wanglab/gogpt-training-data huggingface dataset:
Protein: Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (MMP-X1) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT1-MMP) (MT1MMP) (P50281)
Organism: Homo sapiens (Human)
Function: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8015608}; Single-pass type I membrane protein {ECO:0000305}. Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasm {ECO:0000269|PubMed:22065321}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Forms a complex with BST2 and localizes to the cytoplasm (PubMed:17081065). {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 2
- 72 kDa type IV collagenase
- Acireductone dioxygenase-requiring))
- Proheparin-binding EGF-like growth factor
- Metalloproteinase inhibitor 3
- Radixin
- CD44 antigen
- Apolipoprotein A-I
- Furin
Sequence:
MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV
Protein: Coronin-B (Coronin-7) (DdCRN7) (Doublecoronin) (Q55E54)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in phagocytosis and cell motility. Binds to actin filaments and protects them against depolymerization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20071332}. Cell projection {ECO:0000269|PubMed:20071332}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20071332}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20071332}. Note=Accumulates in cell surface projections during movement, phagocytosis and pinocytosis. Detected at the leading edge of the cell during chemotaxis.
Interaction partners:
Sequence:
MFKVSKYRHTVGKIDKRELWYPDVNTTGNSSASTFIKANSKWVALNWQSNTGTIGLIPLKSFGKRKGETFLIHAHSSGVIDFEFNPFNEHQLVTASDDSTIKVWNIDEAIRSGATSLSSASIVCSGHSKSVECIAFNPVANNILASCSADKTLKIWDLSNGEEKYSWNFEQGSLTSLSWNYDGSLLVATGKDLKNRIIDARTGESIQVGDGNQGVKASRVVWLGNLNHFLTAGFSKMRERQLVLWSSQDLSKPIKSITLDSSTGIISPIYDQDAQLLFISGSGDSSVRVFDMNTQFTKDPAFTELSPVPSDTPSKGICALPKRALDVMEVEIDRIFKATPNNIIPITFNMSRKSKSTFADDLFPNTASTKPSLSSIDWLSGENKQPILVSLNPSDNQINNDLDDLQLNDNEPVKKSTFFIDDNTNDNSNVVEQSKSEPEQQQQEEKKISSSSSSSSPTNSSSNVINSTPSSPIVNDNIQRTGIVPKVVRSSKYRHISGSAHQKSQFYTNLKINGSTSNTCIAVNSEYVAVPMVGIGGPLAVIPLADKGRQIQVPCIEIGSQLCDYDLSQHNTSLVATGSEDSHVKVFKIPTGGIPKTTANKSNNYTTTEADFVGHNRKVISVNFHPTAENVLITSGGDMVVKLWDLNEGGAGEKLSFANVHTDMITSVDVNWTGDKILTSSKDKKMRIFDPRTNKGGLASETVTHSGSKGGKAVWLGQTGNIFSVGFNKSSEREYQLWDSRNLQSGTPLASDKLDHLSGVITPFYDEDSGVIYLAGKGDSSIRMFEINDQEPYVHYLTQFSAGTPQVGVAKFAKKTSMDVKKCEIARFYRSTDSTIEPLSMTVPRNRQEFFQDDIYPDTRQTCTPVMTSEEWFDGCIREPEFVSMKPSDMINLSDAPPPPKKEDKFVVSQEVDNTPSRDQVTNSLLSRVSNQNASSNWEQIEKLKHNFTDYDNGDISDSEWD
Protein: Protein lsb5 (P87308)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for the organization of the actin cytoskeleton, fluid phase endocytosis and vesicle trafficking.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SH3 domain-containing protein PJ696.02
- Glutaredoxin-1
- Probable clathrin heavy chain
Sequence:
MGIFSETVPITAVTTYIDRLTSRDTDDEDLSGIVQLSEAVNLTVTGPREASRTLRKKLKYSTPHEQVRALVILQALIENAGSHFLQNFSDEKLEDRMLQCATNSEYSKPVRKRAIHMIKLWHNDYSNVRGMESMSSLVSRLPQRQSSASHSEQPTINLKKVGPILERLIASSSMAATNLSNSLVRINPNTENPAKNKQIMVYYVDCKRAHRSLLRYIQAIQDEMWLANLLKANDEIVTAIDAFKEKCSENSDYSSDSGSYSSSYSRHLDDRASYISRSSSGGSNAQRSEDLDVNNPFGDHNRLE
Protein: Sphingosine N-acyltransferase (Q5A879)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alkaline dihydroceramidase
