wanglab/gogpt-training-data huggingface dataset:
Protein: RHO1 GEF localizing protein 1 (Q12194)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulator of RHO1 signaling that acts as a cofactor required for the efficient localization of the TUS1 GTP exchange factor (GEF) for RHO1 to the bud neck during all phases of cytokinesis. RHO1 is a key, essential hub protein in the cell wall integrity (CWI) pathway in which activated RHO1-GTP binds directly to and activates multiple different downstream effectors required for cell wall synthesis and actin assembly during cytokinesis (Probable).
Interaction partners:
- Rho1 guanine nucleotide exchange factor TUS1
- Inorganic pyrophosphatase
- Uncharacterized protein YPL067C
Sequence:
MTHPVISLKPSYNSVIRGCPGLPDTLPRIECQLRVRSNNSLPFKLVKIEIVLKTIEIYFNKNLYSSNNSSFTPFNRPSDPSNGHSDTSNQNISIHYKKNIVLSHPTHDGDDLNNDLIGIDIPLTIGLPDDIKETNYNPKFGKTQTFLDCTVFYTEVGGGSSNKKRNFLYPVNVERYTYLPSPSYFRPINRSNITSPDQKFLISYSIENPCVSMNNDTLKLSISIRLNPFPNNATTPSSNDFDVSTPTLFSTKKKFKSKLKLKSITTQILEYLEILKNQSEFSSTQTTNILQTSVRQVDQIISMNSMIFQFNLKIFTKDKILQSFRSSESSCPETKVLINKIDDIPLQYHSSITTIGQHFNVSHYLSIRFKFNKSLKNFEINHPLIISFWSVSQLPLIENLILQERQTAKFAKKFYKNFGRIKNTSNNNNSSNCLEYPSLPPIIYNFNDPETNNRFNILYSQKDPSRTDPSKLRRVPVIQ
Protein: Metal binding protein (Q382P1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRGHMAEFVVRQLSGLRVLPSLADVDTSSFPVIGTHNGSFHCDEALACGMLRCSGQFRAANVLRTRDAKTLDRCSIVVDVGGVYDADALRFDHHQPTFHDTMKTPKSMYRTRLSSAGLVYKHFGREIIQRYVEAALSSSYRAELLKMGSWSESRKNLSEAELDTVFDIVYKNFVEHIDGIDNGVNSFGPATETVTASGCSADAQSASCVRNYAVTTTLSDRIGRLMPWWNEGGDGNPESENTAFLQAVELALSEFVAAVHFFTFSWMPARGLVEDAFHAAESVHPSGRIIVLKERFCPWKDHLLEIEAEHGKVGHVLYVLFSDKSGWRVQAVPKDAVSFESRKPLPWKGIRDADLSEASGVEGCVFVHVSGFIGGNKTYEGALQMATKALVAV
Protein: LIM domain 7 (A0A0G2K174)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEGMEDAEADCSVAFAEAQRWVEAVTEKNFETRDFRASLENGVLLCDLINKLKPGVVRKINRLSTPIAGLDNINVFLKACEQIGLKEAQLFHPGDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQNNPYYHGPYLNLKAFETLLGQALTKALEDSSCLKRSGRDSGYGDIWCPDRGDFPAPPGSHRREDSFESLDSLGSRSLTSCSSDLTLRGGREGCESDNDWEFTFKMQDYNKDDMSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKNEDNRRSWASPVYTETEGTFSRLFQKIYGENGSKSLSDVSAEDVQSLRQLRYEEMQKIKSQLKEQDQKWQDDLAKWKDRRKSYTSDLQKKKEEREEIEKQALEKSDRSSKTFREMLQDRESQSSTTTSRRRIYSSDDILDDGVLPPTVTLSETSYQSERLEDKARAHPAEMPKEDSTTFASREDGIAAEIPLASHIPEERRQAPWPSAETRQASSSSAESHQASLPSTESDQARLPSAEPHQASFSSAEPRQVPLVSAEPHQASSFSSTEPHQASLSSALQRPSSLSSSQQSWSTRGESTRISASLPRSYQRSDTARLTSVVTARPFGTSSRGISSLPRSYTMDDGWKYNGDVEVVKREQHDSGRAAGMKPDSSHFILGSSSEKEVATGEDVASLSSFVLPSSSSLSHDQAASSKATFSSTSGLDSVSDSGEGRSSSLREVSRSPDQFSDMRISINQTPGTKHDFGFTIKWDVSGISVASVEKGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEAMANAQETGNLVMDVRRYGKSGSPETKWIDTTSGIYSTEKSSSLSVTTDFSESLQSPYSESKEINGIHEESNAFDSKASESISLKNLKRRSQFFEQGKPAPSRWAWDQEEERRRQERWQKEQDRLLQEKYQREQEKLREEWQRAQQEAERENSKYLDEELMVLNSNSISLTSRESVTASWEPSWSEGSKSLDREGTRAGDEDRGQLEDDAVYEDQSQKLQERLMLEHEKKRKEQEAQEEELRKQREAEAQARAEAEAQARAEAQARAEAQAQAEAEARKRAEAQKLQAERERETSVKIYQYRRPIDSYDLPKREEESSGLLPIDRSKSRSTTELNDPLIEKSGSSKYSDRIGTTSFSQRSSKKDQGPSEAELERQQILQEMRKKTSLHNDNSWIRQRSASVNKEPICLTGIMRRGESLDNLDSQRPGSWRQSSWHSQPAGVYASSSVQDFSRLPPQLLSTSNRAYMRNPSSAVPPLAGSVKTSPGSPSPRSHSPSMSQSGSQLRNRSVSGKRVCSYCNSILGKGAAMIIETLGLCYHLHCFKCVSCERDLGGSSSGAEVRIRNHQLYCNDCYLRFKCFIPIVSLYPSLMIRT
Protein: Sll1130 protein (P73488)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Ssl2245 protein
- Photosystem II CP47 reaction center protein
- Sll1390 protein
- Photosystem II reaction center protein Z
- Photosystem II protein D1 2
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem II CP43 reaction center protein
- Photosystem II extrinsic protein U
- Photosystem II reaction center protein K
- Photosystem II reaction center protein M
Sequence:
MNTIYEQFDVVIVPVPFTDRQSDIRRPALILSDAPAFNNRIGHSVMAMITSAKNAPWPLDTPIEDTRSAGLFTPSVVRMKLFTLEHKYILDCVGSLSKQDRLMVKSAFPHVFKLG
Protein: Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase) (Q9L9C1)
Organism: Aromatoleum evansii (Azoarcus evansii)
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism.
Interaction partners:
Sequence:
MPVKTPSPGDLEPIEKASQDELRALQLERLKWSVRHAYENVPHYRKAFDAKGVHPDDLKSLADLAKFPFTAKGDLRDNYPFGMFAVPREKVARVHASSGTTGKPTVVGYTLKDIDTWATVVARSIRASGGRAGDMVHIAYGYGLFTGGLGAHYGAEKLGCTVVPMSGGQTEKQIQLIQDFKPDIIMVTPSYMLTVLDEMERMGIDPHQTSLKVGIFGAEPWTQAMRAAMEARAGIDAVDIYGLSEVMGPGVANECIEAKDGPVIWEDHFYPEIIDPHTGEVLPDGSEGELVFTTLTKEAMPVIRYRTRDLTRLLPPTARSMRRMAKITGRSDDMLIIRGVNLFPTQVEELICKNPKLAPQYLLEVDKDGHMDTLTVKVEINPEANVGRHPEQKEALAKELQHDIKTFIGVSAKVHVCEPFAIERVTIGKAKRVVDRRPKE
Protein: Eukaryotic translation initiation factor 4H (eIF-4H) (Williams-Beuren syndrome chromosomal region 1 protein) (Q15056)
Organism: Homo sapiens (Human)
Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}.
Interaction partners:
- Eukaryotic initiation factor 4A-I
- Eukaryotic initiation factor 4A-II
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit 3
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 4 gamma 3
Sequence:
MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE
Protein: Trypsin, putative (Q9KSQ6)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Lcl C-terminal domain-containing protein
- Nucleoside diphosphate kinase
- AnkB protein
- Leucine aminopeptidase-related protein
- Chaperone protein DnaK
- Alkaline serine protease
- Decarboxylase, group II
- Heat shock protein 70 family protein
- DnaK-related protein
- DnaK-related protein
Sequence:
MHQVSKLLSCFIGFSLFSTLLYAESTADISSRIINGSNANSAEWPSIVALVKRGADAYQGQFCGGSFLGGRYVLTAAHCFDSRSAASVDVIIGAYDLNNSSQGERIAAQKIYRHLSYSPSNLLNDIAIVELAQTSSLPAITLAGPATRTSLPALTPLTVAGWGITVQSKPPQFTPILQEVDVDLVSQSLCQIVMQHGISSDPNSTNFCAARLTKDSCQGDSGGPIVVKTGREQLGIVSWGDEQCAKTGTYGVYTNVSYFRDWITKHTNQLSYDQVANLGIRPLGKVSQSFTYTNLDANALTYTGNTFSSLPADFSVLSDGCSTKVTLATGESCSVEVAVDAQHYRQYQYDFELIFSYAGGSKRATSRIQLDTSPFAPSASSGGSIGWFGLLLLAPLWMRRKTA
Protein: Oxysterol-binding protein homolog C354.07c (O43021)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSETSEQMEETVQSGNEPISKSTWMGFIKNLATFTGDLSTLSAPSFILSGTSLLEYMSYWFEFPELFVTIVDFPTPKERMLAVLKWYITGLSREYASRNKNYGTEKKPLNPILGELFYGSWDSSKGKVELTAEQVSHHGPESAAHVVCKEAGITVDTHNKYRSGFSGRTVYVNQLGQLRVHLEKYNETYYITLPNISLEGLWFMAPYIELYGSTYIVSNTNYITKIDYSGRGYFRGTKNSFKATIFEKNEDPDYIVEGVWTGESKLTIPSLKSTIFFLSIPSLEATPITVKPESEMGDWESRNVWKEVSAALASGNYDIVSSKKSTIEQSQRDMRKKEEAEGAVWARRYFKWEEHDSDARNALAQAVLEVIEPGFWIYIGDTHPSLPAGEQPVKRME
Protein: Oocyst rupture protein 1, putative (Q8IHQ2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Oocyst rupture protein 2, putative
- Zinc finger protein, putative
Sequence:
MPSILESDNSLNDEENNKTLERSGDINMIEPNNNIMNDNIYRLDEIHCSNNINNEKEVGNIYCDVEKKGDIKYINRISNKNENIEEKSNVLKDTDIDVPYYYNNNSNNGTHHCDNENYEEDNDYINNNETRKNGNDSDIDYGSNFSYTNPDKNCNRSNSFTSNIDKESNDNNVNKKSQHVICLNVQNKDHNNNNNLKEKEYPFFGTIEKNDENVSNKKKISAHENISIYENGSGCMNILIGKNEHSKENKENEKNETNEKNATNETNEKNEKNETNETNETNQTNQTNQTNQTNQTNQTNQTNETNQTNDIVNFDSNKNKPLDEYNHSNIGDCTSVFKNEINGNYNLEQNMDSINNVNGVAILDAEDMNISKDYDNMNILQNYNMMNNDISFEKNLGEKMNDKDDKNSYLEDINNKDNVNNNDNIINNDNINNNDNINNNDNINNNDNINNNDNINNNINNNNNNNNNDDDEIYKPGDDENSNKMYETQFNDSKIKSKISYNDNVDKLDSYNLKDFFIDNNNYNMKEEKYSKESINNINSDEKMNERNFINDKTNKINNSNCNNNKDSDSNYINLINNGNILIDQENYPNDNTKIDELLKNIANGNDAYVKAHEYKRIDLLNTNYKRSIMNNINNNINNNNNNNDNNLNDPFFNYQHMNYANNNNDPSYIYLNKDNMIFDNINKYNVSSNPDYLIKDNEMINFNQMSYINKNIKEENMNHFNEGDFYFDKGKMGSTMGNIENMTNLEFMEYNNIMSSNNKNNNTNKKRRSKKKDSVVKEDIKTENKLYEMKDGNTNRKRRNSYMGDEKRKERKSIIYDNKMVEKNNNDNDNNNNNNINMDNNFIHTNYEYIKNNNNNNNMYIPTNLNNMNYKNYTNYTNDIDNISYMNESLSNNDQHYNMHNLINTNGDNFYAMNNHANNIIMNNMNIGFLKNNINDDKAMEQSEAYLNNISQAYDSHNNNNDNNNNNNNNNNNNNNNNNNNNNNNNNSDNNNNSSSNNNTTNDSTTTNNNTNSSTYNGTQNNTNLSNNNNSNNSNNSFNMSSFFSKGANSNDSQRNYNFSEMNNINESSDYANLSKNTEYDVYDEYVNLGDQKNDDMSDDSNSCDDKGNDKNGDSIDSTDKKKGSKCDSETLLPIANISRIMKRILPGSAKVAKESKDIIRECVTEFIQFLTSEASDRCTREKRKTINGEDILYSMEKLGFNDYIEPLTEYLNKWKQLKELNNSNNYHEKKFDNIKKTEESGDLNNNNNSVENKNLDENAYAEENYPIMNNVYNDQNEIFESNIKNIYTNSNDCDYGNGV
