wanglab/gogpt-training-data huggingface dataset:
Protein: T-cell surface glycoprotein CD4 (T-cell differentiation antigen L3T4) (T-cell surface antigen T4/Leu-3) (CD antigen CD4) (P06332)
Organism: Mus musculus (Mouse)
Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase LCK
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 4
- T-cell surface glycoprotein CD8 alpha chain
- Tyrosine-protein kinase ZAP-70
- H-2 class II histocompatibility antigen, A beta chain
- H2-O alpha
- T-cell surface glycoprotein CD8 beta chain
- CD40 ligand
- Tyrosine-protein kinase Fyn
Sequence:
MCRAISLRRLLLLLLQLSQLLAVTQGKTLVLGKEGESAELPCESSQKKITVFTWKFSDQRKILGQHGKGVLIRGGSPSQFDRFDSKKGAWEKGSFPLIINKLKMEDSQTYICELENRKEEVELWVFKVTFSPGTSLLQGQSLTLTLDSNSKVSNPLTECKHKKGKVVSGSKVLSMSNLRVQDSDFWNCTVTLDQKKNWFGMTLSVLGFQSTAITAYKSEGESAEFSFPLNFAEENGWGELMWKAEKDSFFQPWISFSIKNKEVSVQKSTKDLKLQLKETLPLTLKIPQVSLQFAGSGNLTLTLDKGTLHQEVNLVVMKVAQLNNTLTCEVMGPTSPKMRLTLKQENQEARVSEEQKVVQVVAPETGLWQCLLSEGDKVKMDSRIQVLSRGVNQTVFLACVLGGSFGFLGFLGLCILCCVRCRHQQRQAARMSQIKRLLSEKKTCQCPHRMQKSHNLI
Protein: Myosin type-2 heavy chain 1 (Myosin type II heavy chain 1) (Q9USI6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cell division. It is a component of the cdc12 'spot', a structure thought to mark the site of septation. May work in conjunction with myo3.
Interaction partners:
- Myosin regulatory light chain cdc4
- Myosin regulatory light chain 1
- Cell division control protein 12
- Actin
- Ras GTPase-activating-like protein rng2
- Cell division control protein 15
- Tropomyosin
- Myosin type-2 heavy chain 2
- Ring assembly protein 3
- Anillin-related medial ring protein mid1
Sequence:
MTEVISNKITAKDGATSLKDIDDKRWVWISDPETAFTKAWIKEDLPDKKYVVRYNNSRDEKIVGEDEIDPVNPAKFDRVNDMAELTYLNEPAVTYNLEQRYLSDQIYTYSGLFLVAVNPYCGLPIYTKDIIQLYKDKTQERKLPHVFAIADLAYNNLLENKENQSILVTGESGAGKTENTKRIIQYLAAIASSTTVGSSQVEEQIIKTNPVLESFGNARTVRNNNSSRFGKFIKVEFSLSGEISNAAIEWYLLEKSRVVHQNEFERNYHVFYQLLSGADTALKNKLLLTDNCNDYRYLKDSVHIIDGVDDKEEFKTLLAAFKTLGFDDKENFDLFNILSIILHMGNIDVGADRSGIARLLNPDEIDKLCHLLGVSPELFSQNLVRPRIKAGHEWVISARSQTQVISSIEALAKAIYERNFGWLVKRLNTSLNHSNAQSYFIGILDIAGFEIFEKNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYMKEEIVWDFIDFGHDLQPTIDLIEKANPIGILSCLDEECVMPKATDATFTSKLDALWRNKSLKYKPFKFADQGFILTHYAADVPYSTEGWLEKNTDPLNENVAKLLAQSTNKHVATLFSDYQETETKTVRGRTKKGLFRTVAQRHKEQLNQLMNQFNSTQPHFIRCIVPNEEKKMHTFNRPLVLGQLRCNGVLEGIRITRAGFPNRLPFNDFRVRYEIMAHLPTGTYVESRRASVMILEELKIDEASYRIGVSKIFFKAGVLAELEERRVATLQRLMTMLQTRIRGFLQRKIFQKRLKDIQAIKLLQANLQVYNEFRTFPWAKLFFNLRPLLSSTQNDKQLKKRDAEIIELKYELKKQQNSKSEVERDLVETNNSLTAVENLLTTERAIALDKEEILRRTQERLANIEDSFSETKQQNENLQRESASLKQINNELESELLEKTSKVETLLSEQNELKEKLSLEEKDLLDTKGELESLRENNATVLSEKAEFNEQCKSLQETIVTKDAELDKLTKYISDYKTEIQEMRLTNQKMNEKSIQQEGSLSESLKRVKKLERENSTLISDVSILKQQKEELSVLKGVQELTINNLEEKVNYLEADVKQLPKLKKELESLNDKDQLYQLQATKNKELEAKVKECLNNIKSLTKELENKEEKCQNLSDASLKYIELQEIHENLLLKVSDLENYKKKYEGLQLDLEGLKDVDTNFQELSKKHRDLTFNHESLLRQSASYKEKLSLASSENKDLSNKVSSLTKQVNELSPKASKVPELERKITNLMHEYSQLGKTFEDEKRKALIASRDNEELRSLKSELESKRKLEVEYQKVLEEVKTTRSLRSEVTLLRNKVADHESIRSKLSEVEMKLVDTRKELNSALDSCKKREAEIHRLKEHRPSGKENNIPAVKTTEPVLKNIPQRKTIFDLQQRNANQALYENLKRDYDRLNLEKHNLEKQVNELKGAEVSPQPTGQSLQHVNLAHAIELKALKDQINSEKAKMFSVQVQYEKREQELQKRIASLEKVNKDSLIDVRALRDRIASLEDELRAA
Protein: LD03170p (Rho guanine nucleotide exchange factor 4) (Q9VS45)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Kinesin-like protein Klp61F
Sequence:
MFTPRQKGYGNGFIHSPQTPLSFSRELRQVLQERNLLTAKSRRKVCSMLDSNNSSPIGSPNPDAGKRLGFRRQAIQEIISSEKSYLEQLELLMNFFVRPLKEQAIIDCSNHTLLFGQIEMIHNLNGEFLRELEANMENVAHAFLKMAPFFKLYSVYAFDYRGALFIIQDLISKNPVFRKFLEQTESRPEVQRKLNSLMIVPIQRVPRYKLLLEQVLLYTSPADADYKLLKESVKEIEATASHINTCVEEQEITQYLIHLQNSLVNRTPNIVKPSRRVIKEGVLQKITHKGTEIKRYCVLMSDIFMYCKMIKERAPNTVVENSLECCCIFPLKKCKVYEMLPGNFKLTCQSDGIIFGSGDVQLSRTWVGFIRDAIDLHVQCRKTLRKDSSKRTPIRKKDMKKFGADYVLSPNKRKCEYDTVFRNKNRSTDSEEETEDSACFSRKRKVASGILRAPNGNPMGKASSSSSSSVSMKRVAPPPPAPPPPPAVQMRHQPGRPGELATASKENRISKLYKKIAAGDKVANVRGILKRSNVPAPNNDHDPSYGFASRYSDSKSYFRAHNVDNTIPTFVKREDLFNGDNMFPVHLKSHEEICTPPQKKRVKFDDTLDAVSPVLVEKPFAFSSESSSALKPTSLRERIYDFFANLF
Protein: Methyltransferase domain-containing protein (Q8I4K4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MERVPESRIDVIVFVNSSDNLVSADCASIPHSLRDLKANLKLFEYNRKCVENPSDLWRQWTGTTRDGLNASFRTISSANGLVRKRIKAKKQHEIDRIVELISQIQIFQKDSADPIDSLVDIGAGIGHLSRMISIHNNISVMAVEGNQQFTLAANSLDEKLLLDSAKIGSRIENFNVKSTPIRYTNFVTEDLALKIDDFAVNSAILVGLHCCGDFSSTILKVFQKSEKSKALVLFGCCYHKEFQCFHFLRPENNENEREISENTSFGKSTVFPLSKKWENVEIDYLLREAACHNNENLEERFLKQKIDLSRYARSYLEKWIWKVSELPEDRNIGMCSVKCIENQTTFEEYIRKAMANRGNHLLDKVLQIIPQSELSAHVSSLRSSQFDSFEVLRCMFAPAIESAIIDDRVELLRENGINSRVVPLFEPSISPRNLAIIAYK
