wanglab/gogpt-training-data huggingface dataset:
Protein: Probable alpha/beta-glucosidase agdC (EC 3.2.1.20) (EC 3.2.1.21) (Q5BET9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Glucoamylase
- Glucoamylase
- Alpha-glucosidase
- Hexokinase
- Alpha-glucosidase
- Phosphotransferase
- Phosphotransferase
- Alpha/beta-glucosidase agdC
- Glycosyl hydrolases family 32 superfamily
- Alpha/beta-glucosidase agdC
Sequence:
MLGFLLFLPLVGAAVIGPRANSQICPGYKASHAKHNSHTFTADLTLAGKPCDTYGTDLKDLKLLVEYQTDERLHVMIYDANEQVYQVPESVLPRVGNGNGTEKDSALKFDYVEEPFSFTVSRNGDVLFDTSASNLIFQSQYLNLRTWLPNDPHLYGLGEHTDSLRLETNNYTRTLWNRDSYGVPSHSNLYGAHPVYYDHRGSAGTHGVFLANSNGMDIKINKTLDGKQYLEYNILGGVLDFYFFTGSTPKEASTQYAKVVGLPAMQSYWTFGFHQCKYGYRDVYEVAEVVYNYSQAGIPLETMWTDIDYMELRRVFTLDPERFPLGKMRELVDYLHDHNQHYIVMVDPAVSTSGAVWPGVTVYPDWFHPAIQDYWNGEFNKFFDPETGIDIDGLWIDMNEAANMCTFPCTDPERYSIENDLPPAPPAVRPSNPRPLPGFPDDFQPGSSKRLSKRAHGDKLGLPGRNLLSPPYSIKNAAGALSQNTIQTNIGHAGGYVEYDTHNLYGTMMSSASRIAMQQRRPDVRPLIITRSTLGDNLSTWKLYRASIAQVLAFASMFQIPMVGADVCGFGSNTTEELCARWASLGAFYTFYRNHNEIGNIPQEYYYWESVTESATKAINIRYQLLDYVYTAFHRQSKTGEPFLQPLFYLYPEDKNTFAIDLQFFYGDAILISPVTEKNSTSVNAYFPKDIFYDWYTGAVIQGQGANIILSNINITHIPIHIRGGNIVPIRSSGAMTTTELRKKGFQLIIASGIDGTASGSLYLDDGDSLEQTDTANIEFEYRSGVLYIKGQFIHDVPVKIESVILLGQTTTAGAGRHNQKQVIETNLELTAPTRVKLA
Protein: Catabolite gene activator protein (P74171)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- cAMP protein kinase regulatory chain
- Sll1924 protein
- Slr2127 protein
- Slr1732 protein
- Slr0316 protein
- Sll1268 protein
- Uncharacterized protein sll1247
- Slr0869 protein
Sequence:
MGTSPQNSEFTERLSQEIPFFEGLRLEVLQEAIAHVSVRSHPANQVILLEHDWGGSVYFVMDGWVKIRTHNVDGREVTLNIVGRGEIVGEMAAIEEAPRSTDVITLTPAEVCSVPAPEFYNFLQTEPMAGIRLAQIIARRLRQLNRRLRLREAESLTRVADTLLFLAEGRGRDTDKGVIIPNLPHRELSSISGLARETVTRCLTKLEKRGLIHREPDFISVANLRDLEDLIS
Protein: Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2) (Q80YA9)
Organism: Mus musculus (Mouse)
Function: May function as an adapter protein or regulator of Ras signaling pathways.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MALIMEPVSKWSPSQVVDWMKGLDDCLQQYIKNFEREKISGDQLLRITHQELEDLGVSRIGHQELILEAVDLLCALNYGLETENLKTLSHKLNASAKNLQNFITGRRRSGHYDGRTSRKLPNDFLTSVVDLIGAAKSLLAWLDRSPFAAVTDYSVTRNNVIQLCLELTTIVQQDCTVYETENKILHVCKTLSGVCDHIISLSSDPLVSQSAHLEVIQLANIKPSEGLGMYIKSTYDGLHVITGTTENSPADRCKKIHAGDEVIQVNHQTVVGWQLKNLVNALREDPSGVILTLKKRPQSMLTSAPALLKNMRWKPLALQPLIPRSPTSSVATPSSTISTPTKRDSSALQDLYIPPPPAEPYIPRDEKGNLPCEDLRGHMVGKPVHKGSESPNSFLDQEYRKRFNIVEEDTVLYCYEYEKGRSSSQGRRESTPTYGKLRPISMPVEYNWVGDYEDPNKMKRDSRRENSLLRYMSNEKIAQEEYMFQRNSKKDTGKKSKKKGDKSNSPAHYSLLPSLQMDALRQDIMGTPVPETTLYHTFQQSSLQHKSKKKNKGAISGKSKRRISCKDLGRGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTAGYAERERIKQEQDYWSESDKEEADTPSTPKQDSPPPPYDTYPRPPSMSCASPYVEAKHSRLSSTETSQSQSSHEEFRQEVTGSSAVSPIRKTASQRRSWQDLIETPLTSSGLHYLQTLPLEDSVFSDSAAISPEHRRQSTLPTQKCHLQDHYGPYPLAESERMQVLNGNGGKPRSFTLPRDSGFNHCCLNTPVSACDPQDDIQPPEVEEEEEEEEEEAAGENVGEKNENREEKLGDSLQDLYRALEEASLSPLGEHRISTKMEYKLSFIKRCNDPVMNEKLHRLRILKSTLKAREGEVAIIDKVLDNPDLTSKEFQQWKQMYLDLFLDICQSTTSNDPLSISSEVDVLTSSLTHTHSYIETHV
Protein: Lens fiber major intrinsic protein (A0A0K0LTP0)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MWEFRSMTFWRAVFAEFFGTMFFVFFGMGAALRWTTGPNHILHVALCFGLAAATMIQSIGHISGGHINPAVTFAYLVGSQMSLFRAFFYWAAQILGAMAGAAVLYGVTPNNMRGNMALNTLQPGISLGMGTTVEVFLTMQLVICIFAVTDERRNGRMGSAALSIGFAVTIGHLMGMYYTGAGMNPARSFAPAVLFRNFVNHWVYWVGPMIGGAMGALLYDFTLFPRMRGLSERLATLKGSRPPETETQQDNRGEPIELKTQAL
Protein: HLA class I histocompatibility antigen A alpha chain (MHC class I antigen) (Major histocompatibility complex, class I, A) (Q5SUL5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLEGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSLTACKV
Protein: CCR4-NOT transcription complex subunit 9 (Cell differentiation protein RQCD1 homolog) (Q7JVP2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.
Interaction partners:
- poly
- CCR4-NOT transcription complex subunit 3
- poly
- CCR4-NOT transcription complex subunit 10
- Not1, isoform H
- CCR4-NOT transcription complex subunit 4
- Regulator of gene activity
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 9
- FI22161p1
Sequence:
MSAQPSPHMNPQQQQQQQQQQQQTEQEKVYQWINELAHPDTRETALLELSKKRETDLAPMLWNSFGTACALLQEIVNIYPSITPPTLTAHQSNRVCNALALLQCVASHPETRTAFLQAQIPLYLYPFLSTTSKTRPFEYLRLTSLGVIGALVKTDEQEVITFLLTTEIVPLCLSIMDSGSELSKTVATFIIQKILLDESGLSYICQTYERFSHVAITLGKMVIQLAKDPCARLLKHVVRCYLRLSDNTRARKALGQCLPDQLRDGTFALCLQEDKSTKQWLQMLLKNLELGATPQQIGMSPLGS
Protein: Pro-apoptotic serine protease NMA111 (EC 3.4.21.-) (111 kDa nuclear mediator of apoptosis) (P53920)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor BIR1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14657274}.