- Sphingosine hydroxylase
- Sphinganine kinase
- Sphingolipid delta
- 3-ketodihydrosphingosine reductase TSC10
- Sphinganine kinase
- Lac1p
Sequence:
MSSSSSSLGVPHENPIRHRSSSVGRIDVGDTSASLSTMPTTRSSRRRSIARLKELQDNSTTDSAIVHKLYVGFRELTYRHTWIIPLIVLLMAFGTYYLSSPSGKVHQVLEDMIIPSYHIPGTDQYGKGGNDFKFVGFYAIFFTFLREFMMCCVLRPISVWFGIKKEAKQKRFLEQTYAMFYYGITGPFGLWIMRRLPLWYFNTTQFYINYPHKTHDIYFKIYYLGQAAFWVQQSVVLILQLEKPRKDFKELVLHHIITIALIWCSYRFHFTWMGLAVYITMDISDFFLALSKTLNYLESPITGPFFVIFIGVWIYLRHYINLQILWSVLTEFRTVGDFELNWITQQYKCWISQPITFFLIFALQLVNFYWLVLIFRILYRYVFTGVSKDERSDDEDEDEDSEDSADEKKKEQ
Protein: Transmembrane protein 182 (Q6ZP80)
Organism: Homo sapiens (Human)
Function: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1 (By similarity). Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0A1D5NY17}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRLNIAIFFGALFGALGVLLFLVAFGSDYWLLATEVGRCSGEKNIENVTFHHEGFFWRCWFNGIVEENDSNIWKFWYTNQPPSKNCTHAYLSPYPFMRGEHNSTSYDSAVIYRGFWAVLMLLGVVAVVIASFLIICAAPFASHFLYKAGGGSYIAAGILFSLVVMLYVIWVQAVADMESYRNMKMKDCLDFTPSVLYGWSFFLAPAGIFFSLLAGLLFLVVGWHIQIHH
Protein: Sugar transporter family protein (O06339)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTVSIAPPSRPSQAETRRAIWNTIRGSSGNLVEWYDVYVYTVFATYFEDQFFDRADRNSTVYVYAIFAVTFVTRPVGSWFLGRFADRRGRRAALTFSVSLMAACSLIVALVPSRSSIGVAAPILLILCRLVQGFATGGEYGTSATYMSEAATRERRGYFSSFQYVTLVGGHVLAQFTLLVILAVFTREQVHEFGWRIGFAVGGGAAIVVFWLRRTMDESLSQERLTAIKAGRDHDSGSLRELATHYWKPLLLCFLVTLGGTVAFYTYSVNAPAIVKSVYGSQAMTATWINLVGLILLMMLQPIGGMISDKIGRKPLLLWFGVGGLIYTYVLVTYLPETRSPTMSFLLVAVGYVILTGYCSINALVKSELFPAHVRALGVGVGYALANSVFGGTAPLIYQALKERDQVPMFIAYVTACIAVSLIVYVFFIKNKADTYLDREQGFAFYGHA
Protein: Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein] (P04601)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.
Subcellular location: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19912576}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19912576}.
Interaction partners:
Sequence:
MGGKWSKSSVIGWPTVRERMRRAEPAADRVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKIEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC
Protein: Cell division cycle-associated protein 3 (Gene-rich cluster protein C8) (Trigger of mitotic entry protein 1) (TOME-1) (Q99618)
Organism: Homo sapiens (Human)
Function: F-box-like protein which is required for entry into mitosis. Acts by participating in E3 ligase complexes that mediate the ubiquitination and degradation of WEE1 kinase at G2/M phase (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Borealin
- Cyclin-dependent kinase 1
- Ubiquitin-conjugating enzyme E2 C
- Baculoviral IAP repeat-containing protein 5
- Disks large-associated protein 5
- Lymphokine-activated killer T-cell-originated protein kinase
- Cyclin-A2
- G2/mitotic-specific cyclin-B1
- Aurora kinase B
Sequence:
MGSAKSVPVTPARPPPHNKHLARVADPRSPSAGILRTPIQVESSPQPGLPAGEQLEGLKHAQDSDPRSPTLGIARTPMKTSSGDPPSPLVKQLSEVFETEDSKSNLPPEPVLPPEAPLSSELDLPLGTQLSVEEQMPPWNQTEFPSKQVFSKEEARQPTETPVASQSSDKPSRDPETPRSSGSMRNRWKPNSSKVLGRSPLTILQDDNSPGTLTLRQGKRPSPLSENVSELKEGAILGTGRLLKTGGRAWEQGQDHDKENQHFPLVES
Protein: Relaxin 3 (Relaxin-like peptide locus B) (B1AC67)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- G_PROTEIN_RECEP_F1_2 domain-containing protein.