Protein: ATP synthase subunit f, mitochondrial (ATP synthase membrane subunit f) (C9JU26)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MASVVGIFSHSSVSVPVKDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRGYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLKHERLRKYH
Protein: Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Asparagine-linked glycosylation protein 3) (Dol-P-Man-dependent alpha(1-3)-mannosyltransferase) (Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase) (Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase) (Q9Y7I4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38179}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-1,2-mannosyltransferase alg9
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- GDP-Man:Man
- Probable Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannosyltransferase
- Dol-P-Glc:Glc
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
Sequence:
MSSVETRNSFNPFRVLFDLGSYGWLHPSRLLLLEIPFVFAIISKVPYTEIDWIAYMEQVNSFLLGERDYKSLVGCTGPLVYPGGHVFLYTLLYYLTDGGTNIVRAQYIFAFVYWITTAIVGYLFKIVRAPFYIYVLLILSKRLHSIFILRLFNDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMSSLLYVPAYLVLLLQILGPKKTWMHIFVIIIVQILFSIPFLAYFWSYWTQAFDFGRAFDYKWTVNWRFIPRSIFESTSFSTSILFLHVALLVAFTCKHWNKLSRATPFAMVNSMLTLKPLPKLQLATPNFIFTALATSNLIGILCARSLHYQFYAWFAWYSPYLCYQASFPAPIVIGLWMLQEYAWNVFPSTKLSSLIAVCVPLITILKLYTSDYRKP
Protein: Catechol O-methyltransferase domain-containing protein 1 (Q9XXH0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSLVNAYCSEHTTIESELQAELRRATIDSVPMAMILGAPEVFTFGQNFIRSFGGKRVLDIGTFTGASALAWALAVPDGTGEVLTFDINLSDYKKYGVPIISKCKKTFKKIRAIEGPALENLDKLIADGQSGSFDFAFIDADKTNYSKYYDRCVTLLRKGGVIFVDNCLWDGSVCQETTRTDESSVAIHEANEKIFHDDRTYSAILNLGDGTHVAFKK
Protein: Resistin-like gamma (Resistin-like molecule gamma) (RELMgamma) (Ten-cysteine protein 1) (XCP1) (Q8K426)
Organism: Mus musculus (Mouse)
Function: Probable hormone (Probable). Promotes chemotaxis in myeloid cells.
Subcellular location: Secreted {ECO:0000269|PubMed:14733912, ECO:0000269|PubMed:15064728, ECO:0000269|PubMed:15834545}.
Interaction partners:
- Toll-like receptor 4
- Adiponectin
- Leptin
- Adenylyl cyclase-associated protein 1
- Nicotinamide phosphoribosyltransferase
- Insulin-2
- Insulin-1
- Tumor necrosis factor
- Interleukin-6
- Interleukin-1 beta
Sequence:
MLTFNKMKTTTCSLLICISLLQLMVPVNTEGTLESIVEKKVKELLANRDDCPSTVTKTFSCTSITASGRLASCPSGMTVTGCACGYGCGSWDIRDGNTCHCQCSTMDWATARCCQLA
Protein: 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (P17649)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11914276}.
