wanglab/gogpt-training-data huggingface dataset:
Protein: Kelch domain-containing protein 2 (Hepatocellular carcinoma-associated antigen 33) (Host cell factor homolog LCP) (Host cell factor-like protein 1) (HCLP-1) (Q9Y2U9)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC2) complex specifically recognizes proteins with a diglycine (Gly-Gly) at the C-terminus, leading to their ubiquitination and degradation. The CRL2(KLHDC2) complex mediates ubiquitination and degradation of truncated SELENOK and SELENOS selenoproteins produced by failed UGA/Sec decoding, which end with a diglycine. The CRL2(KLHDC2) complex also recognizes proteolytically cleaved proteins ending with Gly-Gly, such as the N-terminal fragment of USP1, leading to their degradation. May also act as an indirect repressor of CREB3-mediated transcription by interfering with CREB3-DNA-binding.
Subcellular location: Nucleus {ECO:0000269|PubMed:11384994, ECO:0000269|PubMed:16964437}.
Interaction partners:
- Elongin-B
- Cullin-2
- Amyloid protein-binding protein 2
- E3 ubiquitin-protein ligase RBX1
- Protein fem-1 homolog C
- PRAME family member 6
- Protein zyg-11 homolog B
- Protein zer-1 homolog
- Kelch domain-containing protein 3
- demerged
Sequence:
MADGNEDLRADDLPGPAFESYESMELACPAERSGHVAVSDGRHMFVWGGYKSNQVRGLYDFYLPREELWIYNMETGRWKKINTEGDVPPSMSGSCAVCVDRVLYLFGGHHSRGNTNKFYMLDSRSTDRVLQWERIDCQGIPPSSKDKLGVWVYKNKLIFFGGYGYLPEDKVLGTFEFDETSFWNSSHPRGWNDHVHILDTETFTWSQPITTGKAPSPRAAHACATVGNRGFVFGGRYRDARMNDLHYLNLDTWEWNELIPQGICPVGRSWHSLTPVSSDHLFLFGGFTTDKQPLSDAWTYCISKNEWIQFNHPYTEKPRLWHTACASDEGEVIVFGGCANNLLVHHRAAHSNEILIFSVQPKSLVRLSLEAVICFKEMLANSWNCLPKHLLHSVNQRFGSNNTSGS
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (AtPARN) (Protein ABA hypersensitive germination 2) (Q9LG26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. Essential for early development, possibly by participating in silencing certain maternal mRNAs translationally. May have a pivotal role in stress response.
Subcellular location: Nucleus {ECO:0000269|PubMed:15019988}. Cytoplasm {ECO:0000269|PubMed:15019988, ECO:0000269|PubMed:15247430}. Note=Only cytoplasmic. {ECO:0000269|PubMed:15247430}.
Interaction partners:
- Poly
- Uncharacterized CRM domain-containing protein At3g25440
- mRNA-decapping enzyme subunit 2
- Exosome complex component RRP4 homolog
- Inactive exonuclease DIS3L2
- Nuclear poly
- Nuclear poly
- Exosome complex exonuclease RRP46 homolog
- Nuclear poly
- Exosome complex component RRP41 homolog
Sequence:
MRRHKRWPLRSLVCSFSSSAAETVTTSTAASATAAFPLKHVTRSNFETTLNDLRSLVKAADFVAIDLEMTGVTSAPWRDSLEFDRYDVRYLKVKDSAEKFAVVQFGVCPFRWDSRTQSFVSYPHNFFVFPRQELTFDPPAHEFLCQTTSMDFLAKYQFDFNTCIHEGISYLSRREEEEASKRLKMLHGEDGIDSSGETEELKLVRLADVLFAARMEKLLNEWRSGLLHGGNASSEFPRISNGSNQSMETVFHHMRPALSLKGFTSHQLRVLNSVLRKHFGDLVYIHSNDKSSSSRDIVVYTDSDSDKENLMKEAKDERKRLAERKIQSAIGFRQVIDLLASEKKLIVGHNCFLDIAHVYSKFVGPLPSTAEKFVASINSHFPYIVDTKILLNVNPMLHQRMKKSSTSLSSAFSSLCPQIEFSSRSSDSFLQQRVNIDVEIDNVRCSNWNAGGKHEAGYDAFMTGCIFAQACNHLGFDFKQHSQLDDFAQNEKLEKYINRLYLSWTRGDIIDLRTGHSNADNWRVSKFKYENIVLIWNFPRKLKARGIKECICKAFGSASVTSVYHVDDSAVFVLFKNSELVWDFLALKRQLESSDGPVSVLHPLSKILEGGNTGAADYEAYKEICSSHVSEVMFSDQAETVGVKSRTRPNAQCETETREENTVTVTHKASDLIDAFLANRVEVETATSN
Protein: 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABALDH) (EC 1.2.1.47) (Aldehyde dehydrogenase E3 isozyme) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) (Formaldehyde dehydrogenase) (EC 1.2.1.46) (Gamma-aminobutyraldehyde dehydrogenase) (EC 1.2.1.19) (R-aminobutyraldehyde dehydrogenase) [Cleaved into: 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed] (P49189)
Organism: Homo sapiens (Human)
Function: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JLJ3}. Cytoplasm {ECO:0000269|PubMed:1799975}.
Interaction partners:
- Gamma-butyrobetaine dioxygenase
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Aldo-keto reductase family 1 member A1
- Peroxisomal bifunctional enzyme
- 4-aminobutyrate aminotransferase, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Amine oxidase [flavin-containing] B
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Amine oxidase [flavin-containing] A
Sequence:
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF
Protein: Histidine ammonia-lyase (Histidase) (EC 4.3.1.3) (P42357)
Organism: Homo sapiens (Human)
Interaction partners:
- Urocanate hydratase
- Probable imidazolonepropionase
- Histidine decarboxylase
- Cytosolic non-specific dipeptidase
- Beta-Ala-His dipeptidase
- Carnosine synthase 1
- Arginase-1
- Formimidoyltransferase-cyclodeaminase
- Guanine deaminase
- Arginase-2, mitochondrial
Sequence:
MPRYTVHVRGEWLAVPCQDAQLTVGWLGREAVRRYIKNKPDNGGFTSVDDAHFLVRRCKGLGLLDNEDRLEVALENNEFVEVVIEGDAMSPDFIPSQPEGVYLYSKYREPEKYIELDGDRLTTEDLVNLGKGRYKIKLTPTAEKRVQKSREVIDSIIKEKTVVYGITTGFGKFARTVIPINKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEMFNASCLPYVPEKGTVGASGDLAPLSHLALGLVGEGKMWSPKSGWADAKYVLEAHGLKPVILKPKEGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHALRPHRGQIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKNIITTELNSATDNPMVFANRGETVSGGNFHGEYPAKALDYLAIGIHELAAISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSENKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL
Protein: Peroxisomal membrane protein PEX18 (Peroxin-18) (P38855)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in peroxisome biogenesis and the import of peroxisomal matrix proteins that contain the peroxisomal targeting sequence PTS2. Required for peroxisomal targeting of PEX7 and growth on oleate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9864360}. Peroxisome membrane {ECO:0000269|PubMed:9864360}; Peripheral membrane protein {ECO:0000269|PubMed:9864360}; Cytoplasmic side {ECO:0000269|PubMed:9864360}.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Peroxisomal protein PEX21
- 3-ketoacyl-CoA thiolase, peroxisomal
- Proteasome subunit beta type-6
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein PEX17
- Peroxisomal ATPase PEX6
- Peroxisome assembly protein 12
Sequence:
MNSNRCQTNEVNKFISSTEKGPFTGRDNTLSFNKIGSRLNSPPILKDKIELKFLQHSEDLNQSRSYVNIRPRTLEDQSYKFEAPNLNDNETSWAKDFRYNFPKNVEPPIENQIANLNINNGLRTSQTDFPLGFYSQKNFNIASFPVVDHQIFKTTGLEHPINSHIDSLINAEFSELEASSLEEDVHTEEENSGTSLEDEETAMKGLASDIIEFCDNNSANKDVKERLNSSKFMGLMGSISDGSIVLKKDNGTERNLQKHVGFCFQNSGNWAGLEFHDVEDRIA
Protein: Slr2048 protein (P73091)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- TPR repeat-containing protein slr0751
- Sll1628 protein
- Sll0837 protein
- Sll1882 protein
- Mitochondrial outer membrane 72K protein
- Sll0910 protein
- Slr1956 protein
- Sll0886 protein
- Sll1390 protein
Sequence:
MPSRPLGRSFTTSFSMNLRYLWSGKQILIGGGLIPLLFGAAVSAQSPSQTNPSNLPDVTPLLAQRSATDDRRQFNELLRQGKAYVDNGNFPQAIAIYQQAAMLDGENAELFGSMGYLYARQGQFAEASRSFQQALRVNPNNPDYYDGLGFSYARQGLLNEAASAYATAISLGPSSRESVKYRLALGIIMLQQGDYNRVRQLYNEIHSLQSDNEEAAVMMGAALLQSSEYEQLITFNNQALRLFPNRSELTLQLGKAYLAQGDLVAARRALEPRLNPDWRSFSLYLTWAELLEREGNFAGALDAYKQALRNEPTAIAAKIGTGRMYLELDNPAEAVWVFRDLTRLQPSNADFYYLLGEAYAVDEKIDLAKKSFGEAKKLYQAQGNTAGSDRTQEKLDNL
Protein: Exocyst complex component 8 (Exocyst complex 84 kDa subunit) (Q6PGF7)
Organism: Mus musculus (Mouse)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
Interaction partners:
- Exocyst complex component 7
- Exocyst complex component 5
- Exocyst complex component 3
- Exocyst complex component 1
- Exocyst complex component 4
- Exocyst complex component 2
- Exocyst complex component 6
- Ras-related protein Ral-A
- Ras-related protein Ral-B
- Exocyst complex component 6B
Sequence:
MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASAGEDTAGAGPRERGAVQAGFLPGPAGVPREGSGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAAPRAPPPVTSKGSNPFEDEDDEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
Protein: Drosophila melanogaster dynein-related heavy chain polypeptide protein (V9GZG7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
CYRTLFAALNLHLGGAPEGPAGTGKTETTKDLAKAVAKQCVVFNCSDGLDYLALGKFFKGLASCGAWSCFDEFNRIDLEVLSVVAQQILTIQRGINSGSPTLVFEGTTLTLDPTCA
Protein: Pentatricopeptide repeat-containing protein At3g09650, chloroplastic (Protein HIGH CHLOROPHYLL FLUORESCENCE 152) (Q9SF38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the processing of polycistronic chloroplast psbB-psbT-psbH-petB-petD transcript. Could bind RNA.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12782738}.
Interaction partners:
- Cytochrome b6
- Photosystem II reaction center protein H
- Protein high chlorophyll fluorescent 107
- Cytochrome b6-f complex subunit 4
- Photosystem II CP47 reaction center protein
- ATP synthase subunit a, chloroplastic
- Small RNA 2'-O-methyltransferase
- ATP synthase subunit c, chloroplastic
- Auxin transport protein BIG
- Photosystem I reaction center subunit IX
Sequence:
MNILRPPTSSSSSSFPPYPKPVSLTPPVSFTLIHNPINLCSINPPFTNAGRPIFQRSASGTANSSAEDLSSFLGSPSEAYSTHNDQELLFLLRNRKTDEAWAKYVQSTHLPGPTCLSRLVSQLSYQSKPESLTRAQSILTRLRNERQLHRLDANSLGLLAMAAAKSGQTLYAVSVIKSMIRSGYLPHVKAWTAAVASLSASGDDGPEESIKLFIAITRRVKRFGDQSLVGQSRPDTAAFNAVLNACANLGDTDKYWKLFEEMSEWDCEPDVLTYNVMIKLCARVGRKELIVFVLERIIDKGIKVCMTTMHSLVAAYVGFGDLRTAERIVQAMREKRRDLCKVLRECNAEDLKEKEEEEAEDDEDAFEDDEDSGYSARDEVSEEGVVDVFKKLLPNSVDPSGEPPLLPKVFAPDSRIYTTLMKGYMKNGRVADTARMLEAMRRQDDRNSHPDEVTYTTVVSAFVNAGLMDRARQVLAEMARMGVPANRITYNVLLKGYCKQLQIDRAEDLLREMTEDAGIEPDVVSYNIIIDGCILIDDSAGALAFFNEMRTRGIAPTKISYTTLMKAFAMSGQPKLANRVFDEMMNDPRVKVDLIAWNMLVEGYCRLGLIEDAQRVVSRMKENGFYPNVATYGSLANGVSQARKPGDALLLWKEIKERCAVKKKEAPSDSSSDPAPPMLKPDEGLLDTLADICVRAAFFKKALEIIACMEENGIPPNKTKYKKIYVEMHSRMFTSKHASQARIDRRVERKRAAEAFKFWLGLPNSYYGSEWKLGPRED
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FM24)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MFEVAVGSALRRALESAVEAAVAAGDGDAKVRLLELIERGSVPCGELAELCRAWGSEVSVSEALSGLEFKFKDRETRKPSPEFQAQLARLRALQQEQEYQQIVKNRDLAITTESEATPAQINREIKEQVTTVFNIIISVISVVVAIWYWSRTSAGLAIHHRIFLCMFFGILVLVAEVVVYSSYLSKIEEAKASEKSKKEHKKLVQKYVF
Protein: Thioredoxin-like 1-3, chloroplastic (Atypical cysteine/histidine-rich thioredoxin 3) (AtACHT3) (Lilium-type thioredoxin 1-3) (O22779)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19109414}.
Interaction partners:
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 2
- HVA22-like protein j
- Probable acyl-activating enzyme 9
- B3 domain-containing protein At5g60140
- DUF674 family protein
- Transmembrane protein
- Berberine bridge enzyme-like 1
- At5g58530
- MEI2 C-terminal RRM only like 2
- At4g19430
Sequence:
MATDSFIKLNPISFNRARFDLRDFAGISPKSISSLCCISPRLISCNHFSPRTLISGENGNILFSKKKIPAFVRCQTSLGIGRNQKWWEKELKPNMKSVTSPQDLVVSLRNAGDKLVVVDFFSPSCGGCKALHPKICKIAEKNPEVEFLQVNYEEHRSLCQSLNIHVLPFFRFYRGSSGRVCSFSCTNATIRKFKEALEKHGREQCSIGETKGLEEKELVAMAANKDLSFDYKPTSCGNIQEQKKKEIFLPKSPTFNKQKEVEHSLLLVSPAPA
Protein: Homeobox A4 (H0YHX3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
XKSPLGLKGKEPVVYPWMKKIHVSAVNPSYNGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQVKIWFQNRRMKWKKDHKLPNTKMRSSNSASASAGPPGKAQTQSPHLHPHPHPSTSTPVPSSI
Protein: Psychosine receptor (G-protein coupled receptor 65) (T-cell death-associated gene 8 protein) (Q61038)
Organism: Mus musculus (Mouse)
Function: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids (By similarity). Plays a role in immune response by maintaining lysosome function and supporting phagocytosis-mediated intracellular bacteria clearance. May have a role in activation-induced cell death or differentiation of T-cells.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAMNSMCIEEQHHLEHYLFPVVYIIVFIVSVPANIGSLCVSFLQAKKENELGIYLFSLSLSDLLYALTLPLWINYTWNKDNWTFSPTLCKGSVFFTYMNFYSSTAFLTCIALDRYLAVVYPLKFSFLRTRRFAFITSLSIWILESFFNSMLLWKDETSVEYCDSDKSNFTLCYDKYPLEKWQINLNLFRTCMGYAIPLITIMICNHKVYRAVRHNQATENSEKRRIIKLLASITLTFVLCFTPFHVMVLIRCVLERDMNVNDKSGWQTFTVYRVTVALTSLNCVADPILYCFVTETGRADMWNILKLCTRKHNRHQGQKRDILSVSTRDAVELEIID
Protein: Niacin transporter NiaX (A0A0H2UQ73)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MSGLLYHTSVYAVKKEILVNTRKKTQFMTMTALLTAIAILIPIVMPFKIVIPPASYTLGSHIAIFIAMFLSPLMAVFVILASSFGFLMAGYPMVIVFRAFSHISFGALGALYLQKFPDTLDKPKSSWIFNFVLAVVHALAEVLACVVFYATSGTNVENMFYVLFVLVGFGTIIHSMVDYTLALAVYKVLRKRR
Protein: Cell cycle associated protein 1 (E9PLA9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLL
Protein: Schwannomin interacting protein 1 (C9JWG6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNLDSDGMDDIISQESSLDMEGNYKKAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK
Protein: Rho-related protein racG (Q9GPS0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Protein BRICK1
- Mss4-like family protein
- Protein pirA
- Cofilin-1A
- Serine/threonine-protein kinase pakB
Sequence:
MKSIKVCVVGEGGIGKTSMLLSYTSNSISNEYQPTVFDNYSTLLMHNKKPYNLSLWDTAGQEEFSKLRRLSYPQTDVFLLCFSLINPSSFSNILDSWVQELNENCPNTPIVLVGTQMDLKSNSVILDRLCEKKQLPISTQQGIELSKKINAFDFVECSALTQKNLHLVFEKAIDACEAHQKCQSKEKKKNNKKFKKNCIIM
Protein: Transketolase (TK) (EC 2.2.1.1) (P9WG25)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Glucose-6-phosphate 1-dehydrogenase 2
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase class 2
- Fructose-bisphosphate aldolase
- Pyruvate kinase
- Enolase
- Ribose-phosphate pyrophosphokinase
Sequence:
MTTLEEISALTRPRHPDYWTEIDSAAVDTIRVLAADAVQKVGNGHPGTAMSLAPLAYTLFQRTMRHDPSDTHWLGRDRFVLSAGHSSLTLYIQLYLGGFGLELSDIESLRTWGSKTPGHPEFRHTPGVEITTGPLGQGLASAVGMAMASRYERGLFDPDAEPGASPFDHYIYVIASDGDIEEGVTSEASSLAAVQQLGNLIVFYDRNQISIEDDTNIALCEDTAARYRAYGWHVQEVEGGENVVGIEEAIANAQAVTDRPSFIALRTVIGYPAPNLMDTGKAHGAALGDDEVAAVKKIVGFDPDKTFQVREDVLTHTRGLVARGKQAHERWQLEFDAWARREPERKALLDRLLAQKLPDGWDADLPHWEPGSKALATRAASGAVLSALGPKLPELWGGSADLAGSNNTTIKGADSFGPPSISTKEYTAHWYGRTLHFGVREHAMGAILSGIVLHGPTRAYGGTFLQFSDYMRPAVRLAALMDIDTIYVWTHDSIGLGEDGPTHQPIEHLSALRAIPRLSVVRPADANETAYAWRTILARRNGSGPVGLILTRQGVPVLDGTDAEGVARGGYVLSDAGGLQPGEEPDVILIATGSEVQLAVAAQTLLADNDILARVVSMPCLEWFEAQPYEYRDAVLPPTVSARVAVEAGVAQCWHQLVGDTGEIVSIEHYGESADHKTLFREYGFTAEAVAAAAERALDN
Protein: Odorant-binding protein (OBP) (P08937)
Organism: Rattus norvegicus (Rat)
Function: This protein is found in nasal epithelium and it binds a wide variety of chemical odorants.
Subcellular location: Secreted.
Interaction partners:
- Vomeromodulin
- Allergen Fel d 4-like
Sequence:
MVKFLLIVLALGVSCAHHENLDISPSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYFHVLKKTDDIIFFHNVNVDESGRRQCDLVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTCNQ
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (70 kDa mitochondrial autoantigen of primary biliary cirrhosis) (PBC) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (P08461)
Organism: Rattus norvegicus (Rat)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:3571977}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Ac1164
- Citrate synthase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- ATP-citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MWRVCARRVQSAVPRAGFRARWATLKGPRTGPAAVRCGSGIPSYGVRSLCGWSYGSATVPRNRILQQLLGSPSRRSYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEAFKNYTLDSATAATQAAPAPAAAPAAAPAAPSASAPGSSYPVHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKQEDIAAFADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQPLAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTKAAPAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL
Protein: Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A) (P12345)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids.
Subcellular location: Mitochondrion matrix {ECO:0000250}. Cell membrane {ECO:0000250}.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- alanine transaminase
- Malate dehydrogenase
- Glutamate dehydrogenase 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Aspartate aminotransferase
- L-lactate dehydrogenase A chain
- L-lactate dehydrogenase
- L-lactate dehydrogenase
- Tyrosine aminotransferase
Sequence:
MALLHSARVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAYKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKGLDKEYLPIGGLAEFCRASAELALGENSEVVKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQSYRYYDPKTCGFDFTGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVICKDADEAKRVESQLKILIRPMYSNPPIHGARIASTILTSPDLRKQWLQEVKGMADRIIGMRTQLVSNLKKEGSTHSWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
Protein: Protein S100-A4 (Metastasin) (Nerve growth factor-induced protein 42A) (P9K) (Placental calcium-binding protein) (S100 calcium-binding protein A4) (P05942)
Organism: Rattus norvegicus (Rat)
Function: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By similarity). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000250|UniProtKB:P07091}.
Interaction partners:
- Annexin A2
- Myosin-9
- Annexin A1
- Cellular tumor antigen p53
- Fibroblast growth factor 2
- Protein S100-A10
- Pro-epidermal growth factor
- Advanced glycosylation end product-specific receptor
- Protein S100-A6
- Galectin-1
Sequence:
MARPLEEALDVIVSTFHKYSGNEGDKFKLNKTELKELLTRELPSFLGRRTDEAAFQKLMNNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK