNALCSSSLDRCCARDQCTSARCLLEDIYPGSRMRPRTTGAGSNRNLSAADWLFEERAGRQRTPAAPTVICCCSAAEDCCCHRQRQQQPPLPARPRSRPLCPGHHPAAEEEEHMHCRYDTDLEHFIRAERERLMLQDKFLDDDERYLAAAPAPRSPGRRYPAGNYHRPPRSKSLLEMQPPTILYDEDTCSDTTEIDLEDFNIDLEKYWEQLDKPPSPINMDMRRNMHSSLKVKNVNVRCYNNGQPIDLHDREHERLMIKKSLLEGMPSPPQLDSSESSTNAGGYPFFDTAPAVAPAPAFHHHPAYGQPQGYGHKVYPTVDTLPSYQYNNFYPEHSHPTVGSVLTQQPTAGIHHPSAGGHSALSLINNIFSIYKPNKYSPENCQMNYESKPEPCKKMNVPSTHRPLGAAAHPYPAHDYMHSSMKRPLLVSADQPHFKIIPEKTGLKISPLLSYEDYGGGGGGEKAHHRLTSTARPLMLPHXWCWTFPWYGNGNGNGNYC
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (P9WFT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
Interaction partners:
- Arginine--tRNA ligase
- Leucine--tRNA ligase
- Phenylalanine--tRNA ligase beta subunit
- Valine--tRNA ligase
- Isoleucine--tRNA ligase
- Methionine--tRNA ligase
- Aspartate--tRNA
- Glutamate--tRNA ligase
- Putative 3-methyladenine DNA glycosylase
- Threonine--tRNA ligase
Sequence:
MSGMILDELSWRGLIAQSTDLDTLAAEAQRGPMTVYAGFDPTAPSLHAGHLVPLLTLRRFQRAGHRPIVLAGGATGMIGDPRDVGERSLNEADTVAEWTERIRGQLERFVDFDDSPMGAIVENNLEWTGSLSAIEFLRDIGKHFSVNVMLARDTIRRRLAGEGISYTEFSYLLLQANDYVELHRRHGCTLQIGGADQWGNIIAGVRLVRQKLGATVHALTVPLVTAADGTKFGKSTGGGSLWLDPQMTSPYAWYQYFVNTADADVIRYLRWFTFLSADELAELEQATAQRPQQRAAQRRLASELTVLVHGEAATAAVEHASRALFGRGELARLDEATLAAALRETTVAELKPGSPDGIVDLLVASGLSASKGAARRTIHEGGVSVNNIRVDNEEWVPQSSDFLHGRWLVLRRGKRSIAGVERIG
Protein: CD164 sialomucin-like 2 protein (Q6UWJ8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEAPGPRALRTALCGGCCCLLLCAQLAVAGKGARGFGRGALIRLNIWPAVQGACKQLEVCEHCVEGDGARNLSSCVWEQCRPEEPGHCVAQSEVVKEGCSIYNRSEACPAAHHHPTYEPKTVTTGSPPVPEAHSPGFDGASFIGGVVLVLSLQAVAFFVLHFLKAKDSTYQTLI
Protein: SH3 domain-containing protein (Q59U90)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- RVS161-like protein RVS162
- Abp1p
- Regulator of cytoskeleton and endocytosis RVS161
- Regulator of cytoskeleton and endocytosis RVS167
Sequence:
MVVDQLKNNIVSISSNIGTHIKDGYKYTESEFKNISYNIKDTVTFHTRDYDKDDELVEIYYHDIKQSVSGLKYITSQNHHLSKSFLPHVLSSNIKIIKGFINLIGQDSLRFDKINEYYQEFDSWQATQEIPHVHPKEMQFLNESINEELNNYLITVENLKFDLENNWEAYDESLKYRIDEMKKYLKKTLKLIKKRNMKRTEQDHLHRKIEKLNQKAIPLDEKDNDKLEKLETTYQTVDAAFNSLNKKCIQLLPNIVSFLDEFVENITKMILCQQLETFKKLTDTFQYFTEFYGLIKENSPKSYTEIIDDWESNSTATRLQIESLLTIVHEKHPDLLDKEINDEDSSSNYYRFWRNMSNKFVEKKHVVNTKDKVNGIFNDTLEIDPLVAYKQYQDPSMNPSETYHPRKLVDEEDIKVPAVPKKDGPELPPRSNTAIVRHSVLVSPMSSAGASRLYSISTDSMDSISLSDFEDESATIMSEASSISSMSSVSYSNHDSSEAKLRRIYNGSKNEIKESPITTKPIQYEPFTFEKPMSLTYKLNLIQSFFEKLNINTDNKVLKTAKYDFSGYEPGDLSFKQGDNIEILLDFQNIDTLYHSDELNWLIGVSRIDDESYRIGFVPNNYVE
Protein: Large ribosomal subunit protein uL14 (50S ribosomal protein L14) (P56039)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Interaction partners:
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS8
Sequence:
MIQSFTRLNVADNSGAKEIMCIKVLGGSHKRYASVGSVIVASVKKAIPNGKVKRGQVVKAVVVRTKKEIQRKNGSLVRFDDNAAVILDAKKDPVGTRIFGPVSREVRYANFMKIISLAPEVV