Interaction partners:
- Metacaspase-1
- Bax inhibitor 1
- Mitochondrial nuclease
- Chromosomal passenger complex protein BIR1
- Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
- Pheromone-processing carboxypeptidase KEX1
- Apoptosis-inducing factor 1
- Cytochrome c isoform 2
- Deoxyribonuclease Tat-D
- Cytochrome c isoform 1
Sequence:
MTISLSNIKKRDHSKISDGTSGESSLVKRKQLESATGDQEEEYTDHEIIIEPLHFANNNNTVLTDSENYLRWQNTISNVVKSVVSIHFSQVAPFDCDSALVSEATGFVVDAKLGIILTNRHVVGPGPFVGYVVFDNHEECDVIPIYRDPVHDFGFLKFDPKNIKYSKIKALTLKPSLAKVGSEIRVVGNDAGEKLSILAGFISRIDRNAPEYGELTYNDFNTEYIQAAASASGGSSGSPVVNIDGYAVALQAGGSTEASTDFFLPLDRILRALICIQTNKPITRGTIQVQWLLKPYDECRRLGLTSERESEARAKFPENIGLLVAETVLREGPGYDKIKEGDTLISINGETISSFMQVDKIQDENVGKEIQLVIQRGGVECTVTCTVGDLHAITPHRYVEVCGATFHELSYQMARFYALPVRGVFLSSASGSFNFDSKERVGWIVDSIDNKETPDLDTFIEIMKTIPDRKRVTVRYHHLTDQHSPLVTSIYIDRHWCNEFRVYTRNDTTGIWDYKNVADPLPADALKPRSAKIIPIPVNNEKVAKLSSSLCTVATMAAVPLDSLSADILKTSGLIIDAEKGYVLVSRRVVPHDCLDTFVTIADSLVVPATVEFLHPTHNFAIVKYDPELVKAPLITPKLSTTRMKRGDKLQFIGFTQNDRIVTSETTVTDISSVSIPSNLIPRYRATNLEAISIDCNVSTRCNSGILTDNDGTVRGLWLPFLGERLENKEKVYLMGLDIMDCREVIDILKNGGKPRVSIVDAGFGSISVLQARIRGVPEEWIMRMEHESNNRLQFITVSRVSYTEDKIHLETGDVILSVNGKLVTEMNDLNGVVSSADGILPSAMLDFKVVRDGNIVDLKIKTVEVQETDRFVIFAGSILQKPHHAVLQAMVDVPKGVYCTFRGESSPALQYGISATNFITHVNEIETPDLDTFLKVVKTIPDNSYCKMRLMTFDNVPFAISLKTNYHYFPTAELKRDNITHKWIEKEFTGNSQSEK
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (E7ETB3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARSLSIMFVPNSWLNGYHKVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD
Protein: Ras-related protein Rab-9A (EC 3.6.5.2) (Q99P75)
Organism: Rattus norvegicus (Rat)
Function: Involved in the transport of proteins between the endosomes and the trans-Golgi network. Involved in the recruitment of SGSM2 to melanosomes and is required for the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51151}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51151}. Late endosome {ECO:0000269|PubMed:12051767}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9R0M6}. Melanosome {ECO:0000250|UniProtKB:Q9R0M6}. Note=Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis. Mainly localizes to late endosomes and partially localizes to Golgi. Colocalizes with NDE1 to membrane vesicles (By similarity). {ECO:0000250|UniProtKB:P51151}.
Interaction partners:
- Small G protein signaling modulator 1
- GRIP and coiled-coil domain-containing protein 2
- small monomeric GTPase
- Pleckstrin homology domain-containing family M member 2
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
Sequence:
MAGKSSLFKIILLGDGGVGKSSLMNRYVTNKFDSQLFHTIGVEFLNKDLEVDGHFVTMQIWDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFVILGNKTDIKERQVSTEEAQAWCKDNGDYPYFETSAKDSTNVAAAFEEAVRRILATEDRSDHLIQTDTVNLHRKPKPNSSCC
Protein: Scm polycomb group protein like 2 (A0A571BGE2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XNGEPKEKRSLKRLSLHPHRSAPVSSKVPRKSGQASKASSYITVPDPSVLKQGFCKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHEIDGKALLLLKSELLMKYMGLKLGPAVKLCYYIEKLKEINHN
