wanglab/gogpt-training-data huggingface dataset:
Protein: Superoxide dismutase [Fe] 2, chloroplastic (EC 1.15.1.1) (Protein ALBINO OR PALE GREEN 8) (Protein FE SUPEROXIDE DISMUTASE 2) (Q9LU64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD3.
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000269|PubMed:18996978}.
Interaction partners:
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 3
- Superoxide dismutase 1
- Superoxide dismutase 3, chloroplastic
- Superoxide dismutase 1, mitochondrial
- Superoxide dismutase 2, mitochondrial
- Superoxide dismutase 1, chloroplastic
- Large ribosomal subunit protein uL29m
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Large ribosomal subunit protein mL46
Sequence:
MMNVAVTATPSSLLYSPLLLPSQGPNRRMQWKRNGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P00396)
Organism: Bos taurus (Bovine)
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:27605664, ECO:0000269|PubMed:31533957}; Multi-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b
Sequence:
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKREVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK
Protein: 26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A) (Q9SGW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. May help to control the degradation of one or more factors that repress cytokinin signaling. Plays an important role for balancing cell expansion with cell proliferation rates during shoot development.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 6A homolog A
- Proteasome subunit beta type-6
- 26S proteasome regulatory subunit 6A homolog B
- Proteasome subunit beta type-4
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
Sequence:
MDPQLTEVSQQFERFKAAFARKDYNTCSDLLSQLKVLLTKFTSLPPLFENSPNAAKELTIARDIYEHAVVLSVKTEDQDAFERDFFQLKPYYVDARNRIPQSPQENLILGLNLLRLLVQNRIAEFHTELELLSSATLEDPCIKHAVELEQSFMEGAYNRVLSARQTAPDATYVYFMDLLAKTIRDEIAGCSEKAYDYVSISDARQMLLFSSDQELLTYVTDEHPEWEVKEGFVVFQKAKETAPCKEIPSLQLINQTLSYARELERIV
Protein: SKP1-like protein 16 (AtSK16) (O81055)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-like protein 3
- Cullin-2
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Cullin-3A
Sequence:
MSSNKIVLTSSDDESFEVEEAVARKLKVIAHMIDDDCADKAIPLENVTGNILALVIEYCKKHVLDDVDDSDDSTEATSENVNEEAKNELRTWDAEFMKEFDMETVMKLILAVNYLNVQDLLGLTCQTVADHMKDMSPEEVRELFNIENDYTPEEEDAIRKENAWAFEDLK
Protein: Peroxiredoxin-1 (EC 1.11.1.24) (Thioredoxin-dependent peroxiredoxin 1) (P0CB50)
Organism: Gallus gallus (Chicken)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
Interaction partners:
- Thioredoxin
- Sulfiredoxin-1
- Superoxide dismutase
- NME/NM23 family member 8
Sequence:
MSSGKAFIGKPAPDFTATAVMPDGQFKDIKLSDYRGKYVVFFFYPLDFTFVCPTEIIAYSDRADEFKKINCEIIGASVDSHFCHLAWINTPKKQGGLGTMKIPLVSDTKRVIAKDYGVLKEDEGIAYRGLFIIDEKGILRQITINDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK
Protein: UDP-glucuronosyltransferase (EC 2.4.1.17) (F1QM88)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Membrane {ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein {ECO:0000256|RuleBase:RU362059}.
Interaction partners:
Sequence:
MACLWLLGSLLLLGSAEAGKLLVIPTDGSHWLGLKPIVEELGRRGNQVVVVIPEASLSMGPSEKTTTLTYPVNYTKVELEAVLASELNALLSIDVSTDLAKFQSFFFTLNVLQTFILRNAEGLLFNKDLMKKLQDYNFDAILTDPFEPVGAIAGEYLSIPAIYMQINHPCGVDTLASQCPAPPSYVPQTFTHFTDRMNLWQRSINFVRALLQPKACKLIFARADEIASHLLQRKTSMVEIFSRAALWFLRFNFALEFPRPVMPNMVMIGATVNQKPKPLTHELEEFVNGSGEHGFVVFTLGSMVSQLPEAKAREFFEAFRQIPQRVLWRYTGPVPENAPKNVKLMKWLPQNDLLGHPKVRAFVTHGGSHGIYEGICNGVPMVMLPLFGDQGDNAQRLVSRGVAESLTIYDVTSEKLLVALKKVINDKSYKEKMMKLSAIHRDRPIEPLDLAVFWTEFVMRHKGAEHLRPAAHDLNWIQYHSLDVIGFLLLILLTVIFVTVKSCMFCFRKCFKKSQKKKKA
Protein: Uncharacterized protein C6orf47 (Protein G4) (O95873)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFLRRLGGWLPRPWGRRKPMRPDPPYPEPRRVDSSSENSGSDWDSAPETMEDVGHPKTKDSGALRVSGAASEPSKEEPQVEQLGSKRMDSLKWDQPISSTQESGRLEAGGASPKLRWDHVDSGGTRRPGVSPEGGLSVPGPGAPLEKPGRREKLLGWLRGEPGAPSRYLGGPEECLQISTNLTLHLLELLASALLALCSRPLRAALDTLGLRGPLGLWLHGLLSFLAALHGLHAVLSLLTAHPLHFACLFGLLQALVLAVSLREPNGDEAATDWESEGLEREGEEQRGDPGKGL
Protein: Peroxisome assembly protein, putative (Q57U74)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peroxisomal ATPase PEX1
- Peroxisomal membrane protein PEX14
- Peroxisome targeting signal 1 receptor
- Peroxin-13
- RING-type E3 ubiquitin transferase
- Peroxisome assembly protein, putative
- Peroxin-7
- Peroxin 19
- Polyubiquitin, putative
Sequence:
MMSRTVELERCILRTKTYEAYKNVLQQSTSMTDNAQSLVNTLIQTHGEIHLGEKIPSGDGRPVEFVVVDLVPATVGTLTESTTVIVLPPSSDGKELPPTAAMGTTGSSAEGTGADGVSTNNELERGGICSVRLDYSLSGSSTAASEAFLLSTLLQDGSIVCVGDEEYTTAFTLVRQRDDPVPTTEQQEQAETQRRKQQCDTLPTLYASPSVFRNIRAFLMLDVLPTIMKSRFQYNDDQLCVPVSLFREVHNGSGAPITIEAVSSGSRKELHLSAVAVTPAWPVFILTEVFGESYETLLTATLKASERALHGRIVAEGDVIVLSVTPTQLVEMQLEPNTAVEAVLVQVIHAVQSGCALPAVVTSVLHDGAIAIPFRVLEVNTLSGAAYGRIELEDKGNGTELLLLLQNALASPDTTPLFPPPPTPPTFFPQLSLTMNIRSALERCYVPSNAGTTSVFVVHATKENLPVECVSMVMALLGVECLLVDMERKSDEEVQRLLGAYMSCSGEVALVIRNAQKLDQRTELLRLFDADNSGNGVDGTCSDGDCLNGIRVIFLVCECVEAPPPAVAAQARNVEGVLKGTHPSEKDRRFIVENIFTGAQRSRGFCKSLLLSFDSVASWTVGLSTVDVVAYAEECVSVLASMSLPDGVLPVLSESLCSSILEKFQKAHGHNLVSTKLQPVRWSDVGGLEDAKRELREMIQLPLLYPELLGNGGNAKHGAGILFYGPPGCGKTLLAKAVATEMNMNFMAVKGPELINQYVGESEKNIRLLFQRARDNSPCIIFFDELDALAPARGAKGDAGGAMDRVVAQLLVEVDGVGHSRSDGTAAGKVFIIAATNRPDLLDPALLRPGRFDKLCYLGIPSTRSEQLVALRALTRKFHLAEDVDLEALLQPMTLDYTGADLFALCSDAMMFAVEAMLQESLTFNEEGSPSMLAEPAKNLVVRMNDFVRARDQLKPSVTAEDLRRYESLRTKFTANSGRVAD
Protein: Lon protease (EC 3.4.21.53) (ATP-dependent protease La) (A0A059VAZ3)
Organism: Meiothermus taiwanensis
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
Interaction partners:
Sequence:
