wanglab/gogpt-training-data huggingface dataset:
Protein: MICOS complex subunit MIC60 (Cell proliferation-inducing gene 4/52 protein) (Mitochondrial inner membrane protein) (Mitofilin) (p87/89) (Q16891)
Organism: Homo sapiens (Human)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:25781180}.
Interaction partners:
- Sorting and assembly machinery component 50 homolog
- MICOS complex subunit MIC27
- MICOS complex subunit MIC10
- MICOS complex subunit MIC19
- MICOS complex subunit MIC26
- MICOS complex subunit MIC25
- MICOS complex subunit MIC13
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Metaxin-2
- DnaJ homolog subfamily C member 11
Sequence:
MLRACQLSGVTAAAQSCLCGKFVLRPLRPCRRYSTSGSSGLTTGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFEMVLGPAAYNVPLPKKSIQSGPLKISSVSEVMKESKQPASQLQKQKGDTPASATAPTEAAQIISAAGDTLSVPAPAVQPEESLKTDHPEIGEGKPTPALSEEASSSSIRERPPEEVAARLAQQEKQEQVKIESLAKSLEDALRQTASVTLQAIAAQNAAVQAVNAHSNILKAAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKSVIENAKKKEVAGAKPHITAAEGKLHNMIVDLDNVVKKVQAAQSEAKVVSQYHELVVQARDDFKRELDSITPEVLPGWKGMSVSDLADKLSTDDLNSLIAHAHRRIDQLNRELAEQKATEKQHITLALEKQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKIEEVRDAMENEMRTQLRRQAAAHTDHLRDVLRVQEQELKSEFEQNLSEKLSEQELQFRRLSQEQVDNFTLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAETPTIPLGSAVEAIKANCSDNEFTQALTAAIPPESLTRGVYSEETLRARFYAVQKLARRVAMIDETRNSLYQYFLSYLQSLLLFPPQQLKPPPELCPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTAYASAVGIGTTQVQPE
Protein: 3,2-trans-enoyl-CoA isomerase, mitochondrial, putative (EC 5.3.3.8) (Q57V74)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Enoyl-CoA delta isomerase 1, mitochondrial
- Probable enoyl-CoA hydratase, mitochondrial
- propanoyl-CoA C-acyltransferase
- Nonspecific lipid-transfer protein, putative
Sequence:
MRRSVVTSLHTASFASLTRVGVFNVAAVAHLAIRSQTTMHGAPGNTSPGPRPPVQQGTVPMQHHQQMHPSAVGAEAEDDFEPPCKPSEPPKMLKVDTSDRGITTVALNRAPVNSLSLELFEELNSWMLWLGSDESCRAVILTSSIPTVFSAGLDINELHNPEPERLRRFWKSFQEAWLILNSFPKPIIGAVSGNSPAGGCVLALGCDFRVMLRHPTDKPDRPFRIGLNETKLGITTPPWVVPAYAYVLGSRRAERMLQLGDTPTADEALRVGLVDLVVDGEQQLREAVLKEAERFLSVPQQSRWMLRDMLRREYLQVIGSEEDREYDTQFFVELMMNPDVQKSLEAFTARLKGVAAKK
Protein: Actin nucleation-promoting factor WASL (Neural Wiskott-Aldrich syndrome protein) (N-WASP) (O00401)
Organism: Homo sapiens (Human)
Function: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9422512}. Nucleus {ECO:0000269|PubMed:16767080}. Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q91YD9}.
Interaction partners:
- Cell division control protein 42 homolog
- WAS/WASL-interacting protein family member 2
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 3
- Src substrate cortactin
- SH2/SH3 adapter protein NCK1
- Actin-related protein 2
- Intersectin-1
- WAS/WASL-interacting protein family member 1
- WAS/WASL-interacting protein family member 3
Sequence:
MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPSVAVPPPPPNRMYPPPPPALPSSAPSGPPPPPPSVLGVGPVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVADGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDEEDFEDDDEWED
Protein: Tryptophan synthase alpha chain (EC 4.2.1.20) (P0A877)
Organism: Escherichia coli (strain K12)
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Interaction partners:
- Tryptophan synthase beta chain
- Bifunctional protein TrpGD
- Anthranilate synthase component 1
- Tryptophan biosynthesis protein TrpCF
- Aminodeoxychorismate synthase component 1
- Serine hydroxymethyltransferase
- Tryptophanase
- L-threonine dehydratase biosynthetic IlvA
- L-threonine dehydratase catabolic TdcB
- Sodium/proline symporter
Sequence:
MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS
Protein: SSD domain-containing protein (Q09934)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRSLLLPYHPSEMLRQQRQIQMNWISYYLGNHPRCVLFSVFCVLIPLLSYFVIYPLEIECDIRRGFANKHGHAVEELTKFSNFYNISVGGLEIWGVLARNKTTDTDLHINLKLLNEIDQLHQFVWNYTTQYKQETIRFKDLSSEDINYVFNYYRKLLAIEWMPGVNLSYPLAEAFGHPFYLGNQFFGVNNGQASKAGPIKTAKFVALWYMSKAETFEQKQKLQAVQLGIFKKSAERPNNLQFDFEMFGDQVANSEMLRGTLTTVKLFFIGGCLMVAFMACTFTELTIFSKCMLIAGAIGSPLAATGACFAILGWVGHPFNSIMCITPFLILGIGVDDAFLLLNCWRREEGKDKSAKQAENQLARVIREISPSMAITSLTNTMAFGVGFLAPTPQMSSFCLGTALAIVLDFLLEFLIFVPCMVLFYKKKPEIIAIENEEFANEKTEKRSETSTGKYSRINWKCFTNLLLSVPGRVLVIILYFSIFTASYFGVAKMEKTFDPSKTFPSDSKLVDSLASFTSIQVEYSPLNFLSSVPDLKNDTDVANFNEMLHKLEFREECYGDVGSHNMYRDYVQFLNYSNITDKSYNHLEKFLKGRGMADVGTIKYHKEGNDTIIDMINFVVVCQGREKWAERAVNVEKTRQILVDYSDYNITLFDYDGTIYDLIITVKGELVKSLAITFTCMTIACFVIMPSFVAPTIASVATVSISFCLIGFLSIWGQNLDPVTMIDVIMAIGFSVDYSAHVCYHYYCAREQHLGSKHEVITSVLQAVGRPVVEASLTTLLCMAPLFVVPVYMIQSFAKTVTLVTSFGLLHGLFFLPVVLYFIPLNAQKHSLPSYTPSTQPLVSLVEDEK
Protein: Putative white-brown complex homolog protein 30 (Putative non-intrinsic ABC protein 12) (WBC-related protein 1) (Q9SJK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- At5g38760 family protein)
- ECA1 gametogenesis related family protein
- ECA1 gametogenesis related family protein
- E3 ubiquitin protein ligase RIE1
- RING-H2 zinc finger protein
- F-box/LRR-repeat protein At1g52650
- RNA-binding
- Putative F-box protein At1g59675
- Calcium-transporting ATPase 1, endoplasmic reticulum-type
- Coatomer subunit zeta-3
Sequence:
MRVRVDVCWTQHIFLFFVFGLSFMSFALSLDGDDYSKTGNPKALVSVTNLIYTRLQNLKTVLKADVDRDLGYCIKNLKGDWNEAFNFDKNLDFLSNCVKKNDGDLTLRLCSAAEIKFYFSSFVRRDEATTVHVKPNINCNLAKWVSGCEPGWSCNADDEKRFDLNNGKILPSRTRKCQPCCEGFFCPQGLACMIPCPLGAYCPLAKLNKTTGFCEPYNYQIPPGKLNHTCGSADSWVDAESSGDMFCSPGSYCPTTIRKVTCSSGHYCRQGSTSQKPCFKLATCNPNTANQNIHAYGAILIASLSLLMIMVYNCSDQVLATREKRQAKSREAAARHAKETTQARERWKTAKGVAKNQKMGLSAQLSQTFSRMKSARKDATPVKASGKSKDKKKEPSNLTKMMKSMEENPSNNEGFNVGTGSKPGKKPQAPKGKQLHTQSQIFKYAYGQIEKEKAMEQNNKNLTFSGVISMATDTEMRTRPVIEVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINSYKKITGFVPQDDVVHGNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLTVYHGSVKKIEEYFADIGITVPDRVNPPDHYIDILEGIVKPDGDITIEQLPVRWMLHNGYPVPHDMLKFCDGLPSSSTGSAQEDSTHNSFSNDLWQDVKTNVEITKDQLQHNYSNSHDNSNRVTPTVGRQYRYFVGRVGKQRLREARLQALDFLILLVAGACLGTLAKVNDETIDTLGYTYTIIAVSLLCKISALRSFSVDKLQYWRESAAGISSLAHFMAKDTMDHLNTIMKPLVYLSMFYFFNNPRSSFEDNYIVLVCLVYCVTGMAYIFAILYSPSAAQLLSVLVPVVMTLIANQDKESMVLKYLGSFCYPKWTLEAFVLSNAQRYSGVWVVTRCSSLSQNGYDLSDWILCLIVLVLMGLICRFIAYFCMVTFQKK
Protein: Cysteine proteinase 7 (EC 3.4.22.-) (Proteinase 1) (Q94504)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Lysosome {ECO:0000305}.
Interaction partners:
- Cathepsin D
Sequence:
MKVLSALCVLLVSVATAKQQLSEVEYRNAFTNWMIAHQRHYSSEEFNGRYNIFKANMDYVNEWNTKGSETVLGLNVFADISNEEYRATYLGTPFDASSLEMTESDKIFDASAQVDWRTQGAVTPIKNQGQCGGCWSFSTTGATEGAQYLANGKKNLVSLSEQNLIDCSGSYGNNGCEGGLMTLAFEYIINNKGIDTESSYPYTAEDGKKCKFNPKNVAAQLSSYVNVTSGSESDLAAKVTQGPTSVAIDASNQSFQLYVSGIYNEPACSSTQLDHGVLAVGFGTGSGSSGSHGGSQSQSAGSDSQSAGSESSQSESGSQSQSESGSQSQSQSGSQSFSGSLYSGSYSGSQSGSQSGNSGAAVKQTGAGSGSGSGSGSGSGSGSGSVSGSASGSASGSASGSSSGSNSNGGVYPTAGDYWIVKNSWGTSWGMDGYILMTKGNNNQCGIATMASRPTAVASL
Protein: Exported repetitive protein (Cell surface protein PirG) (EXP53) (P9WIQ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Surface-exposed protein required for multiplication and intracellular growth.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Possible conserved transmembrane alanine and glycine rich protein
- Conserved hypothetical proline and threonine rich protein
- Diacylglycerol acyltransferase/mycolyltransferase Ag85C
- Possible conserved membrane protein
- Peptidoglycan endopeptidase RipA
- Conserved hypothetical ala-, pro-rich protein
- Probable transmembrane protein
- Uncharacterized protein Rv1417
- Proline-rich 28 kDa antigen
- Possible Inv protein
Sequence:
MPNRRRRKLSTAMSAVAALAVASPCAYFLVYESTETTERPEHHEFKQAAVLTDLPGELMSALSQGLSQFGINIPPVPSLTGSGDASTGLTGPGLTSPGLTSPGLTSPGLTDPALTSPGLTPTLPGSLAAPGTTLAPTPGVGANPALTNPALTSPTGATPGLTSPTGLDPALGGANEIPITTPVGLDPGADGTYPILGDPTLGTIPSSPATTSTGGGGLVNDVMQVANELGASQAIDLLKGVLMPSIMQAVQNGGAAAPAASPPVPPIPAAAAVPPTDPITVPVA
Protein: CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Leukocyte mono-Ig-like receptor 3) (Myeloid-associated immunoglobulin-like receptor 5) (MAIR-5) (MAIR-V) (CD antigen CD300f) (Q6SJQ7)
Organism: Mus musculus (Mouse)
Function: Acts as an inhibitory receptor for myeloid cells and mast cells. Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis. Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide which acts as a ligand. May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2 (By similarity). Inhibits osteoclast formation. Induces macrophage cell death upon engagement.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
Sequence:
MHLSLLVPFLFWITGCCTAEDPVTGPEEVSGQEQGSLTVQCRYTSGWKDYKKYWCQGVPQRSCKTLVETDASEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGLDPMFKVTVNIGPAIQVPITVPTMPPITSTTTIFTVTTTVKETSMFPTLTSYYSDNGHGGGDSGGGEDGVGDGFLDLSVLLPVISAVLLLLLLVASLFAWRMVRRQKKAAGPPSEQAQSLEGDLCYADLSLKQPRTSPGSSWKKGSSMSSSGKDHQEEVEYVTMAPFPREEVSYAALTLAGLGQEPTYGNTGCPITHVPRTGLEEETTEYSSIRRPLPAAMP
Protein: Acyl-CoA binding domain containing 4 isoform 2 (A0A0S2Z5W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTEKESPEPDCQKQFQAAVSVIQNLPKNGSYRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEMKLVAQKVIDTVPLGEVAEDMFGYFEPLYQVIPDMPRPPETFLRRVTGWKEQVVNGDVGAVSEPPCLPKEPAPPSPESHSPRDLDSEVFCDSLEQLEPELQVWTEQRAASGGKRDPRNSPVPPTKKEGLRGSPPGPQELDVWLLGTVRALQESMQEVQARVQSLESMPRPPEQRPQPRPSARPWPLGLPGPALLFFLLWPFVVQWLFRMFRTQKR
Protein: Beta-1 adrenergic receptor (Beta-1 adrenoreceptor) (Beta-1 adrenoceptor) (P34971)
Organism: Mus musculus (Mouse)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity). Involved in the regulation of sleep/wake behaviors.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P18090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early endosome {ECO:0000250}. Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Natriuretic peptides A
- Beta-2 adrenergic receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pro-glucagon
- Guanine nucleotide-binding protein G
- VIP peptides
Sequence:
MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQQWTAGMGLLLALIVLLIVVGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPEPSPSPGPPRPADSLANGRSSKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRDLVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAACRRRAAHGDRPRASGCLARAGPPPSPGAPSDDDDDDAGTTPPARLLEPWTGCNGGTTTVDSDSSLDEPGRQGFSSESKV
Protein: Dysfusion, isoform B (A8JRD4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYADNKRGLDKVTAATPPTHALQQQQQQQHPHQQQQHLQHVLQLQQQQQQHLQQQQHHLQHQMHTHHNFQQHETSPTVSQQQHMQQQQPQTTQQQHATQQQQQQQQQTAGMFTRFDANKSTKGASKMRRDLINAEIANLRDLLPLPQSTRQRLSQLQLMALVCVYVRKANYFQQVFKRHNAMHHLHHQTATPNIGFSKALSGFLMMLTQNGKLLYISDNAAEYLGHSMEDLLIHGDSVYDIIDKQDHANIQAELNRNVPPQPGGSSQASSGGAGGAGGAGDSTSSNGSAAGAGGAGGASSLEGEHRMFLCRMNVSRNARRQMRFGDQKVVLVQGHYLSFLPLCSRNEPVFLATCTPIAMPETRECVVQGATNVFTTIHSMDMKIAHIDKNGEFHLGYDKSTLQGTSWYNLIHSDNLTEAQKKHSLIIQSEQDRSCILLVRMQRSSGEYTWVHVVLQVRDSPDSTQQPVIVCTNQVLNDREASIMLANSWLYHYYTVQSKIQFGMPLDSGIRVPPGTPSSGYYSPHSSHPPATPGGATPNLGIASSFGPHHHPHHSHHPHHHHHHHHPATAYHHHPHMGTYGGVYHAKAAIELKEDQPLFCFQEPVDYSQVNSHVNPPNATSTPNPPISKSSTPPPPKKRARKLEPLYLHAERSPAAAITPEPDCYAIHTHPAAAYATSSVVSSDASVIYATIVPTRPRLPNKSLPPDPADFIEQWNPSPPWSESAQKASLDSFGSSHELSPCITTTPPTPTSATPHQSGLGTTQTIGPAFSFEWMSDPLVPVTYQQWPPTGDHHQHLSQHLSQSQNHQNPLQQQQNEQLLLGQQPHLHQQHQHLALHHGRGEHSLEGESQGVVVVPPIPISIPIPTATGHGDAGEPVEDRDPKN
Protein: Probable Fe(2+)-trafficking protein (P0A8P3)
Organism: Escherichia coli (strain K12)
Function: Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. Necessary to maintain high levels of aconitase under oxidative stress.
Interaction partners:
- Adenine DNA glycosylase
- Membrane-bound lytic murein transglycosylase C
- Iron-sulfur cluster repair protein YtfE
- tRNA-modifying protein YgfZ
Sequence:
MSRTIFCTFLQREAEGQDFQLYPGELGKRIYNEISKEAWAQWQHKQTMLINEKKLNMMNAEHRKLLEQEMVNFLFEGKEVHIEGYTPEDKK
Protein: Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (LACH2) (ACH2) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2) (O88267)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9490035}.
Interaction partners:
Sequence:
MEATLSLEPAGRSCWDEPLSITVRGLVPEQPVTLRAALRDEKGALFRARALYRADAHGELDLARAPALGGSFTGLEPMGLIWAMEPERPFWRLVKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTICYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVEQKSFIPVERSDTTFLFLVGQDDHNWKSEFYANEISKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLGGKSHGVSPKI
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (A8K517)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS
Protein: Rac family small GTPase 2 (A0A8I6G820)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKDIGMMLELREGSWGLEAPGHSLVPALCCVVKLCFPNH
Protein: Phenylcoumaran benzylic ether reductase-like protein (A3F7Q4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAEKSKVLIIGGTGYLGKFIVEASAKEGHPTFVFVRESTVSDPVKGKLVDNFKNLGVHLLLGDMYDHESLVKAIKQVDVVISVVGQMQLADQVKIIAAIKEAGNVKRFFPSEFGMDVDKNNAVEPAKSTFAIKAQIRRAVEAEGIPYTYVPANCFAGYFLPTLSQPGATSPPRDKVVILGDGNPKAVFNHEADIGTYTIKAVDDPRTANKTLFIKPPKNTYSFNELIALWEKLIGKALEKTYVPEDQLLKQIQESPIPINIVLAISHSIFVNGGCTNFEIDPSFGYEASELYPEVKYTTVEEGLSHFV
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (Q57W79)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MKGAQFLKMPCVRVLLVLVRVFFVHLPSFAFGDAFPVNGARGGNSQGYNTDGMHPIQAEMLPYVRDMIDHAFGSYIKYAFPKDELCPVSGTGKNTMGGYGWTLIDSLDTLAIAGFHKEFRRHAKWVEEHLTFDIDESVSVFETTIRALGGLLAAHFMYEEGIVPIIPSEHDYNGGFLRLAVDLADRLMPCFDTPTGIPYGKVNLRSKSKEMWISRSNTAEVGTMLMEMTVLSRITGDEKYERAARRASEALFAARDSQTELMGTYVSVSSGGFSSSESSVAGNIDSVIEYFIKSHSMSGDIGDWERFERTARAVNRYVRKGGMLLAASMYSGRRLQTSQESLSSFFPGNLVLGGHLHEAVESSWPIHTFFKHFGVLPEIFSLESGEPSWISHDYIGRPEHIESLYMLYRATRDPTYLLMGKELALAINLPALSCFFF
Protein: RE23041p (Q8SZ23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLMVVLFALMGITLARPGYDGAATAQWGLRSVPQSGQSGYGSSPSGYGGSASQSGQGGYGGGQGGYGGGQGGYGGGQGGYGGGQGGYGGVQGGYGQPAPLTEQVGYGGTQGGYGSAQKGYGASVPPNEFALGLSGQGRLGGYGNATPQSGKLGYGGGQGGYRRPAPQSGQLYAAGELGAGPQLVQGEFSGGIGHENCNHEHHKHHGHHGRY
Protein: Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)] (P08887)
Organism: Homo sapiens (Human)
Function: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:P22272}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:28060820}.; SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted {ECO:0000269|PubMed:28060820}.
Interaction partners:
- Interleukin-6 receptor subunit beta
- Interleukin-6
- Interleukin-11
- Signal transducer and activator of transcription 3
- Tyrosine-protein kinase JAK1
- Tumor necrosis factor
- Ciliary neurotrophic factor
- Interleukin-1 beta
- Tyrosine-protein kinase JAK2
- Non-receptor tyrosine-protein kinase TYK2
Sequence:
MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR
Protein: Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (Lymphocyte antigen 15) (Ly-15) (CD antigen CD11a) (P24063)
Organism: Mus musculus (Mouse)
Function: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R (By similarity). Integrin ITGAL/ITGB2 is a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Required for generation of common lymphoid progenitor cells in bone marrow, indicating the role in lymphopoiesis. Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20701}; Single-pass type I membrane protein {ECO:0000255}. Note=Upon antigen recognition by the TCR, is recruited to lipid rafts. {ECO:0000250|UniProtKB:P20701}.
Interaction partners:
- Intercellular adhesion molecule 2
- Intercellular adhesion molecule 1
- Integrin beta-2
- Integrin alpha-M
- Junctional adhesion molecule A
- Integrin beta-2-like protein
- Vascular cell adhesion protein 1
- Intercellular adhesion molecule 5
- Integrin beta-1
- Ras association domain-containing protein 5
Sequence:
MSFRIAGPRLLLLGLQLFAKAWSYNLDTRPTQSFLAQAGRHFGYQVLQIEDGVVVGAPGEGDNTGGLYHCRTSSEFCQPVSLHGSNHTSKYLGMTLATDAAKGSLLACDPGLSRTCDQNTYLSGLCYLFPQSLEGPMLQNRPAYQECMKGKVDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSNTSYQFAAVQFSTDCRTEFTFLDYVKQNKNPDVLLGSVQPMFLLTNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGNISAAHDITRYIIGIGKHFVSVQKQKTLHIFASEPVEEFVKILDTFEKLKDLFTDLQRRIYAIEGTNRQDLTSFNMELSSSGISADLSKGHAVVGAVGAKDWAGGFLDLREDLQGATFVGQEPLTSDVRGGYLGYTVAWMTSRSSRPLLAAGAPRYQHVGQVLLFQAPEAGGRWNQTQKIEGTQIGSYFGGELCSVDLDQDGEAELLLIGAPLFFGEQRGGRVFTYQRRQSLFEMVSELQGDPGYPLGRFGAAITALTDINGDRLTDVAVGAPLEEQGAVYIFNGKPGGLSPQPSQRIQGAQVFPGIRWFGRSIHGVKDLGGDRLADVVVGAEGRVVVLSSRPVVDVVTELSFSPEEIPVHEVECSYSAREEQKHGVKLKACFRIKPLTPQFQGRLLANLSYTLQLDGHRMRSRGLFPDGSHELSGNTSITPDKSCLDFHFHFPICIQDLISPINVSLNFSLLEEEGTPRDQKVGRAMQPILRPSIHTVTKEIPFEKNCGEDKKCEANLTLSSPARSGPLRLMSSASLAVEWTLSNSGEDAYWVRLDLDFPRGLSFRKVEMLQPHSRMPVSCEELTEGSSLLTKTLKCNVSSPIFKAGQEVSLQVMFNTLLNSSWEDFVELNGTVHCENENSSLQEDNSAATHIPVLYPVNILTKEQENSTLYISFTPKGPKTQQVQHVYQVRIQPSAYDHNMPTLEALVGVPWPHSEDPITYTWSVQTDPLVTCHSEDLKRPSSEAEQPCLPGVQFRCPIVFRREILIQVTGTVELSKEIKASSTLSLCSSLSVSFNSSKHFHLYGSKASEAQVLVKVDLIHEKEMLHVYVLSGIGGLVLLFLIFLALYKVGFFKRNLKEKMEADGGVPNGSPPEDTDPLAVPGEETKDMGCLEPLRESDKD