wanglab/gogpt-training-data huggingface dataset:
Protein: Serine hydroxymethyltransferase (SHMT) (Serine methylase) (EC 2.1.2.1) (Q72CT0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
Interaction partners:
- aminomethyltransferase
- Glycine cleavage system H protein
- Bifunctional protein FolD
- glycine dehydrogenase
- Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative
- Phosphoribosylglycinamide formyltransferase
- Probable glycine dehydrogenase
- L-serine ammonia-lyase
- Methionyl-tRNA formyltransferase
- Methylenetetrahydrofolate reductase
Sequence:
MDELLLQDPEVGKAIILEIERQTGKLELIASENFVSAAVRQAQGSVLTHKYAEGYPGKRYYGGCEFVDIAENIAIERARTIFGCEYANVQPHSGSQANMGVYFACLKPGDTILGMNLSHGGHLTHGSPVNFSGRLFNVVFYGVEKETGRIDYEQVAALAREHKPSLIVAGASAYPRTIDFARFRAIADEVGAKLMVDMAHIAGLVAAGYHPSPVQHAHYTTTTTHKTLRGPRGGMILSTEDNGKTLNSQIFPGIQGGPLMHVIAAKAVAFGEALRPAFKEYQKQVVDNAAALAGVLTAAGFDLVSGGTDNHLMLVDLTSKDVTGKDAEIALDKAGITVNKNTVPFETRSPFVTSGVRLGTPALTTRGMKAAEMEKVGGWIVDAIANTTNETRLAEISREVERFARQFPLFAW
Protein: Glutaredoxin-1 (O36032)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides (By similarity).
Interaction partners:
- Glutathione peroxidase-like peroxiredoxin gpx1
- Thioredoxin-1
- Protein lsb5
- Glutathione reductase
- Ribonucleoside-diphosphate reductase large chain
Sequence:
MSSVESFVDSAVADNDVVVFAKSYCPYCHATEKVIADKKIKAQVYQIDLMNNGDEIQSYLLKKTGQRTVPNIFIHQKHVGGNSDFQALFKKGELDSLFNTA
Protein: RNA polymerase-binding transcription factor DksA (Q9KKG5)
Organism: Pseudomonas aeruginosa
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}.
Interaction partners:
Sequence:
MSTKAKQQSSQQMTRGFEPYQETKGEEYMSERMRAHFTAILNKWKQELMEEVDRTVHHMQDEAANFPDPADRASQEEEFSLELRARDRERKLIKKIDETLQLIEDEEYGWCDSCGVEIGIRRLEARPTATLCIDCKTLAEIREKQLGS
Protein: Isotocin receptor-like 1 (Oxytocin receptor b) (Oxytocin receptor like) (E4W698)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}.
Interaction partners:
- Oxytocin
- Isotocin receptor-like 2
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MESLLKDVILWPINDSWANSSRGNDSRGLNQTVNPLKRNEEVAKVEVTVLVLILLLALAGNLCVLVAIQTSKHGQSRMYYFMKHLSIADLVVAVFQVLPQLIWDITFRFYGPDFLCRLVKYLQVVGMFASTYMLVLMSIDRCLAIWQPLRSLRRRKDRFYVLASWIISLLFSLPQVYIFSLREVGDGVFDCWGDFVQPWGAKAYVTWISLTIYIIPVAILSVCYGLISYKIWQNFRLKTRRDQCLSLTPRPTKGAALSRVSSVKLISKAKIRTVKMTFVIVMAYIICWTPFFFVQMWSAWDPMAPREAMAFIIAMLLASLNSCCNPWIYMFFAGHLFRDLMQRCLTVSHCGCKRHWRNKNHSGTGAMRSSSSQKSVTQSSTT
Protein: Sodium/hydrogen exchanger 3 (Na(+)/H(+) exchanger 3) (NHE-3) (Solute carrier family 9 member 3) (P26432)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15888551}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Cell membrane {ECO:0000269|PubMed:16540524}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Recycling endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Early endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Note=In intestinal epithelial cells, localizes to the ileal brush border (PubMed:28495796). Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity). {ECO:0000250|UniProtKB:Q28362, ECO:0000269|PubMed:28495796}.
Interaction partners:
- Na
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Na
- Solute carrier family 26 member 3
- Ezrin
- Calcineurin like EF-hand protein 1
- EF-hand domain-containing protein
- Na
- Carbonic anhydrase 2
- Sodium/glucose cotransporter 1
Sequence:
MSGRGGCGPCWGLLLALVLALGALPWTQGAEQEHHDEIQGFQIVTFKWHHVQDPYIIALWVLVASLAKIVFHLSHKVTSVVPESALLIVLGLVLGGIVLAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFSNLGSILLYAVVGTVWNAATTGLSLYGVFLSGIMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFQSFVTLGGDKVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRVIEPGFVFIISYLSYLTSEMLSLSSILAITFCGICCQKYVKANISEQSATTVRYTMKMLASGAETIIFMFLGISAVDPLIWTWNTAFVLLTLLFVSVFRAIGVVLQTWLLNRYRMVQLELIDQVVMSYGGLRGAVAFALVALLDGNKVKEKNLFVSTTIIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPKLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWANFDRRFLSKLLMRQSAQKSRDRILNVFHELNLKDAISYVTEGERRGSLAFIRSPSTDNMVNVDFSTPRPSTVEASVSYLLRESASAVCLDMQSLEQRRRSVRDAEDVITHHTLQQYLYKPRQEYKHLYSRHVLSPSEDEKQDKEIFHRTMRKRLESFKSAKLGLGQSKKATKHKRERERAQKRRNSSVPNGKLPLDSPAYGLTLKERELELSDPEEAPDYYEAEKMSGGIEFLASVTKDTTSDSPAGIDNPVFSPDEDLAPSLLARVPPWLSPGEAVVPSQRARVQIPYSPGNFRRLAPFRLSNKSVDSFLLAEDGAEHPESTHM
Protein: Proteasome 26S subunit, non-ATPase 14 (A0A8I6AHX8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
Protein: 2-oxoadipate dehydrogenase complex component E1 (E1a) (OADC-E1) (OADH-E1) (EC 1.2.4.-) (2-oxoadipate dehydrogenase, mitochondrial) (Alpha-ketoadipate dehydrogenase) (Alpha-KADH-E1) (Dehydrogenase E1 and transketolase domain-containing protein 1) (Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial) (A2ATU0)
Organism: Mus musculus (Mouse)
Function: 2-oxoadipate dehydrogenase (E1a) component of the 2-oxoadipate dehydrogenase complex (OADHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoadipate (alpha-ketoadipate) to glutaryl-CoA and CO(2) catalyzed by the whole OADHC. Catalyzes the irreversible decarboxylation of 2-oxoadipate via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Can catalyze the decarboxylation of 2-oxoglutarate in vitro, but at a much lower rate than 2-oxoadipate. Responsible for the last step of L-lysine, L-hydroxylysine and L-tryptophan catabolism with the common product being 2-oxoadipate.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96HY7}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Glutaryl-CoA dehydrogenase, mitochondrial
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MASAATVAAAGRALRRAVLLLRRGYQTERGVYGYRPRKAKSGEPRGDRARPSVDHGLARLVTVYCEHGHKAAQINPLFPGQALLDTVPEIQALVRTLQGPFTTTGLLNLGKEAASLEEVLAYLNHIYCGPISIETAQLQSQEERDWFARRFEELKKETFTTEERKYLSKLLLESQEFDHFLATKFATVKRYGGEGAESMMGFFHELLKLSAYGGITDIIIGMPHRGRLNLLTGLLQLPPELMFRKMRGLSEFPENVATIGDVLSHLTSSVDLDFGAHQPLHVTMLPNPSHLEAVNPVAVGKTRGRQQSREDGDYSPNGSAQPGDKVICLQVHGDASFCGQGIVLETFTLSNLPHFRIGGSIHLIVNNQLGYTTPAERGRSSLYSSDIGKLVGCAIIHVNGDSPEEVVRATRLAFEYQRQFRKDVIVDLLCYRQWGHNELDEPFFTNPVMYKIIRARKSIPDTYAEHLIASGLMTQEEVSDIKTSYYTKLNDHLANVAHYSPPATNLQARWQGLVQPEACVTTWDTGVPLELLRFIGVKSVEVPEELQVHSHLLKMYVQSRMEKVKNGSGLDWATAETLALGSLLAQGFNVRLSGQDVGRGTFSQRHAMVVCQDTDDAYIPLNHMDPNQKGFLEVSNSPLSEEAVLGFEYGMSIESPTLLPLWEAQFGDFFNGAQIIFDTFISGGEAKWLLQSGLVILLPHGYDGAGPEHSSCRIERFLQMCDSAEEGVDSDTVNMFVVHPTTPAQYFHLLRRQMIRNFRKPLIVASPKMLLRYPAAVSTLEEMAPGTAFKPVIGDSSVDPKNVKTLIFCSGKHFYALLKQRESLGTKKHDFAIIRLEELCPFPLDALQQEMSKYKHVRDVIWSQEEPQNMGPWSFVSPRFEKQLACRLRLVSRPPLPAPAVGIGTVHQQQHEDILSKTFTQ