MRLELPVIPLRNTVILPHTTTPVDVGRAKSKRAVEEAMGADRLIFLVAQRDPEVDDPAPDDLYTWGVQAVVKQAMRLPDGTLQVMVEARARAQVTDYIPGPYLRARGEVFSEIFPIDEAVVRVLVEELKEAFEKYVANHKSLRLDRYQLEAVKGTSDPAMLADTIAYHATWTVAEKQEILELTDLEARLKKVLGLLSRDLERFELDKRVAQRVKEQMDTNQREYYLREQMKAIQKELGGEDGLSDLEALRKKIEEVGMPEAVKTKALKELDRLERMQQGSPEATVARTYLDWLTEVPWSKADPEVLDINHTRQVLDEDHYGLKDVKERILEYLAVRQLTQGLDVRNKAPILVLVGPPGVGKTSLGRSIARSMNRKFHRISLGGVRDEAEIRGHRRTYIGAMPGKLIHAMKQVGVINPVILLDEIDKMSSDWRGDPASAMLEVLDPEQNNTFTDHYLDVPYDLSKVFFITTANTLQTIPRPLLDRMEVIEIPGYTNMEKQAIARQYLWPKQVRESGMEGRIEVTDAAILRVISEYTREAGVRGLERELGKIARKGAKFWLEGAWEGLRTIDASDIPTYLGIPRYRPDKAETEPQVGTAQGLAWTPVGGTLLTIEVAAVPGSGKLSLTGQLGEVMKESAQAALTYLRAHTQDYGLPEDFYNKVDLHVHVPDGATPKDGPSAGITMATAIASALSRRPARMDIAMTGEVSLRGKVMPIGGVKEKLLAAHQAGIHKIVLPKDNEAQLEELPKEVLEGLEIKLVEDVGEVLEYLLLPEPTMPPVVQPSDNRQQPGAGA
Protein: Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Q10488)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38071}.
Interaction partners:
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
- Fatty acid synthase subunit alpha
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Probable octanoyltransferase
- Uncharacterized protein C22H10.11c
Sequence:
MSFFKTAVRRFSSTSITRGMAKAIAYSEYGNPKEVLRAVSYNVPKCSKNQVNVRFLASPINPSDINQIQGVYPSKPPFTNDVCSSKPSAVAGNEGLVEVVDVGDQFKGTFSPGQWAILGSVNLGSWRTEMNIDGRSLVPVDKSAFPSIAEAATLSVNPCTAYCLLQHVVQLNKGDWFIQDGANSMVGIATIQLAKHFGYKSINVVRNRPDIEKLKEQLKSLGATIVITDEELMDRKTMKQKVPEWIQGGEVKLGIDCVSGRVAAEMAKYMSKGATMATFGGMSRQPLPVPVSLLIFKNLKFHGFWVTKWKSEHPEEFLKIIHKVEDFYRNGTLKTVNTELVSLKEDADEKTFLDTFLNAIEGHGKKIIKFEH
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (Q6IQG3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Alkyl transferase
- Geranylgeranyl diphosphate synthase 1
- CAAX prenyl protease 2
- CAAX prenyl protease 2
- All trans-polyprenyl-diphosphate synthase PDSS1
- CAAX prenyl protease
- Farnesyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Prenyl
Sequence:
MEEAPPSLRCFQESHSSELFNDDGLQTVTSREQRKVERSIQEVYSVYQQIHTSPQPALLREQHYHYLKKGLRHLSDAYECLDASRPWLCYWILHSLELLEEPVPAAVASDVCQFLARCQAPTGGFGGGPGQQAHLAPTYAAVNALCILGTEEAYNVINRETLLDFLYSVKQPDGSFVMHIGGEVDVRSAYCAASVASLTNIIAPTLFDGTHNWIISCQNWEGGLGGVPGLEAHGGYTFCGTAALVILGKEHMLDLKALLRWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALFKEGDSTLSVSSWMFERKALQEYILLCCQNPGGGLLDKPGKSRDFYHTSYCLSGLSVAQHFGNKDLHNELILGRDENKLAPTHPVYNICPEKVARAVEYFHRLPVPIPTGATASAMDQS
Protein: Accessory gland-specific peptide 70A (Paragonial peptide B) (Sex peptide) (SP) (P05623)
Organism: Drosophila melanogaster (Fruit fly)
Function: Male seminal protein which triggers short- and long-term post-mating behavioral responses (PMR) in female Drosophila. Binds initially to sperm where it is later cleaved to release an active peptide within the female reproductive tract. Signals via the sex peptide receptor (SPR) in female flies; may also act via other receptors. Moderates the activity of distinct neuronal circuitries in the female genital tract to promote specific PMRs including: enhanced ovulation, increased egg laying rate, increased feeding/foraging rate, induced antimicrobial peptide synthesis, reduced mating receptivity, reduced day-time sleep and reduced lifespan in multiple mated females.