Interaction partners:
- Glutamate decarboxylase
- Succinate-semialdehyde dehydrogenase [NADP
- Transcriptional activator protein UGA3
- Aldehyde dehydrogenase [NAD
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Fatty aldehyde dehydrogenase HFD1
- Aldehyde dehydrogenase [NAD
- NAD-specific glutamate dehydrogenase
- Aldehyde dehydrogenase 5, mitochondrial
- Magnesium-activated aldehyde dehydrogenase, cytosolic
Sequence:
MSICEQYYPEEPTKPTVKTESIPGPESQKQLKELGEVFDTRPAYFLADYEKSLGNYITDVDGNTYLDLYAQISSIALGYNNPALIKAAQSPEMIRALVDRPALGNFPSKDLDKILKQILKSAPKGQDHVWSGLSGADANELAFKAAFIYYRAKQRGYDADFSEKENLSVMDNDAPGAPHLAVLSFKRAFHGRLFASGSTTCSKPIHKLDFPAFHWPHAEYPSYQYPLDENSDANRKEDDHCLAIVEELIKTWSIPVAALIIEPIQSEGGDNHASKYFLQKLRDITLKYNVVYIIDEVQTGVGATGKLWCHEYADIQPPVDLVTFSKKFQSAGYFFHDPKFIPNKPYRQFNTWCGEPARMIIAGAIGQEISDKKLTEQCSRVGDYLFKKLEGLQKKYPENFQNLRGKGRGTFIAWDLPTGEKRDLLLKKLKLNGCNVGGCAVHAVRLRPSLTFEEKHADIFIEALAKSVNEL
Protein: Stanniocalcin (STC) (Corpuscles of Stannius protein) (Q6PHV3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU369112}.
Interaction partners:
- Solute carrier family 12 member 10, tandem duplicate 3.
- P2X purinoceptor
Sequence:
MLLKSGFLLLVVLAACAFCTTQESTQPRRARFSSNTPSDVARCLNGALQVGCATFACLENSTCDTDGMHEICNVFLHTAAVFNTEGKTFVKESIKCMANGITSKVFQTIKRCSTFQKMIAEVQEECYKKLDLCEVARSNPEAIGDVVQVPNTFPNRYYSTLLQSLMECEEDTVEVVRAGLVSRLGPDMATLFQLLQNKPCSSEPAAAEPSGTESQTGFRWPPMFKIQPNMYNRDQTHLFARKRSIVGSP
Protein: RIM-binding protein, isoform L (Q86BP0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPEEAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKRDDRSRW
Protein: Proline-serine-threonine phosphatase interacting protein 2 isoform 3 (Proline-serine-threonine phosphatase interacting protein 2, isoform CRA_a) (A0A0S2Z505)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTRSLFKGNFWSADILSTIGYDNIIQHLNNGRKNCKEFEDFLKESTLKRALEVFKQQVDNVAQCHIQLAQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRKSLEMCSIQRDIEYFVNQRKTGQIPPAPIMYENFYSSQKNAVPAGKATGPNLARRGPLPIPKSSPDDPNYSLVDDYSLLYQ
Protein: Protein SEED AND ROOT HAIR PROTECTIVE PROTEIN (Protein ROOT HAIR SPECIFIC 13) (O81417)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to cell wall structure in root hairs and seeds, especially in phosphate (Pi) deprivation conditions or in the presence of ethylene. Particularly important in maternal tissues (pericarps and seed coats) during seed development, especially under stress conditions. Confers thermotolerance in seed germination rate.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:28138059}.
Interaction partners:
- Peroxidase 73
- At5g05500
- Xyloglucan endotransglucosylase/hydrolase protein 14
- Peroxidase 7
- Expansin-A7
- Putative pectinesterase/pectinesterase inhibitor 24
- Expansin-A18
- Probable pectinesterase/pectinesterase inhibitor 46
- Proline-rich extensin-like family protein
- Peroxidase 44
Sequence:
MAFSRLSFAASLIVFSSLIISSVAYYGNEADPETGKLIPIAVEGIIKCKSGGKTYPIQGATARIACVKVDAYGNELVPISILSSKTDAKGYFIATIFPSQLRAGRTVTKCKTYLYKSPLADCDFPTDVNKGVRGQPLSTYRILQDKSFKLYWAGPFFYTSEPTYY
Protein: MICOS complex subunit Mic27 (Apolipoprotein O-like) (Protein FAM121A) (Q78IK4)
Organism: Mus musculus (Mouse)
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. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol. Plays a crucial role in crista junction formation and mitochondrial function.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6UXV4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6UXV4}. Mitochondrion {ECO:0000250|UniProtKB:Q6UXV4}.
Interaction partners:
- MICOS complex subunit Mic25
- MICOS complex subunit Mic19
- MICOS complex subunit Mic26
- MICOS complex subunit MIC13
- MICOS complex subunit Mic60
- MICOS complex subunit Mic10
- DnaJ homolog subfamily C member 11
- Coiled-coil-helix-coiled-coil-helix domain containing 10
- Metaxin-2
Sequence:
MAAFRMGKLTTIPAGLIYASINVRLAKEEEPKKQLVRPDQLPIYTAPPLHSKYVEEQPGNLQRGFASIRTTTVYYIGWCKSIYLFMKNGVMDTVQFGKDAYVYLKNPPQDFLPKMGVITASGLAGLLSARKGSRFKKIAYPLGLATLGATVCYPAQSVIIAKITGKKAYATSQQIFQAIKSLWTQKSENESLPEPKEESKEGRSDEIHASLPDLKHSVSLPKELASATVIKSESTSGTTQFIPDPKLMDHGQSHPDDKDMYSTRS
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJK7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome I complete sequence
- Arginase
- Glutamyl-tRNA
- Candida glabrata strain CBS138 chromosome L complete sequence
- Pyruvate dehydrogenase E1 component subunit beta
- Glutamine synthetase
- Candida glabrata strain CBS138 chromosome F complete sequence
- 3-hydroxyisobutyryl-CoA hydrolase
- Lactoylglutathione lyase
- [acyl-carrier-protein] S-malonyltransferase
Sequence:
MTATNICPSIGWSIQDWIDFHFKSTPKDSYESLLELVKNQRIAPEDPAWISVATESLLEQQWQLLQSRHEKEKLPLYGVPIAVKDNIDAKGFPTTAACPSFSYMPTRDSTVVELLKQAGAIIIGKTNLDQFATGLVGTRSPYGRTPCVFSDKHVSGGSSAGSASVVARGIVPIALGTDTAGSGRVPAALNNIIGLKPTRGIFSCSGVVPACKSLDCVSVFSMNLSDAEKCLKIMTKLDIENDEYSRSFPANPLQSFNKNLTVAIPKNVMWYGEKENPLLYDRAIDNFKQLGAQIKIIDFEPLLELARCLYEGTWVAERYAATRKFLETSPQQSTLDPVVYGIIKSATKFDAADAFEYEYKRQGILRKVEVLLQDIDVLCVPTCPLNPSFEEVDKEPILVNSRQGTWTNFVNLADLSALAIPVGFRSDGLPNGVTLIAKKFEDYALLQLAKRFLAQLYPSGTRPYGMFLDRYVGLKDDSLEGPIVSSDDSIVLAVVGAHLRGLPLHWQLEKVNATFICSTKTAKKYELYALPKNGPVLKPGLRRITSGTGSQIELELYSVPKEKFGEFISFVPEPLGIGSVELENGKWVKSFICEESGYNSTGSIDISHYGGFRAYIESIIPSNESKKGHFKTVLVANRGEIAVRIIKTLKSMQIKSLAIYSATDKYSQHVLDVDMAQALDGHTVEETYLHVEKIISIAKKYDVDAIIPGYGFLSENASFADRCEQEGIQFIGPRGETIRKLGLKHSAREVAKSAGVPLVPGSPLVKNADEAFTIAKNIGYPVMVKSTAGGGGIGLQKVDNEQDMRKAFETVKHQGSSYFGDSGVFMEKFIDNARHVEVQIMGDGKGKTLALGERDCSLQRRNQKVIEETPAPNLPRETRQKMLTAAERLGAYLNYRGAGTVEFIYDEQRDQFYFLEVNTRLQVEHPITEMVTGLDLVEWMIKISAGVMPSLDEFNISQNGASIEVRVYAENPLKDFRPSPGELVDVQFPNDCRVDTWVKKGTKISPEFDPTLAKIIVHGKDRNEAILKMKKALNETKIYGCVTNVDYLKSLISSEMFRNAQLSTNYLNTYEYSPSAVEIIEPGALTTIQDYPGRVNYWRIGVPPCGPMDNYSFRLANRIVGNDERTPGIEITLTGPTIKFYSDSLVSIAGGEVCCKLDEKKIPMFEPISVKTGSVLSIGKIVKGSRAYLAIRGGIDVPKYMGSFSTFTMGNLGGFNGRALKRGDVLSLPQQFDSEHGIPSPCFSPEKAPIYVRPDIPNDGVWTIGVLAGPHGAPDIFESEGMMEFFKSEWKVHYNSNRFGVRLIGPKPKWSRTDGGEGGLHPSNTHDYVYSLGAINFTGDEPVIITCDGPSLGGFVCQAVVSEAEMWKVGQLKPGDTINFTPIDWQSARNLKENQDVIINDMSSCALQKLSDQPLLKSPEDPILFQKDGQELQSPKVVYRQAGDRYILIEYGDDIFELNLCYRIKSLIDIISQRNTKGIKEMSQGVRSVLVEYDGYEISQKELLKTLIAYEEQLPQEKNWSVKSRIFRLPMAFEDKETLACVKRYQETIRSKAPWLPNNVDFVAEVNNLTHDDIRQLIYTTRYMVLGVGDVFLGSPCAIPLDPRNRLLGSKYNPSRTFTKRGVVGIGGSYMCIYAADSPGGYQLVGRTIPIWDRLMLQSKKDEPWLLSPFDQIEFYPVSEEQIDEYTDEWDNGNYKIDVDDVVFDHGSYLKWVQDNIEAIEEHQRAQRGDNYSKFAQKIQEANADLKQTTTEVIEQNILEDDCEYIFSEYAGRFWKPIVEIGASIEKDQGVAVIEAMKTEMIVSSSVVGKLKKFLFKNGDMVDAGDPVAIIQCL
Protein: Core gene UL1 family protein (Envelope glycoprotein gL) (ORF 47) (ORF47) (Q76RG7)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MGIFALFAVLWTTLLVTSHAYVALPCCAIQASAASTLPLFFAVHSIHFADPNHCNGVCIAKLRSKTGDITVETCVNGFNLRSFLVAVVRRLGSWASQENLRLLWYLQRSLTAYTVGFNATTADSSIHNVNIIIISVGKAMNRTGSVSGSQTRAKSSSRRAHAGQKGK
Protein: Serine endoprotease DegS (EC 3.4.21.107) (Site-1 protease DegS) (S1P protease DegS) (Site-1-type intramembrane protease) (D0ZY51)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and heat shock-induced degradation of RseA but not for acid stress response in this strain.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MFVKLLRSVAIGLIVGAILLAVMPSLRKINPIAVPQFDSTDETPASYNFAVRRAAPAVVNVYNRSMNSTAHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINTKRTPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGLGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQQGSGMDPIQGIVVNEVTPNGPAALAGIQVNDLIISVNNKPAVSALETMDQVAEIRPGSVIPVVVMRDDKQLTFQVTVQEYPASN
Protein: Large ribosomal subunit protein eL33A (60S ribosomal protein L33-A) (L37A) (Q9USX4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS27
- mRNA export factor elf1
- Elongation factor 3
- Small ribosomal subunit protein uS19B
- Large ribosomal subunit protein uL1A
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL29
Sequence:
MPAQGHRLYVKAKHLSFQRSKHVIHPGTSLVKIEGCDSKEEAQFYLGKRICFVYKSNKPVRGSKIRVIWGTVSRPHGNSGVVRARFTHNLPPKTFGASLRVMLYPSNV