Protein: Lysophospholipid acyltransferase LPEAT1 (EC 2.3.1.23) (EC 2.3.1.51) (EC 2.3.1.n6) (EC 2.3.1.n7) (Lysophosphatidylethanolamine acyltransferase 1) (AtLPEAT1) (Q8L7R3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates. Exhibits strong acylation activity on lysophosphatidylethanolamine (LPE) and lysophosphatidate (LPA), and lower activity on lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS). Exhibits acylation activity on both LPE and LPC. Has a preference for 18:1-LPE over 16:0-LPE as acceptor. Palmitoyl-CoA (16:0-CoA) is a better acyl donor than oleoyl-CoA (18:1-CoA). Among several different acyl-CoA species the best acyl donor is palmitoyl-CoA (16:0-CoA). Activity is calcium-independent. Its activity is essential for maintaining adequate levels of phosphatidylethanolamine (PE), LPE and LPC in the cells, which is crucial for plant growth regulation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33809440, ECO:0000305|PubMed:22923678}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lysophospholipid acyltransferase 1
- Lysophospholipid acyltransferase 2
- Lysophospholipid acyltransferase LPEAT2
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- Triacylglycerol lipase SDP1
- Cardiolipin synthase
- Phospholipase A2-alpha
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase A
Sequence:
MESELKDLNSNSNPPSSKEDRPLLKSESDLAAAIEELDKKFAPYARTDLYGTMGLGPFPMTENIKLAVALVTLVPLRFLLSMSILLLYYLICRVFTLFSAPYRGPEEEEDEGGVVFQEDYAHMEGWKRTVIVRSGRFLSRVLLFVFGFYWIHESCPDRDSDMDSNPKTTSTEINQKGEAATEEPERPGAIVSNHVSYLDILYHMSASFPSFVAKRSVGKLPLVGLISKCLGCVYVQREAKSPDFKGVSGTVNERVREAHSNKSAPTIMLFPEGTTTNGDYLLTFKTGAFLAGTPVLPVILKYPYERFSVAWDTISGARHILFLLCQVVNHLEVIRLPVYYPSQEEKDDPKLYASNVRKLMATEGNLILSELGLSDKRIYHATLNGNLSQTRDFHQKEE
Protein: Meckelin (Meckel syndrome type 3 protein) (Transmembrane protein 67) (Q5HYA8)
Organism: Homo sapiens (Human)
Function: Required for ciliary structure and function. Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in centrosome migration to the apical cell surface during early ciliogenesis. Involved in the regulation of cilia length and appropriate number through the control of centrosome duplication. Is a key regulator of stereociliary bundle orientation (By similarity). Required for epithelial cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (SFTPC). Involved in the negative regulation of canonical Wnt signaling, and activation of the non-canonical cascade stimulated by WNT5A. In non-canonical Wnt signaling, it may act as ROR2 coreceptor (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17185389}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19815549}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:17185389}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22121117}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:22121117). {ECO:0000269|PubMed:22121117}.
Interaction partners:
- Transmembrane protein 216
- Coiled-coil and C2 domain-containing protein 2A
- B9 domain-containing protein 1
- Tectonic-like complex member MKS1
- Centrosomal protein of 290 kDa
- Tectonic-2
- B9 domain-containing protein 2
- Nephrocystin-1
- Tectonic-1
- Jouberin
Sequence:
MATRGGAGVAMAVWSLLSARAVTAFLLLFLPRFLQAQTFSFPFQQPEKCDNNQYFDISALSCVPCGANQRQDARGTSCVCLPGFQMISNNGGPAIICKKCPENMKGVTEDGWNCISCPSDLTAEGKCHCPIGHILVERDINGTLLSQATCELCDGNENSFMVVNALGDRCVRCEPTFVNTSRSCACSEPNILTGGLCFSSTGNFPLRRISAARYGEVGMSLTSEWFAKYLQSSAAACWVYANLTSCQALGNMCVMNMNSYDFATFDACGLFQFIFENTAGLSTVHSISFWRQNLPWLFYGDQLGLAPQVLSSTSLPTNFSFKGENQNTKLKFVAASYDIRGNFLKWQTLEGGVLQLCPDTETRLNAAYSFGTTYQQNCEIPISKILIDFPTPIFYDVYLEYTDENQHQYILAVPVLNLNLQHNKIFVNQDSNSGKWLLTRRIFLVDAVSGRENDLGTQPRVIRVATQISLSVHLVPNTINGNIYPPLITIAYSDIDIKDANSQSVKVSFSVTYEMDHGEAHVQTDIALGVLGGLAVLASLLKTAGWKRRIGSPMIDLQTVVKFLVYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPIQEERFVTYVGCAFALKALQFLHKLISQITIDVFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINSLFQVLTVLFFLEVVGFKNLALMDSSSSLSRNPPSYIAPYSCILRYAVSAALWLAIGIIQVVFFAVFYERFIEDKIRQFVDLCSMSNISVFLLSHKCFGYYIHGRSVHGHADTNMEEMNMNLKREAENLCSQRGLVPNTDGQTFEIAISNQMRQHYDRIHETLIRKNGPARLLSSSASTFEQSIKAYHMMNKFLGSFIDHVHKEMDYFIKDKLLLERILGMEFMEPMEKSIFYNDEGYSFSSVLYYGNEATLLIFDLLFFCVVDLACQNFILASFLTYLQQEIFRYIRNTVGQKNLASKTLVDQRFLI
Protein: Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein (Glycosyltransferase) (F4JIW2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
- Arabinogalactan O-methyltransferase 2
Sequence:
MASSNSEKRWIFPLAMASLMFIFLIAASFNMGLLSSVRSINSLIFSYNLSTTNETRVEFAESKINQSSHPPPVQPSLPRFGYLVSGSRGDLESLWRVLRTLYHPRNQYVVHLDLESPAEERLELAKRVSQDPVFSDVGNVHMITKANLVTYRGPTMVANTLHACAILLKQSKEWDWFINLSASDYPLVTQDDLIDTFSGLDRNLNFIDHSSKLGWKEEKRAKPLIIDPGLYSTKKSDVFWVTPRRTMPTAFKLFTGSAWMVLSRSFVEYCIWGWDNLPRTLLMYYTNFLSTPEGYFHTVICNAPEYSSTVLNHDLHFISWDRPPKQHPRALTINDTERMIASGSAFSRKFRHNDPALDKIDKELLGRGNGNFTPGGWCAGEPKCSRVGDPSKIKPGPGANRLRVLVSRLVLTSKLTQRQCR
Protein: Branched-chain amino acid transport system 3 carrier protein (LIV-III) (P25185)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the LIV-III transport system for branched-chain amino acids. BraZ is specific for isoleucine and valine. The LIV-III transport system may be H(+)-coupled.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Serine/threonine transporter SstT
- Oligopeptide transporter, OPT family
- Probable ATP-binding component of ABC transporter
Sequence:
MNALKGRDILALGFMTFALFVGAGNIIFPPIVGLQSGPHVWLAALGFLITAVGLPVITVIALAKVGGSVDALSHPIGRYAGGLLAAVCYLAVGPLFAIPRTATVSFEVGVVPLLGESGTALFVYSLAYFLLALAISLYPGRLLDTVGRFLAPLKILALAILGVAAFLWPAGPIGTAQPEYTQAAFSQGFVNGYLTMDTLAALVFGIVIVNAIRSRGVQSPRLITRYAIVAGLIAGVGLVLVYVSLFRLGAGSHAIAADASNGAAVLHAYVQHTFGSLGSSFLAGLIALACLVTAVGLTCACAEYFCQRLPLSYRSLVIILAGFSFIVSNLGLTKLIQVSIPVLTAIYPPCIVLVALSFCIGLWHSATRILAPVMLVSLAFGVLDALKAAGLGQDFPQWLLHLPLAEQGLAWLIPSVATLAACSLVDRLLGKPAQVAA
Protein: Prostate transmembrane protein, androgen induced 1 (A2A2F5)
Organism: Homo sapiens (Human)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004391}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004391}.
Interaction partners:
Sequence:
MHRLMGVNSTAAAAAGQPNVSCTCNCKRSLFQSMEISCHGFPVCKSHQHQEWKSLCWSLRSPGGASSITGFGSMKVTNPAMNLPECQWLRIQKAELEFVQIIIIVVVMMVMVVVITCLLSHYKLSARSFISRHSQGRRREDALSSEGCLWPSESTVSGNGIPEPQVYAPPRPTDRLAVPPFAQRERFHRFQPTYPYLQHEIDLPPTISLSDGEEPPPYQGPCTLQLR
Protein: Chemerin-like receptor 1 (Chemokine-like receptor 1) (G-protein coupled receptor DEZ) (P97468)
Organism: Mus musculus (Mouse)
Function: Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobilization, phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3, MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B (By similarity). Positively regulates adipogenesis and adipocyte metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16863918}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Retinoic acid receptor responder protein 2
Sequence:
MEYDAYNDSGIYDDEYSDGFGYFVDLEEASPWEAKVAPVFLVVIYSLVCFLGLLGNGLVIVIATFKMKKTVNTVWFVNLAVADFLFNIFLPMHITYAAMDYHWVFGKAMCKISNFLLSHNMYTSVFLLTVISFDRCISVLLPVWSQNHRSIRLAYMTCSAVWVLAFFLSSPSLVFRDTANIHGKITCFNNFSLAAPESSPHPAHSQVVSTGYSRHVAVTVTRFLCGFLIPVFIITACYLTIVFKLQRNRLAKNKKPFKIIITIIITFFLCWCPYHTLYLLELHHTAVPSSVFSLGLPLATAVAIANSCMNPILYVFMGHDFRKFKVALFSRLANALSEDTGPSSYPSHRSFTKMSSLNEKASVNEKETSTL
Protein: ATP12 chaperone protein (Q388L4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MRKFLRPHTFLAAHWCLSGGPQRLCSSAHDGCGLHVAPKKPKRRISAGIDTSAILESIPRDPGAHAELSTAELERKVEEWSKMEPEELEKLFQQLDKQEKEESRVLEEDSLYQMDISLRESSRAAVRVFWKDVDVRKLDEEHEGWYTVLVDGRKVKAFESRGVLAIPSEAMAYACAREFSEQKDYLNKLLMPLSDMCSGALTVAPQMITPRIDYLMSFYQNDNMYFRSPPIVEEQDRTINPVTEWFSHAFEVSVPRIVGIGHPLIPPRATFKVRDALLAMSMNPYQVVALCVAAQFTSSLILPLAVFNGIVDLPTALSINRAEERHNTRTEGIIEGYHDIRDADVVTKLCAAAVTWKLMKDVPLSKCFEVPRSAFLEEVI
Protein: Zinc finger MIZ-type containing 2 (E7EWM3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSMNPMKPALPPAPHGDGSFAYESVPWQQSATQPAGSLSVVTTVWGVGNATQSQCLGQQAFAEGGANKGYVQQGVYSRGGYPGAPGFTTGYAGGPGGLGLPSHAARPSTDFTQAAAAAAVAAAAATATATATATVAALQEKQSQELSQYGAMGAGQSFNSQFLQHGGPRGPSVPAGMNPTGIGGVMGPSGLSPLAMNPTRAAGMTPLYAGQRLPQHGYPGPPQAQPLPRQGVKRTYSEVYPGQQYLQGGQYAPSTAQFAPSPGQPPAPSPSYPGHRLPLQQGMTQSLSVPGPTGLHYKPTEQFNGQGASFNGGSVSYSQPGLSGPTRSIPGYPSSPLPGNPTPPMTPSSSVPYMSPNQEVKSPFLPDLKPNLNSLHSSPSGSGPCDELRLTFPVRDGVVLEPFRLQHNLAVSNHVFQLRDSVYKTLIMRPDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLYLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSGTIPGTPGPNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMLGILIYIQNSDYEEITIDPTCSWKPVPVKPDMHIKEEPDGPALKRCRTVSPAHVLMPSVMEMIAALGPGAAPFAPLQPPSVPAPSDYPGQGSSFLGPGTFPESFPPTTPSTPTLAEFTPGPPPISYQSDIPSSLLTSEKSTACLPSQMAPAGHLDPTHNPGTPGLHTSNLGAPPGPQLHHSNPPPASRQSLGQASLGPTGELAFSPATGVMGPPSMSGAGEAPEPALDLLPELTNPDELLSYLGPPDLPTNNNDDLLSLFENN
Protein: Actinin alpha 2 (A0A8I5ZN92)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
EAKKEGIQGLLNEGRKDGGGGYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERTEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSILAIQNEVEKVIQSYSIRISSSNPYSTVTMDELRNKWDKVKQLVPVRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEVGGALPESGITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPPYSGPGSVPGALDYTAFSSALYGESDL
Protein: Innexin (O44887)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
- Innexin-12
- Eukaryotic translation initiation factor 4E-binding protein Mextli homolog
Sequence:
MFFLDAFLKGLHKQGDDDSIDRLNYYWTPMLLVIFALTLSAKQYVGQPIQCWIPAQFTGAWEQYSENYCFVQNTYFISPDKYIPDSEIDREGAEIGYYQWVPFILGLQAILFYLPSLFWRLMNFNSGVALKKMLFGAKKADRVDEKARNEAAKSTGAHLYESLTLQSRFAKYTSAFTYGGSYLTYLYLFVKFLYLVQIVFQFIILNNFLGTSYTFWGLGILSDILNGREWEESGHFPRVTMCDFEVRVLGNKHRHTVQCVLMINMFNEKVYVFLWFWLVIVGVATFLNLVNWTRKLMFRSARKAHIKSYLQIEDNFSDDNSRNGQILDKFVDYKLKSDGVFITHLIDNNGGSVFSHDVIVDMWDRFLQDEDNRSQKKQPAEFREI
Protein: Suppressor/enhancer of lin-12 protein 9 (O17528)
Organism: Caenorhabditis elegans
Function: May have a role in the negative regulation of lin-12 and glp-1 transport to the cell surface. May also have a role in a quality control mechanism for endoplasmic reticulum-Golgi transport; the budding of coatomer-coated and other species of coated vesicles, could bind cargo molecules to collect them into budding vesicles. Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction.
Subcellular location: Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Golgi-derived coatomer-coated vesicles.
Interaction partners:
- Transmembrane emp24 domain-containing protein bai
- Transmembrane emp24 domain-containing protein eca
- Transmembrane emp24 domain-containing protein eca
- GOLD domain-containing protein
- ERGIC-53-like protein
- Protein transport protein SEC23
- GOLD domain-containing protein
- Surfeit locus protein 4 homolog
- Small COPII coat GTPase SAR1
- Protein lin-12
Sequence:
MNSLTWILAVLFVTPAASYFIHVDANEEQCFFDRLTSGTKMGLMFEVAEGGFLDIDVKITGPDNKEIYKGERESSGKFTFAAHMDGVYTYCFGNKMSTMTPKAVMFTVEITEPHQQAPGAAANQDAADNAKLEEMVRELSSALMSVKHEQEYMEVRERVHRNINENTNSRVVMWAAFEAFVLVGMTVGQIFYLKRFFEVRTMV
Protein: Pre-B-cell leukemia transcription factor 3 (Homeobox protein PBX3) (O35317)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-A9
- Homeobox protein Meis1
- Homeobox protein Hox-B5
- Homeobox protein Hox-C9
- Homeobox protein Meis2
Sequence:
MDDQSRMLQTLAGVNLAGHSVQGGMALPPPPHGHEGADGDGRKQDIGDILHQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRGAQEEDPPDPQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAASGGSSDNSIEHSDYRAKLTQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVGIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAAKTAVTAAHAVAAAVQNNQTNSPTTPNSGSSGSFNLPNSGDMFMNMQSLNGDSYQGSQVGANVQSQVDTLRHVINQTGGYSDGLGANSLYSPHNLNANGGWQDATTPSSVTSPTEGPGSVHSDTSN