Subcellular location: Secreted {ECO:0000269|PubMed:3135120}.
Interaction partners:
- Sex peptide receptor
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp62F
- Accessory gland protein Acp36DE
- Accessory gland protein Acp29AB
- ACP53C14A
- ACP53C14B
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp63F
- Accessory gland protein Acp76A
Sequence:
MKTLALFLVLVCVLGLVQSWEWPWNRKPTKFPIPSPNPRDKWCRLNLGPAWGGRC
Protein: WRKY transcription factor WRKY62 (OsWRKY62) (XA21-binding protein 10) (Q6EPZ0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Regulates negatively basal innate immunity and XA21-mediated defense against X.oryzae pv. oryzae (Xoo).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223, ECO:0000269|PubMed:19825552, ECO:0000269|PubMed:22735448}.
Interaction partners:
- Receptor kinase-like protein Xa21
Sequence:
MDDDGDGSSSPTDDSAAAGLLPLFSRSPAEDLEEKLRRAMEENARLTRALDAILAGHHAHQRALLAPSLSPPPPSATARAPSVSTSCAAREDAAPAVAAAAASTACPSRQQPPTAEPRPKVRTVRVRADAADATDANSMAETVKDGYQWRKYGQKVTRDNPYPRAYFRCAFAPSCPVKKKLQRCAEDRSMLVATYEGEHNHALSTQTTEFVASGCTTSQHAGGSSSSPLPCSISINSSGRTITLDLTNQAGSGSIASCGVEAAAVSGELVTVLSPELRRHLVEEVVQVLKNDAEFVEAVTNAVAARVVDQIPHIPVHL
Protein: Large ribosomal subunit protein uL24m (39S ribosomal protein L24, mitochondrial) (L24mt) (MRP-L24) (Q3SYS0)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10751423}.
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL4m
- 40S ribosomal protein S30
Sequence:
MRLSALLALASKVTLPPNYRYGMSRPGSLADKKKNPPGTRRRRVAVEPIPEEDWHLFCGDRVEILEGKDAGKQGKVVQVIRQRNWVVVEGLNTHYRYVGKTVDFRGTMVPSEAPLLHNQVKLVDPMDRKPTEVEWRFTEAGERVRVSTRSGRIIPKPDVPRADGIVPETWIDGPKDTSVEDALEKTYVPRLKTLEEEVMEAMGIQETRRHKKVYWY
Protein: Trypsin inhibitor 1 (BevuTI-I) (Trypsin inhibitor I) (C0HLV1)
Organism: Beta vulgaris subsp. vulgaris (Beet)
Function: Inhibits trypsin (IC(50)=471 nM).
Interaction partners:
Sequence:
CTPSGTICSPEAPEQCCSNSCVPHQWLRIFVCA
Protein: ATP-binding cassette subfamily C member 4 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (Multidrug resistance-associated protein 4) (F1M3J4)
Organism: Rattus norvegicus (Rat)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:12883481}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O15439}; Multi-pass membrane protein {ECO:0000255}. Note=Its localization to the basolateral or apical membranes is tissue-dependent. {ECO:0000250|UniProtKB:O15439}.
Interaction partners:
- Organic anion transporter 3
- Solute carrier family 22 member 7
- Hepatic sodium/bile acid cotransporter
- Solute carrier family 22 member 6
Sequence:
MLPVHTEVKPNPLQDANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKEVLRAKKDARKPSLTKAIVKCYWKSYLILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFFPSAIERVSEAVVSVRRIKNFLLLDELPERKAQEPSDGKAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDFQLLEDGDRLVIGDRGARLSGGQKARVNLATAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSPVPGTPTLRNRTFSEASIWSQQSSRPSLKDGVPDAQDAENTQAAQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNLMGQVFYVLQDWWLSHWANRQGALNDTKNANGNVTGTLDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECRKRPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHSDEELWKALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQQLGKGEAAALTETAKQVYFRRNYPDIAFSSPAVMSTSNGQPSALTIFETAL
Protein: Pepsin A-3 (EC 3.4.23.1) (Pepsinogen-3) (P0DJD8)
Organism: Homo sapiens (Human)
Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Subcellular location: Secreted.
