wanglab/gogpt-training-data huggingface dataset:
Protein: Glycerophosphocholine acyltransferase 1 (GPCAT) (EC 2.3.1.-) (O94673)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Glycerophosphocholine acyltransferase (GPCAT) that utilizes acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming lysophosphatidylcholine (LPC) (By similarity). Shows broad acyl specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA, and the hydroxylated ricinoleoyl-CoA (By similarity). Catalyzes also the acylation of glycero-3-phosphoethanolamine (GPE) with acyl-CoA (By similarity). In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine (LPE) as acyl donors in the acylation of GPC (By similarity). Contributes to the maintenance of phosphatidylcholine (PC) homeostasis and might also have specific functions in acyl editing of PC, such as transferring acyl groups modified at the sn-2 position of PC to the sn-1 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDHLEFDENTDSEYSIFEEDNDYGLHGLDDSVGFTDLFDAPNIYRVYSWLHKHYNQKKGQLKHGVSRQKNKLQPIHKQINYETDKLKERLGKSIDKFQEQWNSGKVVRFRDKLSFALGVSTCILTALLVGMAPESMHLWYTIQLFVYLPLRYYTYQRKGYEYFIADFCYWGNILLLVYIWIFPESRRLFILSYSISYGTLAWSVVAWRNSLLFHSIDKITSLFIHFFPPLVLHTIVHLTNKSYLKDRFPAVLKVKKIDLLSSVEIASFFYALWQIWYYFFIQVGKQKQIQEGRPTSFTWLSKAYSKTKLGRAVAKLPQNLQPFVFMIIQYLYSITTMLPCSLWYNNKLYSTAFLALIFGWSVWNGASYYIDVFGRRFQKELEALRQQLAETPTNSGSSSALSR
Protein: Hydrogenase, putative (Q729F2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Hydrogenase, putative
- Hydrogenase, iron-sulfur cluster-binding subunit, putative
- Rubrerythrin diiron-binding domain-containing protein
- Dihydroorotate dehydrogenase
- Heterodisulfide reductase, A subunit
- Heterodisulfide reductase, B subunit
- Heterodisulfide reductase, C subunit
- Carbamoyl phosphate synthase large chain
- Orotate phosphoribosyltransferase
- Carbamoyl phosphate synthase small chain
Sequence:
MTTLGSGFTDNPYLPDVATVLETVQETPAIKTLRVRIDDAARMDAFRFNPGQVGQLSLFGVGESTFVINSPPTRMDYLQFSIMRAGEVTAALHGLKPGDKVGVRAPLGNWFPFEDMRGKDIVFVGGGIGMAPLRTLLLYMLDNRADYGNITLLYGARTPGDMAFRDDVQDWLGRSDMNTTLTVDQAPDDWPHRAGLIPHVLLDLAPSNANSVAVLCGPPIMIKFTVEALKKLHFADEQIITTLERRMKCGIGICGRCNIGTKYVCVDGPVFSYAELKELPNEL
Protein: Switch-associated protein 70 (SWAP-70) (Q6A028)
Organism: Mus musculus (Mouse)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10382743}. Cell membrane {ECO:0000250|UniProtKB:Q9UH65}. Nucleus {ECO:0000269|PubMed:10382743, ECO:0000269|PubMed:9642267}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9UH65}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UH65}. Note=Localizes predominantly to the nucleus in activated cells. Only a small amount can be detected in the cytoplasm. {ECO:0000269|PubMed:10382743}.