Protein: GATA-type domain-containing protein (H9G2S7)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHYRDANYSISRNKVNLHHEEFMLDGVVGGEDHDMQNTNEVRAELDSLLRLDPDTNSIIDALHISQPIEQENMDYEGKPVEFTLGTSSGGASLAPTSSTTAASIAPFSYNTSATNYYNTTPSSYPMFLNYQYAGGTTVTTDMDAFSGMDMSMNNGVFGTQNNPSYFYPTTQLNTYGYDTLAAATTASGITVNNNQLNVNIVQGNGTIVPQPITQNIISTVSNVQSSVPINNSQPLTPTGLAGCSTSSGSSSASSSSANSTSTPKNTISKANRSSGGANNSQFSTEDRECVNCGVHNTPLWRRDGSGNYLCNACGLYFKMNHHARPLVKPKKRQNAQKRTGIECVNCRTNTTTLWRRNGEGHPVCNACGLYFKLHKVERPITMKKDGIQTRNRKLSAKGSRRMKKENGGTPTSMGMPTTSSSISSGIELDQSGVWGMKNTQPMLMTPTAYAFPASNFYFNSIEDQLEYKTCPPMMVDFGGQMKNLNLN
Protein: H-2 class II histocompatibility antigen, A-Q alpha chain (P04227)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
GIVVYQSPGDIGQYTHEFDGDEWFYVDLDKKETVWMLPEFGQLTSFDPQGGLQNIATGKHNLGGWTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLDEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRPPGPL
Protein: Ceramide kinase (OsCERK) (EC 2.7.1.138) (C0LT23)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Possesses activity on ceramide analog (C6 synthetic ceramide) in vitro. Ceramide is a critical sphingolipid metabolite that induces programmed cell death (PCD) in plants and ceramide-1-phosphate has a PCD suppressive effect. Thus, ceramide phosphorylation plays a role in the modulation of PCD and CERK activity is crucial for the maintenance of cell viability.
Interaction partners:
- Neutral ceramidase
- Non-lysosomal glucosylceramidase
- Non-lysosomal glucosylceramidase
- Sphingolipid delta
- Os07g0444000 protein
- Alkaline phytoceramidase family protein, expressed
- Non-lysosomal glucosylceramidase
- Os01g0906000 protein
- Phosphatidylinositol:ceramide inositolphosphotransferase
- ASC1-like protein 3
Sequence:
MEGGGEALFLDGVGEVTVAVGDDGLSFQPLHQEVSSSCWSSIIMQPKLESKLKFSDVYAVELLEVGPVCEPWNARATVQGKINTEMNRFVIHTVTRPRKRPSPWVPCEYIFGHKDQQTCKTWVEHIKTCINKEQDRPKSLMVFVHPLCGKGRGCKNWETVAPLFERAKVKTKVIVTQRAGHAYDTLASLSDKDLKKFDGVIAVGGDGLFNEILNGLLSTRHTNSYPPTPEGFGYFRNNMKCQEHRNNDLSNSELTGDDANAISGSSNTPDDHEPLLSTTRSTGLDISSSDSSDEPCNGDQVPLVSFPNNWFRLGIIPSGSTDAIVLSTTGERDPVTSALLIILGRRISLDIAQVVRWKSSPSAEVSPTVRYAASFAGYGFYGEVIRESEKYRWMGPARYDFSGTMVFLKHRSYEAKVAFLENGNTHSLTASAENNANGVQTLQYHQNRHRKTICRTNCLICKGTSTSEQNSEDENPDSSRTACETPKWVWSKGRFLSVGAAVISCRNERAPDGLVADAHLSDGFLHLLLIRDCPLPFYLWHLTQFTKKGSDPLSFKFVEHHKTQAFTFISSHDESVWNLDGELLQACEVSVQAFRGLVNLFASGPEV
Protein: TM2 domain-containing protein almondex (TM2D3) (Beta-amyloid peptide binding-like protein amx) (dBBP-like protein) (dBLP) (Q9U4H5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the control of cell fates in the neurectoderm. Acts as a positive regulator of Notch pathway and is required at different levels during development.
Subcellular location: Membrane {ECO:0000269|PubMed:34905536}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000269|PubMed:34905536}.
Interaction partners:
Sequence:
MRLQRQCIVVNMRSAIVLIMIFVLTGIRNSETASGGNQMDLSDSKGDHKDNSNASNGNGNANDNEVYVPPLVSSMVAKSGGGAGGLLDNITAYSSSSSSSSSNGNNNMLCPYDKETPCDRLQFPCIRCNYNHGCIYGRDLNVTCEVINNVQCLGERSFQRQMNCRYCYQTEMWQQSCGQRSSCNSATDKLFRTNCTVHHDVLCLGNRSFTRNLRCNWTQGYRWSTALLISLTLGGFGADRFYLGHWQEGIGKLFSFGGLGVWTIIDVLLISMHYLGPADGSLYI
Protein: Tartrate-resistant acid phosphatase type 5 (TR-AP) (EC 3.1.3.2) (Tartrate-resistant acid ATPase) (TrATPase) (Type 5 acid phosphatase) (P13686)
Organism: Homo sapiens (Human)
Function: Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias.