- Relaxin family peptide receptor 1
- G-protein coupled receptors family 1 profile domain-containing protein
- Neuropeptide Y receptor type 5
- Protein-L-isoaspartate O-methyltransferase domain-containing protein 1
- Neuropeptide S
Sequence:
MGAKLRLLCAAAALLSVAVPGQPGAQGALVPAGDGDGYGVKLCGREFIRAVIFTCGGSRWKRLSLMAMEPAPAADSSQAASNNLLGRFKMQSAVGPEMQRSNSFLGLETLKDLYSLNDYNEYESMADDFKELLRQLEEAAQGDGGGAGVAPLGPSSYPWARYPRRKRESLGLAGMCCKWGCTKAEISTICRV
Protein: Golgi apparatus membrane protein tvp18 (O74375)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Golgi membrane protein involved in vesicular trafficking.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nuclear transport factor 2
- COPII coat assembly protein sec16
- GTP-binding nuclear protein spi1
Sequence:
MFESIIVDRAKTTFLGELKSYNFSIYAQWLGILSIFLCIILGIVNLFHVTLVVLFSALTIIEGVLLIFIELPFLSRICPVSDKFQAFTNAFASNYYRGLVYFIFSVVTFLSCIFMATSLIATGIVLALTGLCYTFAGIKGQAFTSSSTLGGTGITTETPPSTMV
Protein: L-demethylnoviosyl transferase (EC 2.4.1.302) (Novobiocin biosynthesis protein M) (Q9L9F5)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: Catalyzes the transfer of L-noviose from dTDP-4-O-demethyl-beta-L-noviose to the phenolic oxygen of novobiocic acid, creating the full ABC ring system in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases. Also shows activity with variant coumarin aglycones, suggesting it may be a promiscuous catalyst for noviosylation of a range of planar scaffolds. Does not show activity with TDP-L-rhamnose.
Interaction partners:
Sequence:
MRVLLTSLPGIGHLFPMVPLGWALQAAGHTVLVATDREFLPVVTGAGLSATAVLDPVDPVELFKPVEPFGDPLSPAERTGHRCAEAGVRALPAMRALVDVWHPDLVIAEPMELAGPAAATNAGVPWVRHSYGLIPPGPLLSVAAEVLDAELAVLGLSALAKPARTIDVCPDSLRPSDGVATVPMRYVPYNGPAGVPDWLLAGPPARPRVCLTLGTSLPRRDPHVAPLWRLLLDELVALGQEVVIAIDESHRPLLGHLPDGVRAARIPLCDLLPTCTAIVHHGGSGSTMAAASFGVPQLVVPHFADHFTNAERLTAVGAGLSLPHDTDDLARISAACELITGDGPHRAISRRLADENARRPTPAVVAEGLAAEQRSMTPA
Protein: SsrA-binding protein (Small protein B) (O32230)
Organism: Bacillus subtilis (strain 168)
Function: Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation (By similarity). Required for trans-translation. Probably required for sporulation; deletion of the gene for tmRNA impairs sporulation via its effect on trans-translation, and as smpB is required for trans-translation under non-stress conditions, it is also probably required during sporulation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00023}.