Interaction partners:
Sequence:
MRGLKDELLKAIWHAFTALDLDRSGKVSKSQLKVLSHNLCTVLKVPHDPVALEEHFRDDDEGPVSNQGYMPYLNKFILEKVQDNFDKIEFNRMCWTLCVKKNLTKSPLLITEDDAFKVWVIFNFLSEDKYPLIIVPEEIEYLLKKLTEAMGGGWQQEQFEHYKINFDDNKDGLSAWELIELIGNGQFSKGMDRQTVSMAINEVFNELILDVLKQGYMMKKGHKRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLIKCFDKTFEISASDKKKKQEWIQAIYSTIHLLKLGSPPPHKEARQRRKELRRKLLAEQEELERQMKELQAANENKQQELESVRKKLEEAASRAADEEKKRLQTQVELQTRFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQTTEAEKQELEQQRVMKEQALQEAMAQLEQLELERKQALEQYEGVKKKLEMATHMTKSWKDKVAHHEGLIRLIEPGSKNPHLITNWGPAAFTQAELEEREKSWKEKKTTE
Protein: Polycystin cation channel PKD1/PKD2 domain-containing protein (H2KYJ9)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}.
Interaction partners:
Sequence:
MSRRSTTDRSDFNDNASNASSNASRRPTINFQEIMEDLPHHERETGERLRRHLQFFFMNPMEKWKVRHQLPYKLVLQVLKIVFVTMQLILFAEMRMSHVDFLEDTTTVMRHRFLKEWNDDRDALQYPPAEGRYSVYDDQGLSEHLSFLINSYYSIRNDSFASFSYDVVSHPSGNLGAQISFESIPPIEVLIDRISNVTVNNNTYNFDIREVKDTKRLNLTETEVFQIGQSDDAVRDILATRGITFLPEDALKISTVQFKFRLRTIHYSPTAGDQKPECYKISVSIKFDNSRHTGQVHVTLSTVVSYVNVCNGRIIKGVGWSFDTLLIGGTDIFVLILCILSLILCCRALIKAHLLQIKTSDYFENVLKNKITVTDQLDFLNLWYVMIVVNDALIIIGTVAKISIEFQDFDNSLFTLTSIFLGMGALLVYVGVLRYFGFFSQYNILMLTLKRSAPNIMRFMTCAIVLYAGFLIAGWVIIGPYSMKFRTLAESSEALFSLLNGDDMFATFYTINDSNTVIKVFGTVYIYLFVSLFIYVVLSLFIAIIMDAYEVVKDRYSDGLRAIEKRGCLRDFVESNPPPSELGSPTTRSAYAPSNLLNLAAGNDSSRALRALHAIDNARDWLSSLRDGTRFQSFSNPLNDSNEDVLADQNANGNDPHNSRPSNV
Protein: U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein (U4/U6.U5 snRNP 27 kDa protein) (U4/U6.U5-27K) (Nucleic acid-binding protein RY-1) (U4/U6.U5 tri-snRNP-associated 27 kDa protein) (27K) (U4/U6.U5 tri-snRNP-associated protein 3) (Q8WVK2)
Organism: Homo sapiens (Human)
Function: May play a role in mRNA splicing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 39
- U4/U6.U5 tri-snRNP-associated protein 1
- RNA-binding protein 42
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- U6 snRNA-associated Sm-like protein LSm7
- Small nuclear ribonucleoprotein Sm D3
- U4/U6 small nuclear ribonucleoprotein Prp4
- U5 small nuclear ribonucleoprotein 40 kDa protein
Sequence:
MGRSRSRSPRRERRRSRSTSRERERRRRERSRSRERDRRRSRSRSPHRRRSRSPRRHRSTSPSPSRLKERRDEEKKETKETKSKERQITEEDLEGKTEEEIEMMKLMGFASFDSTKGKKVDGSVNAYAINVSQKRKYRQYMNRKGGFNRPLDFIA
Protein: Ferredoxin-dependent glutamate synthase, chloroplastic (EC 1.4.7.1) (Fd-GOGAT) (SoFdGOGAT) (Q43155)
Organism: Spinacia oleracea (Spinach)
Function: Catalyzes the reductive conversion of 2-oxoglutarate plus glutamine to two molecules of glutamate, using reduced ferredoxin as the electron donor. Contains one FMN but no FAD. The FMN-binding domain is also involved in the delivery of sulfite to the reaction center of SQD1.
Subcellular location: Plastid, chloroplast stroma {ECO:0000255}.