Subcellular location: Lysosome.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 11
- Nuclear factor of activated T-cells, cytoplasmic 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Cathepsin K
- Riboflavin kinase
- Flavin reductase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- FAD synthase
- Osteocalcin
- Dendritic cell-specific transmembrane protein
Sequence:
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASGKSLFKTRLPRRARP
Protein: TRAP dicarboxylate family transporter, DctP subunit (Q5LKP6)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
Sequence:
MRRYISQLIATAVFGAALAGSAAAQEYSFRFQSSDPAGNANFILQKSWAEDVRERTGGKVAIELLPVNTIVAHTETQDAVAAGIIDGHFTDTSYFAGKEPAFGLIANPVGAWSDPQQMFDFMENGGGKELMNSLVEPYGLHFIGATTPGLEAFVSKVPLDGVDDLKGIKMRAPEGMVQRVFAAAGAVPVNLPGSEVFTSLDKGVIDAADYTVFSTNHEQGMHDIAKHPVYPGFHSMPLVEVSMNKTTWESLPADIQATLEQSVSDFARRQVSTLAERDAVAVAAAAADGVTVHDWSAEERARFRAIAKGEWEAAAGASDASARVYSTLTKYLSDNGLLE
Protein: Ribosomal RNA processing protein 4 (EC 3.1.13.-) (Q57X83)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATP-dependent DEAD/H RNA helicase, putative
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Exosome complex exonuclease RRP40
- Ribosomal RNA processing protein 45
- Exosome component CSL4
- Ribosomal RNA-processing protein 43
- Elongation factor 1-alpha, putative
- Ribosomal RNA processing protein 6
- Exosome-associated protein 4
- Exosome complex exonuclease RRP41A
Sequence:
MHHCRTPLFYYRFLYCLFTLFVVMSVPTCITGDTICGSAGPSKLDYVEDHVFLRGYNTYEGNNPNGAAAAQEGGGEIIASINGMVEVTDRVVSVKGMSSRYVAEVGDIVVGRVKEVCGNRWRVDVGAFQDAVMPLANVTEPGGILRRRGRSDELTMRNIFDEGELVVAEVQRVSQDGLISLHTRSGEKYGKLSDFGLLVLISPALVKRVKHHFMCLEFIHVNLVLGTNGAIWVSPATATTATESAKSAYDRFDADIRRAVTRVANCIRVMGNARFPVFDKSIEAAVKASIDFVLGPFEILYPGNQNLITTTVLDTINTRKRTIY
Protein: Bifunctional pinoresinol-lariciresinol reductase 1 (PLR-Lu1) ((-)-lariciresinol reductase) (EC 1.23.1.4) ((-)-pinoresinol reductase) (EC 1.23.1.3) (Q4R0H9)
Organism: Linum usitatissimum (Flax) (Linum humile)
Function: Reductase involved in lignan biosynthesis. Catalyzes the enantioselective conversion of (-)-pinoresinol into (-)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
Interaction partners:
Sequence:
MGRCRVLVVGGTGYIGKRIVKASIEHGHDTYVLKRPETGLDIEKFQLLLSFKKQGAHLVEASFSDHESLVRAVKLVDVVICTVSGAHSRSLLLQLKLVEAIKEAGNVKRFIPSEFGMDPARMGDALEPGRETFDLKMVVRKAIEDANIPHTYISANCFGGYFVGNLSQLGPLTPPSDKVTIYGDGNVKVVYMDEDDVATYTIMTIEDDRTLNKTMYLRPPENVITHRQLVETWEKLSGNQLQKTELSSQDFLALMEGKDVAEQVVIGHLYHIYYEGCLTNFDIDAAQDQVEASSLYPEVEYIRMKDYLMIYL