Interaction partners:
- Ribonuclease R
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein bL27
- Small ribosomal subunit protein uS11
Sequence:
MPKGSGKVLSQNKKANHDYFIEETYETGIVLQGTEIKSIRAGRVNLKDSFAKIERGEVFLHNMHVSPYEQGNRYNHDPLRTRKLLMHRKEINKLIGLTKEKGYSLVPLKLYLKNGFAKVLLGLGKGKKNYDKREDLKRKDAKREIERAFRDSQKGF
Protein: Cell division protein FtsZ homolog 1, chloroplastic (AtFtsZ1) (AtFtsZ1-1) (Chloroplast FtsZ) (CpFtsZ) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 10) (Protein PLASTID MOVEMENT IMPAIRED4) (Q42545)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits GTPase activity. Component of the plastid division machinery that forms a contractile ring at the division site. Required for plastid division in a dose-dependent manner. Involved in epidermal plastids division in a MINE1-dependent manner. Involved in blue light-induced chloroplast movements. May regulate thylakoid development. In the vegetative shoot apex, at the shoot apical meristem (SAM), where the proplastid-to-chloroplast transition takes place, contributes equally with FTSZ2-1 in the L2 layer to plastid division.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:26500667, ECO:0000269|PubMed:29967285}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481}; Peripheral membrane protein. Note=Forms a contractile ring at the chloroplast midpoint that coaligns with FTSZ2-1 rings (PubMed:25731613, PubMed:26500667, PubMed:29967285). Exhibits a dynamic trunover in FtsZ ring facilitated by ARC3-mediated destabilization (PubMed:25731613). {ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:26500667, ECO:0000269|PubMed:29967285}.
Interaction partners:
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- Plastid division protein CDP1, chloroplastic
- Cell division topological specificity factor homolog, chloroplastic
- Dynamin-like protein ARC5
- Septum site-determining protein minD homolog, chloroplastic
- Plastid division protein PDV2
- Plastid division protein PDV1
- Protein MULTIPLE CHLOROPLAST DIVISION SITE 1
- Epimerase family protein SDR39U1 homolog, chloroplastic
Sequence:
MAIIPLAQLNELTISSSSSSFLTKSISSHSLHSSCICASSRISQFRGGFSKRRSDSTRSKSMRLRCSFSPMESARIKVIGVGGGGNNAVNRMISSGLQSVDFYAINTDSQALLQSSAENPLQIGELLTRGLGTGGNPLLGEQAAEESKDAIANALKGSDLVFITAGMGGGTGSGAAPVVAQISKDAGYLTVGVVTYPFSFEGRKRSLQALEAIEKLQKNVDTLIVIPNDRLLDIADEQTPLQDAFLLADDVLRQGVQGISDIITIPGLVNVDFADVKAVMKDSGTAMLGVGVSSSKNRAEEAAEQATLAPLIGSSIQSATGVVYNITGGKDITLQEVNRVSQVVTSLADPSANIIFGAVVDDRYTGEIHVTIIATGFSQSFQKTLLTDPRAAKLLDKMGSSGQQENKGMSLPHQKQSPSTISTKSSSPRRLFF
Protein: Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase) (P97519)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis. Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38060}. Peroxisome {ECO:0000250|UniProtKB:P38060}. Note=Unprocessed form is peroxisomal. {ECO:0000250|UniProtKB:P38060}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Methylglutaconyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Dehydrogenase/reductase SDR family member 6
- Acetoacetyl-CoA synthetase
Sequence:
MATVRKAFPQRLVGLASLRAASTSSMGTLPKRVKIVEVGPRDGLQNEKSIVPTPVKIKLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSIFGAASELFTRKNVNCSIEESFQRFDGVMQAARAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVLHEVPVAALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLTGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL
Protein: Uncharacterized protein At5g22530 (Q9FK86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Disease resistance protein TAO1
Sequence:
MSTGCLSCFKVMCFKKKQSKKEAKPVKTEILPEPVGEKEDVERKEGIQAKPLRTEGLPEPVEKKKKDVKYSACKKMPEKCMFKPKPEWISHVGSNDVGPKVGDFYGDHYAETDDSSSSMTNEFNKVKTFDIRGVKLATS
Protein: UDP-glucuronosyltransferase 2B4 (UDPGT 2B4) (UGT2B4) (EC 2.4.1.17) (HLUG25) (Hyodeoxycholic acid-specific UDPGT) (UDPGTh-1) (P06133)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of the endogenous estrogen hormones such as estradiol and estriol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8333863}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 2D6
- Cytochrome P450 1A1
- Cytochrome P450 2A6
- Cytochrome P450 2E1
- Cytochrome P450 3A5
- Beta-glucuronidase
- Sulfotransferase 1E1
- Cytochrome P450 2A13
Sequence:
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSASISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFNDILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAIEKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVLGRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTMSSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Protein: mRNA-decapping enzyme subunit 2 (AtDCP2) (Protein DECAPPING 2) (EC 3.6.1.62) (M(7)GpppN-mRNA hydrolase DCP2) (Protein TRIDENT) (Q8GW31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Essential for postembryonic development, especially during the formation of the shoot apical meristem (SAM).
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:17158604, ECO:0000269|PubMed:17485080, ECO:0000269|PubMed:17513503}. Note=The localization to P-body is VCS-dependent.
Interaction partners:
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- mRNA-decapping enzyme-like protein
- Enhancer of mRNA-decapping protein 4
- Protein decapping 5
- D-aminoacyl-tRNA deacylase
- Sm-like protein LSM4
- DEAD-box ATP-dependent RNA helicase 12
- DEAD-box ATP-dependent RNA helicase 6
- Regulator of nonsense transcripts 1 homolog
- Sm-like protein LSM2
Sequence:
MSGLHRSSSSSKNIGNCLPSKELLDDLCSRFVLNVPEEDQQSFERILFLVEYAYWYYEDNAVENDPKLKSLSLKEFTSLLFNSCDVLRPYVTHIDDIFKDFTSYKCRVPVTGAIILDETYERCLLVKGWKGSSWSFPRGKKSKDEEDHACAIREVLEETGFDVSKLLKREEYIEFVFRQQRVRLYIVAGVTEDTVFAPLTKKEISEITWHRLDHLQPASNEVITHGVSGLKLYMVAPFLSSLKSWILKHPSPVARRPNKPLKALCVWNARTSVGGNGTATVESQNRKSELRTTTMESNSRKPELKRTTMESHSTKPELRKGTMESHNTTATVESHNTKPVVDHSQDIKPGGSFINFKFNQSVILQALESGNSA
Protein: Killer cell lectin-like receptor subfamily C, member 1 (Natural killer cell receptor NKG2B) (Q9WU32)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MSNERVTYAELKVAKNSRNQHRKPRGPRSSISVIEQEIIYSDFSFQNPSQEHPWICRNCPCKGFPSPPEKLIAGTLGLICFVLIVAVVVITTVATPYINYTLSSAQPCPHCPKEWISYSHNCYFIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLISWTGILRKGRGQPWVWKEDSIFKPKIAEILHDECNCAMMSASGLTADNCTTLHPYLCKCKFPI
Protein: PBAN-type neuropeptides (Pheromone/pyrokinin biosynthesis-activating neuropeptide) [Cleaved into: TSQDITSGMWFGPRL-amide (Pyrokinin-1); QITQFTPRL-amide (Pyrokinin-2); IYLPLFASRL-amide; VPWTPSPRL-amide] (A8CL69)
Organism: Apis mellifera (Honeybee)
Function: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:17068263}.
Interaction partners:
Sequence:
MIGFAVFSSFNRFTTIFVCVLLCVVYLLSYASGEYDGRDSSSGSNNDRAPSNEFGSCTDGKCIKRTSQDITSGMWFGPRLGRRRRADRKPEINSDIEAFANAFEEPHWAIVTIPETEKRQITQFTPRLGRESGEDYFSYGFPKDQEELYTEEQIYLPLFASRLGRRVPWTPSPRLGRQLHNIVDKPRQNFNDPRF
Protein: Lrrk2 protein (Q5BJM3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
AAEKESWVVCGTQSGALLVINAEDETRRHTLDKMTDSVTCLYCNSFAKQSKQSHFLLVGTADGNLMIFEDKTIKCKGAAPLKTLHIGDVSTPLMCLSESMNSSERHITWGGCGTKIFSFSNDFTIQKLIETRTNQLFSYSAFSDSNIIAVAVDTALYIAKKNSPVVEVWDKKTEKLCELIDCVHFLKEVMVKINKDSKHKLSYSGRVKALCLQKNTALWIGTGGGHILLLDLSTRRVIRTIHNFCDSVRAMATAQLGSLKNVMLVLGYKRKSTEGTQEQKEIQSCLSIWDLNLPHEVQNLEKHIEVRTELADKMRKTSVE
Protein: Photosystem II reaction center protein J (PSII-J) (P0C415)
Organism: Oryza sativa subsp. indica (Rice)
Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01305}.
Interaction partners:
- Photosystem II reaction center protein L
- Photosystem II reaction center protein I
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein T
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein Z
- Photosystem II reaction center protein K
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein H
- Photosystem II CP47 reaction center protein
Sequence:
MADTTGRIPLWLIGTVTGIAVIGLIGVFFYGSYSGLGSSL