Interaction partners:
Sequence:
MALQSAPKLLYSSPSPSVFSANERRVAFSDFVGLSKKRSRRRRIAGTFRNFPALSAVSSAIKAVVDVDRAHHSTDSGSPTVSTSSHPLDQQVVNLEDILAERGACGVGFIANLDNKGSFQIVKDALTALGCMEHRGGCGSDNDSGDGSGVMTAIPWDLFNDWGKDQGIGPFDRSHTGVGMVFLPKDDLLAEEAKKVVLDTFAQEGIEVIGWRSVPTNVSVVGRNAKETMPNIQQVFVRIIKEDSTDDIERELYICRKLIERAASSHTWASELYFCSLSNQTIIYKGMLRSEVLGMFYYDLQNERYTSPFAIYHRRYSTNTSPRWPLAQPMRFLGHNGEINTIQGNLNWMRSREPSIQSPVWRGRENEIRPYGNPKASDSANLDSAAELLIRSGRTPEEALMILVPEAYKNHPTLMIKYPEAVDFYDYYKGQMETWDGPALLLFSDGKTVGACLDRNGLRPARYWRTVDNVVYVASEVGVLPMDESKVTMKGRLGPGMMISVDLSSGQVYENTEVKKRVASSNPYGKWVKENLRSLKAVNFLSRALLENDTILRNQQAFGYSSEDVQMVIESMASQGKEPTFCMGDDIPLAVMSQKPHMLYDYFKQRFAQVTNPAIDPLREGLVMSLEVNIGKRGNILEVGPENASQVILPSPVLNEGELEALVNDPLLKAQMLPIFFDIRKGVEGTLEKRLNRLCEAADEAVRNGSQMLVLSDRSEELEPTRPAIPILLAVGAVHQHLIQNGLRMYTSIVVDTAQCFSTHQFACLIGYGASAICPYLALETCRQWRLSNKTVNLMRTGKIPTVTIEQAQKNFCKAVKSGLLKILSKMGISLLSSYCGAQIFEIYGLGKDVVDIAFQGSVSKMGGLTLDELARETLSFWVKAFSEDTAKRLENFGFIQFRPGGEYHVNNPEMSKLLHKAVRNKSESAYAVYQQHLANRPVSVLRDLLEFKSDRAPISVGKVEPATSIVERFCTGGMSLGAISRETHEAIAIAMNRLGGKSNSGEGGEDPIRWRPLTDVVDGYSSTLPHLKGLQNGDTATSAIKQVASGRFGVTPTFLVNADQIEIKIAQGAKPGEGGQLPGKKVSAYIARLRNSKPGVPLISPPPHHDIYSIEDLAQLIYDLHQINPKEKVSVKLVAEAGIGTVASGVAKGNADIIQVSGHDGGTGASPISSIKHAGGPWELGLSETHQTLISNGLRERVILRVDGGLKCGVDVMMAAAMGADEYGFGSLAMIATGCVMARICHTNNCPVGVASQREELRARFPGVPGDLVNFFLYVAEEVRGILAQLGFEKLDDIIGRTDILKPRDISLMKTQHLDLSYILASAGLPTMSSTAIRKQEVHTNGPVLDDQILSDPEIIDAIENEKIVNKTVKIFNVDRAVCGRIAGVIAKKYGDTGFAGQLNLTFEGSAGQSFAVFLTPGMNIRLVGESNDYVGKGMAGGELIVTPAENPGFRPEDATIVGNTCLYGATGGQIFVRGKAGERFAVRNSLAEAVVEGTGDHCCEYMTGGCVVILGKVGRNVAAGMTGGLAYILDEDDTLIPKVNKEIVKIQRVTAPVGQMQLKNLIEAHVEKTGSSKGASILKDWDKYLPLFWQLVPPSEEDTPEASAMFEQMTSEGASLQSA
Protein: Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 7 (I3L2H6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADSAQAQKLVYLVTGGCGFLGEHVVRMLLQREPRLGELRVFDQHLGPWLEELKTGPVRVTAIQGDVTQAHEVAAAVAGAHVVIHTAGLVDVFGRASPKTIHEVNVQGTRNVIEACVQTGTRFLVYTSSMEVVGPNTKGHPFYRGNEDTPYEAVHRHPYPCSKALAEWLVLEANGR
Protein: Lipid kinase YegS (EC 2.7.1.-) (P76407)
Organism: Escherichia coli (strain K12)
Function: In vitro phosphorylates phosphatidylglycerol but not diacylglycerol; the in vivo substrate is unknown.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17351295}.
Interaction partners:
- Inner membrane protein YfdC
- Chaperonin GroEL
- Prophage late control protein OgrK
Sequence:
MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKFGVATVIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGDAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGSVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR
Protein: Golgi SNAP receptor complex member 1-2 (Golgi SNARE 12 protein) (AtGOS12) (O22151)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Syntaxin-31
- Membrin-11
- Syntaxin-32
- VAMP-like protein YKT62
- Membrin-12
- VAMP-like protein YKT61
- Bet1-like SNARE 1-1
- Bet1-like SNARE 1-2
- Syntaxin-23
- Syntaxin-21
Sequence:
MTESSLDLQESGWEELRREARKIEGDLDVKLSSYAKLGARFTQGDTDLVMNYEKVLKCVLVSGYVDTGSPTVGSGRSWKSMEMEIQSLLEKLLDINDSMSRCAASAAPTTSVTQKLARHRDILHEYTQEFRRIKGNINSLREHAELLSSVRDDISEYKASGSMSPGVQVLRERASIHGSISHIDDVIGQAQATRAVLGSQRSLFSDVQGKVKNLGDKFPVIRGLLGSIKRKRSRDTLILSAVIAACTLFLIIYWLSK
Protein: Ezrin (Q9UK20)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
GXVAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQX
Protein: Ankyrin-repeat, SH3-domain, and Proline-rich-region containing protein, isoform C (A0A0B4KF17)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKEPTNTLDEIVPSRLTSAELRAMALRQQQQIDSQHQLLATKEQRLRFLKSQEVRSAVASAEGERLRRLRERVEAQESKLRRLRALRGQVDLQKTYNVTLSNDLDSIRALFSEKEKELSLAVAKVEALTRQLEELRRDRRCPVNILTAAGNGVGGQSLPPQASRELEKLRRELMYRNQLSLQQDARLHMQREALQQRQAELRSTDQRIYELQTRLQRKKQANTHHQQQQQQQQQHQQQQHQQQHQQTTVQQQQQQQQQLHVQSAQLLAAAAAATAQQQQQHQQHQQQQQQQQQQSASNLGKHGGVAALKQQLLQKQVNQLAAAAAAAAAGRARGNVAAVEPFIHTPQKSTITSTASYLSGGMKHAAATANTNQQNQLIQDLTHVKLGQNSGFFAGSVPVPVASSSCESDESKLAKKLLAAPAKTEAELRKQAQTEAMDSTTHIYAEVGPKKRDREAAAAAAAAAAAAAAAAQAAAEAANQAATAAAASAISPPATANASKIPKSTTSSSSSASALISKLNQQATAKESQDQQQSQAKKNEISVTSETLSERNTQQQLTVHSMPLGAISKSVALAVSNASKPLQVQVSNVAVPPRKPISSVAPNSVSSGSSIPKMITYSPKVNRVAPNVVMTDPRPALPPKPSKMSPTEQPSPVEANTSGSAGGAGSGAASASTANKTQTATFGLQSLNINDNLPIKAKPLTIRKQPLFEQPRLKSSQSSSNGQQKPPLLQLQNQRKSEPSARQPTENLPDTSPQHSPSSESSADETDRMVAPSITTSQQETSTSATSTTTTVTTSNIKERTGNGKPKLGRRVSFDPLALLLDASLEGELELVKKTAMQVANPSAANDEGITALHNAICAGHIDIVKFLVEFGCDVNAQDSDGWTPLHCAASCNNLSMVKFLVESGACLFASTLSDHETPAEKCEEDEEGFDGCSEYLYSIQEKLGILHNGDVYAVFSYEAQNGDELSFHVNEPLIVLRKGDDAENEWWWARNAAGEEGYVPRNLLGLYPRVPPHSPHFSDXQLIRFTILKRKAGRLIQKRYISKYI
Protein: Armadillo repeat containing 6 (F5H4P3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVSKRIAQETFDAAVRENIEEFAMGPEEAVKEAVEQFESQGVDLSNIVKTAPKVSADGSQEPTHDILQMLSDLQESVASSRPQEVSAYLTRFCDQCKQDKACRFLAAQKGAYPIIFTAWKLATAGDQGLLLQSLNALSVLTDGQPDLLDAQGLQLLVATLTQNADEADLTCSGIRCVRHACLKHEQNRQDLVKAGVLPLLTGAITHHGHHTDVVREACWALRVMTFDDDIRVPFGHAHNHAKMIVQENKGLKVLIEATK
Protein: U1 small nuclear ribonucleoprotein A (U1 snRNP A) (U1-A) (U1A) (Q06AA4)
Organism: Sus scrofa (Pig)
Function: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Sm domain-containing protein.
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein G
- Uncharacterized protein
- Small nuclear ribonucleoprotein Sm D3
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPASKKAVQGGAAAPVVGAVQGPVPGMPPMTQTPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK
Protein: Uncharacterized protein YqiI (P76656)
Organism: Escherichia coli (strain K12)
Function: May be involved in a fimbrial system chaperoned by YqiH and exported by YqiG.
Interaction partners:
- Uncharacterized fimbrial chaperone YqiH
- Inner membrane protein YmfA
- Inner membrane protein YigG
- Uncharacterized protein YhdN
Sequence:
MRYLLIVITFFMGFSSLPAWAMDCYAEHEGGNTVVIGYVPRISIPSDGKKGDKIWQSSEYFMNVFCNNALPGPSPGEEYPSAWANIMMLLASGQDFYNQNSYTFGVTYNGVDYDSTSPLPIAAPVCIDIKGAGTFGNGYKKPAVCSGGPEPQLSVTFPVRVQLYIKLAKNANKVNKKLVLPDEYIALEFKGMSGAGAIEVDKNLTFRIRGLNNIHVLDCFVNVDLEPADGVVDFGKINSRTIKNTSVSETFSVVMTKDPGAACTEQFNILGSFFTTDILSDYSHLDIGNGLLLKIFHNDGTATEFNRFSQFASFSSSSAPSVTAPFRAELSANPAETVVEGPFSKDVILKITYN
Protein: Ribosomal protein S3A (D6RG13)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATG
Protein: H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7) (P51799)
Organism: Rattus norvegicus (Rat)
Function: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH (By similarity). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:16222710, ECO:0000269|PubMed:18449189}; Multi-pass membrane protein {ECO:0000269|PubMed:16222710, ECO:0000269|PubMed:18449189}.
Interaction partners:
- Osteoclastogenesis associated transmembrane protein 1
- V-type proton ATPase subunit a
- Pleckstrin homology domain-containing family M member 1
- Cathepsin K
Sequence:
MANVSKKVSWSGRDRDDEEGAPLLRRTGQPDEETPLLNGAGPGARQSHSALFRIGQMNNVELDDELLDPEVDPPHTFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKDNIDKFTEKGGLSFSLLLWATLNSAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGILGAVFNALNYWLTMFRIRYIHRPCLQVIEAMLVAAVTATVAFVLIYSSRDCQPLQGSSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPMTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISMSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGIIVDVLSDTASNHNGFPVVEDVGDTQPARLQGLILRSQLIVLLKHKVFVERSNMGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNHNQVVGLVTRKDLARYRLGKGGLEELSLAQT
Protein: p-aminobenzoyl-glutamate hydrolase subunit A (EC 3.5.1.-) (PABA-GLU hydrolase) (PGH) (P77357)
Organism: Escherichia coli (strain K12)
Function: Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified.
Interaction partners:
- p-aminobenzoyl-glutamate transport protein
- p-aminobenzoyl-glutamate hydrolase subunit B
- HTH-type transcriptional regulator AbgR
- Methylated-DNA--protein-cysteine methyltransferase
Sequence:
MESLNQFVNSLAPKLSHWRRDFHHYAESGWVEFRTATLVAEELHQLGYSLALGREVVNESSRMGLPDEFTLQREFERARQQGALAQWIAAFEGGFTGIVATLDTGRPGPVMAFRVDMDALDLSEEQDVSHRPYRDGFASCNAGMMHACGHDGHTAIGLGLAHTLKQFESGLHGVIKLIFQPAEEGTRGARAMVDAGVVDDVDYFTAVHIGTGVPAGTVVCGSDNFMATTKFDAHFTGTAAHAGAKPEDGHNALLAAAQATLALHAIAPHSEGASRVNVGVMQAGSGRNVVPASALLKVETRGASDVINQYVFDRAQQAIQGAATMYGVGVETRLMGAATASSPSPQWVAWLQSQAAQVAGVNQAIERVEAPAGSEDATLMMARVQQHQGQASYVVFGTQLAAGHHNEKFDFDEQVLAIAVETLARTALNFPWTRGI
Protein: Protein CROWDED NUCLEI 2 (Protein LITTLE NUCLEI 2) (Q9SAF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape).
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:17873096}; Peripheral membrane protein {ECO:0000269|PubMed:17873096}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Nucleus lamina {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Mostly localized in the nucleoplasm and, to a lesser extent, at the nuclear periphery (PubMed:17873096). During prometaphase to anaphase, localized diffusely in the cytoplasm. A small population is later transferred from the cytoplasm to the chromatin surface. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}.
Interaction partners:
- Protein KAKU4
- SUN domain-containing protein 1
- SUN domain-containing protein 2
- Paramyosin
- WPP domain-interacting tail-anchored protein 1
- WPP domain-interacting tail-anchored protein 2
- Protein NTM1-like 9
- NAC domain-containing protein 68
- Nuclear pore complex protein NUP1
- Nuclear envelope-associated protein 1
Sequence:
MTPRSETHKIGGVTNPRNADRKGKAVAFSDDLVIPTLPPPPIGTLTGQGVSRGHTDDMDMGDWRRFREVGLLNEASMEKKDQEALLEKISTLEKELYGYQHNMGLLLMENKELVSKHEQLNQAFQEAQEILKREQSSHLYALTTVEQREENLRKALGLEKQCVQELEKALREIQEENSKIRLSSEAKLVEANALVASVNGRSSDVENKIYSAESKLAEATRKSSELKLRLKEVETRESVLQQERLSFTKERESYEGTFQKQREYLNEWEKKLQGKEESITEQKRNLNQREEKVNEIEKKLKLKEKELEEWNRKVDLSMSKSKETEEDITKRLEELTTKEKEAHTLQITLLAKENELRAFEEKLIAREGTEIQKLIDDQKEVLGSKMLEFELECEEIRKSLDKELQRKIEELERQKVEIDHSEEKLEKRNQAMNKKFDRVNEKEMDLEAKLKTIKEREKIIQAEEKRLSLEKQQLLSDKESLEDLQQEIEKIRAEMTKKEEMIEEECKSLEIKKEEREEYLRLQSELKSQIEKSRVHEEFLSKEVENLKQEKERFEKEWEILDEKQAVYNKERIRISEEKEKFERFQLLEGERLKKEESALRVQIMQELDDIRLQRESFEANMEHERSALQEKVKLEQSKVIDDLEMMRRNLEIELQERKEQDEKDLLDRMAQFEDKRMAELSDINHQKQALNREMEEMMSKRSALQKESEEIAKHKDKLKEQQVEMHNDISELSTLSINLKKRREVFGRERSRFLAFVQKLKDCGSCGQLVNDFVLSDLQLPSNDEVAILPPIGVLNDLPGSSNASDSCNIKKSLDGDASGSGGSRRPSMSILQKCTSIIFSPSKRVEHGIDTGKPEQRLSSSVAVGMETKGEKPLPVDLRLRPSSSSIPEEDEEYTDSRVQETSEGSQLSEFQSSRRGRGRPRKAKPALNPTSSVKHASLEESSKDELSGHVSVTSKKTTGGGGRKRQHIDDTATGGKRRRQQTVAVLPQTPGQRHYNLRRKKTVDQVPADVEDNAAAGEDDADIAASAPSKDTVEETVVETLRARRIETNADVVSAENNGDVPVANVEPTVNEDTNEDGDEEEDEAQDDDNEENQDDDDDDDGDDDGSPRPGEGSIRKKLWTFLTT
Protein: Plasminogen receptor (KT) (Plg-R(KT)) (Q9HBL7)
Organism: Homo sapiens (Human)
Function: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator-dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metalloproteinase activation, such as of MMP2 and MMP9.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21940822}; Multi-pass membrane protein {ECO:0000269|PubMed:21940822}. Note=Colocalizes on the cell surface with urokinase plasminogen activator surface receptor/PLAUR. {ECO:0000250}.
Interaction partners:
- Plasminogen
- Tissue-type plasminogen activator
Sequence:
MGFIFSKSMNESMKNQKEFMLMNARLQLERQLIMQSEMRERQMAMQIAWSREFLKYFGTFFGLAAISLTAGAIKKKKPAFLVPIVPLSFILTYQYDLGYGTLLERMKGEAEDILETEKSKLQLPRGMITFESIEKARKEQSRFFIDK
Protein: HTH-type transcriptional repressor GlaR (Carbon starvation induced regulator) (GlaH operon repressor) (P37338)
Organism: Escherichia coli (strain K12)
Function: Negatively regulates the expression of the glaH-lhgD-gabDTP operon in a temporal manner during entry into stationary phase or during the first few hours of carbon starvation. Thereby is involved in the regulation of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Binds to two primary and two secondary sites in the promoter region of the glaH operon with the consensus sequences TTGTN5TTTT and ATGTN5TTTT of the primary sites, each separated by six nucleotides.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- L-2-hydroxyglutarate dehydrogenase
- Gamma-aminobutyric acid permease
- 4-aminobutyrate aminotransferase GabT
- Succinate-semialdehyde dehydrogenase [NADP
- Glutarate 2-hydroxylase
Sequence:
MTITSLDGYRWLKNDIIRGNFQPDEKLRMSLLTSRYALGVGPLREALSQLVAERLVTVVNQKGYRVASMSEQELLDIFDARANMEAMLVSLAIARGGDEWEADVLAKAHLLSKLEACDASEKMLDEWDLRHQAFHTAIVAGCGSHYLLQMRERLFDLAARYRFIWLRRTVLSVEMLEDKHDQHQTLTAAVLARDTARASELMRQHLLTPIPIIQQAMAGN
Protein: tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (Transfer RNA methyltransferase 8) (tRNA (guanine(46)-N(7))-methyltransferase) (tRNA(m7G46)-methyltransferase) (Q12009)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055, ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- Multisite-specific tRNA:
- tRNA
- tRNA
- Multifunctional methyltransferase subunit TRM112
- tRNA
- tRNA
- tRNA
Sequence:
MKAKPLSQDPGSKRYAYRINKEENRKELKHVKINESSLVQEGQKIDLPKKRYYRQRAHSNPFSDHQLEYPVSPQDMDWSKLYPYYKNAENGQMTKKVTIADIGCGFGGLMIDLSPAFPEDLILGMEIRVQVTNYVEDRIIALRNNTASKHGFQNINVLRGNAMKFLPNFFEKGQLSKMFFCFPDPHFKQRKHKARIITNTLLSEYAYVLKEGGVVYTITDVKDLHEWMVKHLEEHPLFERLSKEWEENDECVKIMRNATEEGKKVERKKGDKFVACFTRLPTPAIL