Protein: SD13780p (Q8MRY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGFFGPAKIEKNIFGNSNGPIWLDQVMCFGNETSIDQCNHWNWGEHNCNHTEDVALHCSAGPPPRSQRYSQTQIKGGRSLGRETTPKTYSQIGLWERSSKAVHTPRRCGIFKDDLTDEYAHREERVVRGNVAQRGRHPWQATIRTRGRGGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENWYLHENFRKGTHMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADHVCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKINESLLRF
Protein: Polyketide synthase (O53579)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MADVAESQENAPAERAELTVPEMRQWLRNWVGKAVGKAPDSIDESVPMVELGLSSRDAVAMAADIEDLTGVTLSVAVAFAHPTIESLATRIIEGEPETDLAGDDAEDWSRTGPAERVDIAIVGLSTRFPGEMNTPEQTWQALLEGRDGITDLPDGRWSEFLEEPRLAARVAGARTRGGYLKDIKGFDSEFFAVAKTEADNIDPQQRMALELTWEALEHARIPASSLRGQAVGVYIGSSTNDYSFLAVSDPTVAHPYAITGTSSSIIANRVSYFYDFHGPSVTIDTACSSSLVAIHQGVQALRNGEADVVVAGGVNALITPMVTLGFDEIGAVLAPDGRIKSFSADADGYTRSEGGGMLVLKRVDDARRDGDAILAVIAGSAVNHDGRSNGLIAPNQDAQADVLRRAYKDAGIDPRTVDYIEAHGTGTILGDPIEAEALGRVVGRGRPADRPALLGAVKTNVGHLESAAGAASMAKVVLALQHDKLPPSINFAGPSPYIDFDAMRLKMITTPTDWPRYGGYALAGVSSFGFGGANAHVVVREVLPRDVVEKEPEPEPEPKAAAEPAEAPTLAGHALRFDEFGNIITDSAVAEEPEPELPGVTEEALRLKEAALEELAAQEVTAPLVPLAVSAFLTSRKKAAAAELADWMQSPEGQASSLESIGRSLSRRNHGRSRAVVLAHDHDEAIKGLRAVAAGKQAPNVFSVDGPVTTGPVWVLAGFGAQHRKMGKSLYLRNEVFAAWIEKVDALVQDELGYSVLELILDDAQDYGIETTQVTIFAIQIALGELLRHHGAKPAAVIGQSLGEAASAYFAGGLSLRDATRAICSRSHLMGEGEAMLFGEYIRLMALVEYSADEIREVFSDFPDLEVCVYAAPTQTVIGGPPEQVDAILARAEAEGKFARKFATKGASHTSQMDPLLGELTAELQGIKPTSPTCGIFSTVHEGRYIKPGGEPIHDVEYWKKGLRHSVYFTHGIRNAVDSGHTTFLELAPNPVALMQVALTTADAGLHDAQLIPTLARKQDEVSSMVSTMAQLYVYGHDLDIRTLFSRASGPQDYANIPPTRFKRKEHWLPAHFSGDGSTYMPGTHVALPDGRHVWEYAPRDGNVDLAALVRAAAAHVLPDAQLTAAEQRAVPGDGARLVTTMTRHPGGASVQVHARIDESFTLVYDALVSRAGSESVLPTAVGAATAIAVADGAPVAPETPAEDADAETLSDSLTTRYMPSGMTRWSPDSGETIAERLGLIVGSAMGYEPEDLPWEVPLIELGLDSLMAVRIKNRVEYDFDLPPIQLTAVRDANLYNVEKLIEYAVEHRDEVQQLHEHQKTQTAEEIARAQAELLHGKVGKTEPVDSEAGVALPSPQNGEQPNPTGPALNVDVPPRDAAERVTFATWAIVTGKSPGGIFNELPRLDDEAAAKIAQRLSERAEGPITAEDVLTSSNIEALADKVRTYLEAGQIDGFVRTLRARPEAGGKVPVFVFHPAGGSTVVYEPLLGRLPADTPMYGFERVEGSIEERAQQYVPKLIEMQGDGPYVLVGWSLGGVLAYACAIGLRRLGKDVRFVGLIDAVRAGEEIPQTKEEIRKRWDRYAAFAEKTFNVTIPAIPYEQLEELDDEGQVRFVLDAVSQSGVQIPAGIIEHQRTSYLDNRAIDTAQIQPYDGHVTLYMADRYHDDAIMFEPRYAVRQPDGGWGEYVSDLEVVPIGGEHIQAIDEPIIAKVGEHMSRALGQIEADRTSEVGKQ
Protein: Transmembrane protein 158 (40 kDa BINP-binding protein) (p40BBP) (Brain-specific binding protein) (Ras-induced senescence protein 1) (Q91XV7)
Organism: Rattus norvegicus (Rat)