Interaction partners:
- Pepsin A-4
- Pepsin A-5
- Vitamin K-dependent protein C
- Gastric triacylglycerol lipase
Sequence:
MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWKAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA
Protein: RNA-binding protein FXR2 (FXR2P) (FMR1 autosomal homolog 2) (P51116)
Organism: Homo sapiens (Human)
Function: RNA-binding protein.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q61584}. Cytoplasm {ECO:0000269|PubMed:9259278}. Postsynapse {ECO:0000250|UniProtKB:Q9WVR4}. Note=Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity). Localization to the post-synaptic region is dependent on FMR1 (By similarity). {ECO:0000250|UniProtKB:Q61584, ECO:0000250|UniProtKB:Q9WVR4}.
Interaction partners:
- Cytoplasmic FMR1-interacting protein 1
- Cytoplasmic FMR1-interacting protein 2
- RNA-binding protein FXR1
- Fragile X messenger ribonucleoprotein 1
- Heterogeneous nuclear ribonucleoprotein K
- Poly
- Tudor domain-containing protein 3
- Protein argonaute-2
- FMR1-interacting protein NUFIP1
- Endoribonuclease Dicer
Sequence:
MGGLASGGDVEPGLPVEVRGSNGAFYKGFVKDVHEDSVTIFFENNWQSERQIPFGDVRLPPPADYNKEITEGDEVEVYSRANEQEPCGWWLARVRMMKGDFYVIEYAACDATYNEIVTLERLRPVNPNPLATKGSFFKVTMAVPEDLREACSNENVHKEFKKALGANCIFLNITNSELFILSTTEAPVKRASLLGDMHFRSLRTKLLLMSRNEEATKHLETSKQLAAAFQEEFTVREDLMGLAIGTHGANIQQARKVPGVTAIELGEETCTFRIYGETPEACRQARSYLEFSEDSVQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRVEGDNDKKNPREEGMVPFIFVGTRENISNAQALLEYHLSYLQEVEQLRLERLQIDEQLRQIGLGFRPPGSGRGSGGSDKAGYSTDESSSSSLHATRTYGGSYGGRGRGRRTGGPAYGPSSDVSTASETESEKREEPNRAGPGDRDPPTRGEESRRRPTGGRGRGPPPAPRPTSRYNSSSISSVLKDPDSNPYSLLDTSEPEPPVDSEPGEPPPASARRRRSRRRRTDEDRTVMDGGLESDGPNMTENGLEDESRPQRRNRSRRRRNRGNRTDGSISGDRQPVTVADYISRAESQSRQRPPLERTKPSEDSLSGQKGDSVSKLPKGPSENGELSAPLELGSMVNGVS
Protein: Solute carrier family 7 (cationic amino acid transporter, y+ system), member 15 (Q8BZV2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTAVPLVTILYVLVNISYLLVMSPSEILSSDAIAVIWGDRVLGSWAWLVPLAVALSTFGTVNGGFFSGSRVCYAAAREGHMPQLMSMIHVNRLTPAPAQIFTTAVALLLVIPGNFSTFVNLLSFLSWLTYGTTFACLLYLRIKTKNLPHTYKVPTFIPAIMLLVSLYLVLAPIIDHPQIEFLYIFLFVLSGFPVYFLLFHFQCQFKCIQTATMHLQLLLEVAPTTKDH
Protein: Ubiquitin carboxyl-terminal hydrolase MIY1 (EC 3.4.19.12) (Deubiquitinating enzyme MIY1) (Q08930)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has endodeubiquitinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyubiquitin
- Ubiquitin carboxyl-terminal hydrolase 15
Sequence:
MDLSFTTKSVKINGQNHRILLQNENGPCALLALANILILSPDHTRFSNELIRLVNKGSQISLKELIEVLADIALQVTDKPSTDISELLSLLPRLHEGLNINPEFNGSFENTKEMSIFRLFNVDVVHGWVINSFINENIDEKLSHYSYESAQRILTQAADINCGISQDENSDEVLRDAMHLGLFLNESPTQLTAFGLLRLREKLLHNKFSILFRNDHFSTLFKYEDRLYTLVTDFGYKNCKDIVWQSLDSVDGSCDAFFAGNFSAAEVNGQQLSTDIERDFGTGNLLLEEIQQIENDKELAKQLQEQEQERVTKFEAKRKIHSHKKNSEIHAPVKKDKFKRRSSLLNAKASEKEKSECVVM