Protein: (S)-beta-macrocarpene synthase (EC 5.5.1.17) (Alpha-terpinolene synthase) (EC 4.2.3.113) (Beta-bisabolene synthase) (EC 4.2.3.55) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.16) (Linalool synthase) (EC 4.2.3.25) (Terpene synthase 6) (Q5GJ60)
Organism: Zea mays (Maize)
Function: Involved in the biosynthesis of the bicyclic sesquiterpene (S)-beta-macrocarpene. Can use both geranyl diphosphate and farnesyl diphosphate as substrate, but not geranylgeranyl diphosphate. Produces mainly (S)-beta-macrocarpene, but also smaller amounts of beta-bisabolene and (E)-beta-farnesene when used with farnesyl diphosphate as substrate. In the presence of geranyl diphosphate, produces the acyclic monoterpenes beta-myrcene and linalool along with minor amounts of the cyclic compounds limonene, alpha-thujene, sabinene and alpha-terpinolene. May be involved in plant defense.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
Interaction partners:
- (S)-beta-macrocarpene synthase (Alpha-terpinolene synthase) (Beta-bisabolene synthase) (Beta-myrcene synthase) (Limonene synthase) (Linalool synthase) (Terpene synthase 11)
- Alpha-humulene/
- Putative cyclotide family protein
- Ent-copalyl diphosphate synthase 2, chloroplastic
Sequence:
MAAPTLTADGPRLGQQEMKKMSPSFHPTLWGDFFLSYEAPTEAQEAQMREKAAVLKEEVRNMIKGSHDVPEIVDLIITLQRLNLDYHYEDEINEKLTVVYKSNYDGGNLDLVSRRFYLLRKCGYDVSSDVFLKFKDQLGNFVEADTRSLLSLYNAAFLRIHGETVLDEAISFTMRVLQDRLEHLESPLAEEVSSALDTPLFRRVGTLEMKDYIPIYEKDAKQNKSILEFAKLNFNLLQLRYSSELKECTTWWKELRVESNLSFVRDRIVEVYFWMSGGCYDPQYSHSRIILTKIVAFITILDDTLDSHATSCESMQLAEAIERWDESAVSLLPEYMKDFYMYLLKTFSSFENELGPDKSYRVFYLKEAVKELVREYTKEIKWRDEDYVPKTLKEHLKVSLISIGGTLVLCSAFVGMGDVVTKKIMKWVMSDAELVKSFGIFVRLSNDIVSTKREQREKHCVSTVQCYMKQHEITMDEACEQIKELTEDSWKFMIEQGLALKEYPIIVPRTVLEFARTVDYMYKEADKYTVSHTIKDMLTSLYVKPVLM
Protein: Tyrosine-protein kinase FRK (EC 2.7.10.2) (FYN-related kinase) (Nuclear tyrosine protein kinase RAK) (Protein-tyrosine kinase 5) (P42685)
Organism: Homo sapiens (Human)
Function: Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7696183}. Nucleus {ECO:0000269|PubMed:7696183}. Note=Predominantly found in the nucleus, with a small fraction found in the cell periphery.
Interaction partners:
- Mirror-image polydactyly gene 1 protein
- Astrotactin-2
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Protein hinderin
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
- ADAMTS-like protein 3
- Tyrosine-protein kinase CSK
Sequence:
MSNICQRLWEYLEPYLPCLSTEADKSTVIENPGALCSPQSQRHGHYFVALFDYQARTAEDLSFRAGDKLQVLDTLHEGWWFARHLEKRRDGSSQQLQGYIPSNYVAEDRSLQAEPWFFGAIGRSDAEKQLLYSENKTGSFLIRESESQKGEFSLSVLDGAVVKHYRIKRLDEGGFFLTRRRIFSTLNEFVSHYTKTSDGLCVKLGKPCLKIQVPAPFDLSYKTVDQWEIDRNSIQLLKRLGSGQFGEVWEGLWNNTTPVAVKTLKPGSMDPNDFLREAQIMKNLRHPKLIQLYAVCTLEDPIYIITELMRHGSLQEYLQNDTGSKIHLTQQVDMAAQVASGMAYLESRNYIHRDLAARNVLVGEHNIYKVADFGLARVFKVDNEDIYESRHEIKLPVKWTAPEAIRSNKFSIKSDVWSFGILLYEIITYGKMPYSGMTGAQVIQMLAQNYRLPQPSNCPQQFYNIMLECWNAEPKERPTFETLRWKLEDYFETDSSYSDANNFIR
Protein: Enhancer of polycomb homolog 2 (EPC-like) (Q52LR7)
Organism: Homo sapiens (Human)
Function: May play a role in transcription or DNA repair.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Chromatin modification-related protein MEAF6
- Transformation/transcription domain-associated protein
- DNA methyltransferase 1-associated protein 1
- Inhibitor of growth protein 3
- YEATS domain-containing protein 4
- Mortality factor 4-like protein 1
- MRG/MORF4L-binding protein
- Histone acetyltransferase KAT5
- Actin-like protein 6A
- Bromodomain-containing protein 8
Sequence:
MSKLSFRARALDAAKPLPIYRGKDMPDLNDCVSINRAVPQMPTGMEKEEESEHHLQRAISAQQVFREKKESMVIPVPEAESNVNYYNRLYKGEFKQPKQFIHIQPFNLDNEQPDYDMDSEDETLLNRLNRKMEIKPLQFEIMIDRLEKASSNQLVTLQEAKLLLNEDDYLIKAVYDYWVRKRKNCRGPSLIPQIKQEKRDGSTNNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRREFSRAITILEMIKRREKTKRELLHLTLEVVEKRYHLGDYGGEILNEVKISRSEKELYATPATLHNGNHHKVQECKTKHPHHLSLKEEASDVVRQKKKYPKKPKAEALITSQQPTPETLPVINKSDIKQYDFHSSDEDEFPQVLSPVSEPEEENDPDGPCAFRRRAGCQYYAPRLDQANHSCENSELADLDKLRYRHCLTTLTVPRRCIGFARRRIGRGGRVIMDRISTEHDPVLKQIDPEMLNSFSSSSQTIDFSSNFSRTNASSKHCENRLSLSEILSNIRSCRLQCFQPRLLNLQDSDSEECTSRKPGQTVNNKRVSAASVALLNTSKNGISVTGGITEEQFQTHQQQLVQMQRQQLAQLQQKQQSQHSSQQTHPKAQGSSTSDCMSKTLDSASAHFAASAVVSAPVPSRSEVAKEQNTGHNNINGVVQPSGTSKTLYSTNMALSSSPGISAVQLVRTVGHTTTNHLIPALCTSSPQTLPMNNSCLTNAVHLNNVSVVSPVNVHINTRTSAPSPTALKLATVAASMDRVPKVTPSSAISSIARENHEPERLGLNGIAETTVAMEVT
Protein: Voltage-gated delayed rectifier potassium channel KCNH8 (Ether-a-go-go-like potassium channel 3) (ELK channel 3) (RELK3) (Potassium voltage-gated channel subfamily H member 8) (Voltage-gated potassium channel subunit Kv12.1) (Q9QWS8)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ELK4, member of ETS oncogene family
Sequence:
MPVMKGLLAPQNTFLDTIATRFDGTHSNFILANAQVAKGFPIVYCSDGFCELAGFARTEVMQKSCSCKFLFGVETNEQLMLQIEKSLEEKVEFKGEIMFYKKNGAPFWCLLDIVPIKNEKGDVVLFLASFKDITDTKVKITSEDKKEDRAKGRSRAGSHFDSARRRSRAVLYHISGHLQRREKNKLKINNNVFVDKPAFPEYKVSDAKKSKFILLHFSTFKAGWDWLILLATFYVAVTVPYNVCFIGNEDLSTTRSTTVSDIAVEILFIIDIILNFRTTYVSKSGQVIFEARSICIHYVTTWFIIDLIAALPFDLLYAFNVTVVSLVHLLKTVRLLRLLRLLQKLDRYSQHSTIVLTLLMSMFALLAHWMACIWYVIGKMEREDNSLLKWEVGWLHELGKRLESPYYGNNTLGGPSIRSAYIAALYFTLSSLTSVGFGNVSANTDAEKIFSICTMLIGALMHALVFGNVTAIIQRMYSRWSLYHTRTKDLKDFIRVHHLPQQLKQRMLEYFQTTWSVNNGIDSNELLKDFPDELRSDITMHLNKEILQLSLFECASRGCLRSLSLHIKTSFCAPGEYLLRQGDALQAIYFVCSGSMEVLKDSMVLAILGKGDLIGANLSIKDQVIKTNADVKALTYCDLQCIILKGLFEVLGLYPEYAHKFVEDIQHDLTYNLREGHESDVISRLSNKSTVPQAEPKGNGSIKKRLPSIVEDEEEEEVEEEETTSLSPIYTRGSSVSHSKKTGSSKSYLGLSLKQLTSGTVPFHSPIRVSSANSPKTKQEADPPNHGTRKEKNLKVQLCSLGTAGTPELSPRIVDGIEDGNSSEETQTFDFGSEQIRPEPRISPSLGESEIGAAFLFIKAEETKQQINKLNSEVTTLTQEVSQLGKDMRSIMQLLENILSPQQPSQFCSLHPTSICPSRESFQTRVSWSAHQPCLHLQANGAHLYHGNVTSDIWSVDPSLVGSNPQRTEAHEQSPVDSELHHSPNLAYSPSHCQVIQEGHLQFLRCISPHSDTTLTPLQSISATLSSSVCSSSETSLHLVLPSRSEEGSITHGPVSSFSLENLPGSWDREGMMSASTEPLENFPVEVVTSTADVKDSKAINV
Protein: Hydrophilin YNL190W (P53872)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrophilin which is essential to overcome the simple stress of the desiccation-rehydration process.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:9613572}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Putative uncharacterized protein YPL025C
Sequence:
MKFSSVTAITLATVATVATAKKGEHDFTTTLTLSSDGSLTTTTSTHTTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTKHDTTTYGPGEKARKNNAAPGPSNFNSIKLFGVTAGSAAVAGALLLL
Protein: Collagen alpha-1(III) chain (P02461)
Organism: Homo sapiens (Human)
Function: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
- Lumican
- Collagen alpha-1
- Periostin
- Integrin alpha-2
- Procollagen C-endopeptidase enhancer 1
- Fibrillin-1
- Collagen alpha-1
Sequence:
MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAGTPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL
Protein: Mitochondrial uncoupling protein 4 (Q9CX10)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MPIAEEEKLLPLTQRWPRTSKFLLSGCAATVAELATFPLDLTKTRLQMQGEAAIARLGDGAVDSAPYRGMVRTALGIVQEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDKHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRRLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWIPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNISTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRSVKPLVPTCWRGCSSVGD
Protein: PAN2-PAN3 deadenylation complex subunit PAN3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (P34653)
Organism: Caenorhabditis elegans
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins. Within the PAN complex, may positively regulate fertility.
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181}.
Interaction partners:
- PolyA-specific ribonuclease subunit panl-2
- Polyadenylate-binding protein
- Polyadenylate-binding protein
- LysM domain-containing protein
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Uncharacterized protein R10E11.5
- Uncharacterized protein T05G5.4
- Serpentine receptor class XA 10
- Target of EGR1 protein 1
- Nucleolin homolog 1
Sequence:
MQPGEGYHYDSGPNNAVHPHQLPAGSRLNQYLANNNRQGPSFGPGTPINVNAPVFVPKHQQPQPAQVAAPPPMVNQFAQLSIHDVPHQMIPFGQINGPPTFGPGQHMNHRASHHHQSPQMAQQPPTLQQSAYDRYQLENRGGTTYFYTEPTEAGPDDEQYTEAEAPDGSILVNTPGAFGYNAPLPISHMARFRGKANANLQTQFISPEIRMELINRQLAYDTKADSAIIGDIPHSVEHFSNLVPLEIAGIQSQTTYKAFSCRDGNYYCLRRIHGNRIQHPGKQTHLVEQWKKLVHGNVVPLREVLINCRAFDDSSLIFAYDYYPLAGTLMEKHFDTKSGTFFDPNNGFRISSPMNVSMPISGTGAHETLIWSYIIQIAAALRAIHSSGLACRTLDLNKIITYGNKIMISFCGIQDVLDPDPTTIQQQQNEDLNMFGNLIVALATGRANGWRKDLYQQLKKFIEDTYSMDLRNVIGFLHNNSTRKTINEIMPMIGGRFFTVMENMQAKTDVLEAELSREMENGRLFRLVAKMNTVLERVEHGTDDAWSETGDRFMLKLFRDYVFHQVTDQGKAWLDMAHIVQCLNKLDCGSQEKIEMVSRSGDTQIIIDYATLKRCLDKSFRDLLGTNMMLHR
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (M0R003)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
XAASAAVFSRLRSGLRLGSRGLCTRLATPPRRAPDQAAEIGSRGSTKAQGPQQQPGSEGPSYAKKVALWLAGLLGAGGTVSVVYIFGNNPVDENGAKMIIEPTSPCLLPDPLQEPYYQPPYTLVLELTGVLLHPEWSLATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGVALRPWDGNSDDRVLLDLSAFLK
Protein: Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha 1,2-fucosyltransferase) (Alpha 1,2-fucosyltransferase B) (Alpha 1-2 fucosyltransferase) (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (Secretor blood group alpha-2-fucosyltransferase) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344) (Q10984)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition (By similarity). Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Hexosyltransferase
- Hexosyltransferase
- Histo-blood group ABO system transferase 2
- Histo-blood group ABO system transferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- Hexosyltransferase
- Histo-blood group ABO system transferase 2
Sequence:
MASAQVPFSFPLAHFLIFVFVTSTITHLQQRIVKLQPLSEKELPMTTQMSSGNTESPEMRRDSEQHGNGELRGMFTINSIGRLGNQMGEYATLFALARMNGRLAFIPASMHNALAPIFRISLPVLHSDTAKKIPWQNYHLNDWMEERYRHIPGHFVRFTGYPCSWTFYHHLRPEILKEFTLHDHVREEAQAFLRGLRVNGSQPSTFVGVHVRRGDYVHVMPNVWKGVVADRGYLEKALDMFRARYSSPVFVVTSNGMAWCRENINASRGDVVFAGNGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLAGGDTIYLANYTLPDSPFLKVFKPEAAFLPEWVGIPADLSPLLKH
Protein: Probable pectinesterase/pectinesterase inhibitor 23 [Includes: Pectinesterase inhibitor 23 (Pectin methylesterase inhibitor 23); Pectinesterase 23 (PE 23) (EC 3.1.1.11) (Pectin methylesterase 23) (AtPME23)] (Q8GXA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- At1g10770
- Pectinesterase inhibitor 5
- Ubiquitin-conjugating enzyme family protein
- CRIB domain-containing protein RIC5
- Probable pectate lyase 3
- Cation/H
- Pectate lyase
- Pectate lyase
Sequence:
MGSDGDKKKKFIVAGSVSGFLVIMVVSVAVVTSKHSPKDDENHIRKTTKAVQAVCAPTDFKDTCVNSLMGASPDSDDPVDLIKLGFKVTIKSINESLEKASGDIKAKADKNPEAKGAFELCEKLMIDAIDDLKKCMDHGFSVDQIEVFVEDLRVWLSGSIAFQQTCMDSFGEIKSNLMQDMLKIFKTSRELSSNSLAMVTRISTLIPNSNLTGLTGALAKYARKLLSTEDSIPTWVGPEARRLMAAQGGGPGPVKANAVVAQDGTGQFKTITDALNAVPKGNKVPFIIHIKEGIYKEKVTVTKKMPHVTFIGDGPNKTLITGSLNFGIGKVKTFLTATITIEGDHFTAKNIGIENTAGPEGGQAVALRVSADYAVFHSCQIDGHQDTLYVHSHRQFYRDCTVSGTVDFIFGDAKCILQNCKIVVRKPNKGQTCMVTAQGRSNVRESTGLVLHGCHITGDPAYIPMKSVNKAYLGRPWKEFSRTIIMKTTIDDVIDPAGWLPWSGDFALKTLYYAEHMNTGPGSNQAQRVKWPGIKKLTPQDALLYTGDRFLRGDTWIPQTQVPYTAKV
Protein: Aquaporin 8 (A0A077CZQ7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
SGSHFNPPFTIAIYLCGGMKLNMVGPYLISQLIGGVLGASMSKLMTTTENYSKAQGAAFALLQSQDQLWGALFGEIAMTCLVTMVVLLGAVNAKSSSPMVPFMVGCTVIINILAGGDVSGTCLNPARALGPAIVANYWTYHWVYWVGPITGGLVAAALVRLLLGD
Protein: Vancomycin/teicoplanin A-type resistance protein VanA (EC 6.1.2.1) (D-alanine--D-lactate ligase) (VanA ligase) (P25051)
Organism: Enterococcus faecium (Streptococcus faecium)
Function: Required for high-level resistance to glycopeptide antibiotics. D-Ala--D-Ala ligase of altered specificity which catalyzes ester bond formation between D-Ala and various D-hydroxy acids; produces a peptidoglycan which does not terminate in D-alanine but in D-lactate, thus preventing vancomycin or teicoplanin binding.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2266943}; Peripheral membrane protein {ECO:0000303|PubMed:2266943}; Cytoplasmic side {ECO:0000303|PubMed:2266943}.
Interaction partners:
Sequence:
MNRIKVAILFGGCSEEHDVSVKSAIEIAANINKEKYEPLYIGITKSGVWKMCEKPCAEWENDNCYSAVLSPDKKMHGLLVKKNHEYEINHVDVAFSALHGKSGEDGSIQGLFELSGIPFVGCDIQSSAICMDKSLTYIVAKNAGIATPAFWVINKDDRPVAATFTYPVFVKPARSGSSFGVKKVNSADELDYAIESARQYDSKILIEQAVSGCEVGCAVLGNSAALVVGEVDQIRLQYGIFRIHQEVEPEKGSENAVITVPADLSAEERGRIQETAKKIYKALGCRGLARVDMFLQDNGRIVLNEVNTLPGFTSYSRYPRMMAAAGIALPELIDRLIVLALKG