Function: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLPLLAALLAAACPLPPARGGATDAPGLSGTPPNASANASFTGEHSTPRLLASAASAPPERAGPEEAPAAPCNISVQRQMLSSLLVRWGRPRGLQCDLLLFSTNAHGRAFFAAAFHRVGPPLLIEHLGLAAGGAQQDLRLCVGCGWVRGRLRAPAGAPTALPAYPAAEPGPLWLQGEPRHFCCLDFSLEELQGEPGWRLNRKPIESTLVACFMTLVIVVWSVAALIWPVPIIAGFLPNGMEQRRTTAGAPAAAPAAVPAGTTAAAAAAAAAAAAAAAVTSGVAPK
Protein: Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (EC 1.13.11.58) (Linoleate 9S-lipoxygenase) (Linoleate 9S-LOX) (Manganese 9S-lipoxygenase) (9S-MnLOX) (P0CT92)
Organism: Nakataea oryzae (Rice stem rot fungus) (Magnaporthe salvinii)
Function: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate products 11S-HPODE and 13R-HPODE from linoleic acid are then transformed into 9S-HPODE as the final product. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S-HPOTrE is further oxidized by the enzyme to 9,16-DiHOTrE as the end product. Also acts on gamma-linolenic acid producing 9-HOTrE(n-6) as the main metabolite.
Subcellular location: Secreted {ECO:0000269|PubMed:23233731}.
Interaction partners:
Sequence:
MRIGLLAFAVAARYVEALPVASGEEVASSSAPTTLPSTSSSSALPSPTKYTLPHEDPNPEARKAEIALKRGGFLYGPSTLGQTTFYPSGTLGTAMSQRDQALWLRDAENQTITAYREANETLRDIQSHGGLKTLDDFALLYDGHWKASVPEGIEKGMLSNYTSDLLFSMERLSNNPYSLKRLHPTKDKLPFSVEDKVVKQLTATTLAALHKAGRLFFVDHSDQKKYTPQAGRYAAACQGLFYVDARSNQFLPLAIKTNVGADLTYTPLDDKNDWLLAKIMFNNNDLFYSQMYHVLFHTVPEIVHMAAIRTLSESHPVLAVLNRIMYQAYAIRPVGERILFNPGGFWDQNLGLPATAAVDFLSSIYAHGEGGFRAGYVENNLRKRGLVGDTFGGPALPHFPFYEDAQRVLGAIRGFMQAFVDSTYGGDDGALARDFELQDWVAEANGPAQVRDFPTAPLRRREELVGILTHIAWNTGGAHHVLNQGAPVRASGVLPLHPAALYAPVPAAKGAVASSDGLLAWLPDEVKSVEQVSLLARFNRAQVRDRNQTVRNMFAAPELLAGNGEAYAAANARFVEETGRISREIEGRGFDSKGLSQGMPFIWTALNPAVNPFFLSI
Protein: Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Fatty acid ester hydrolase) (EC 3.1.1.-) (Oleamide hydrolase 1) (O00519)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Subcellular location: Endomembrane system {ECO:0000269|PubMed:17015445}; Single-pass membrane protein {ECO:0000269|PubMed:17015445}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17015445}. Note=Seems to be attached to intracellular membranes and a portion of the cytoskeletal network.
Interaction partners:
- Glutamyl-tRNA
- Monoglyceride lipase
- Cannabinoid receptor 1
- Bifunctional glutamate/proline--tRNA ligase
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Aspartate--tRNA ligase, mitochondrial
- Diacylglycerol lipase-alpha
- Fatty acid-binding protein 5
- Cannabinoid receptor 2
- Monoacylglycerol lipase ABHD6
Sequence:
MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS