wanglab/gogpt-training-data huggingface dataset:
Protein: At5g51220 (Ubiquinol-cytochrome C chaperone family protein) (Q500Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL23m
Sequence:
MLPRLARVVTQTSKLRSLTTNGSMKNLSFFSRYGYATVAPAAADPPSQKDFPSKSPINLDKMFWSKPCSLALPKDSPLRIDEPDYVGIRRFILKMMMFYSKQSMSIRGANVIYKRIIAQVDKPAIYDVFNLEKTFKITYSLLVLHMWLVLRRLKEDGQEGVDLGQYVYEIYNHDVELRVSKAGVNLLLAKWMKELERIFYGNVVAYDAALLPEAKPNDLQIKLWRNVFSDDGTTTPDNTDLKTAQAMARYVRRELGSLSLTDKESIFSGNFSFTPLENKPL
Protein: Small ribosomal subunit protein uS19z (40S ribosomal protein S15-2) (Q9FY66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein uS12z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS24z
Sequence:
MAEVEPDVSAAALAKKRTFKKFSFKGVDLDALLDMPTDDLVELFPSRIRRRMSRGLTRKPMALIKKLRKAKLDAPAGEKPEVVRTHLRNMVIMPEMIGSIIGVYNGKTFNQIEIKPEMIGHYLAEFSITYKPVRHGKPGHGATHSSRFIPLK
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) (Q8IKK7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Enolase
- Glucose-6-phosphate isomerase
- transketolase
- Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase
- L-lactate dehydrogenase
- Deoxyribose-phosphate aldolase, putative
Sequence:
MAVTKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKGGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWGYSNRVLDLAVHITNN
Protein: Histone acetyltransferase MCC1 (EC 2.3.1.48) (Protein MEIOTIC CONTROL OF CROSSOVERS 1) (Q9M8T9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone acetyltransferase that probably regulates acetylation status of histone H3 during meiosis. Histone acetylation may influence recombination and chromosome segregation.
Interaction partners:
- N-terminal acetyltransferase A complex auxiliary subunit NAA15
- N-terminal acetyltransferase A complex catalytic subunit NAA10
- Histone acetyltransferase GCN5
- DNA-binding enhancer protein-like protein
- Cell division cycle 5-like protein
- SAGA-associated factor 29 homolog A
- TATA box-binding protein associated factor RNA polymerase I subunit B
- TATA box-binding protein associated factor RNA polymerase I subunit B-like protein
- SAGA-associated factor 29 homolog B
- TATA box-binding protein-associated factor RNA polymerase I subunit B
Sequence:
MSRFPRRFIDDSSMEDAGISLCPSIHYRPINPNDLDRLEQIHRDIFPIKYESEFFQSVVNGVDIVSWAAVDRSRPDDHSDELIGFVTAKFVLAKDSEIDDLIHYDSSKGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSVCRGVYLHVIAHNNAAICLYKRLMFRCVRRLHGFYLINRHHFDAFLFVYFINGSRTPCSPLEVAMFVVNYMKSGIKSVASKLANKDEKGLKWLFCKDTDCV
Protein: cDNA FLJ46057 fis, clone T1ESE2000609, highly similar to SON protein (Q6ZRV7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATNIEQIFRSFVVSKFREIQQELSSGRNEGQLNGETNTPIEGNQAGDAAASARSLPNEEIVQKIEEVLSGVLDTELRYKPDKAQLLEIAKANAAAMCAKAGVPLPPNLKPAPPPTIEEKVAKKSGGATIEELTEKCKQIAQSKEDDDVIVNKPHVSDEEEEEPPFYHHPFKLSEPKPIFFNLNIAAAKPTPPKSQVTLTKEFPVSSGSQHRKKEADSVYGEWVPVEKNGEENKDDDNVFSSNLPSEPVDISTAMSERALAQKRLSENAFDLEAMSMLNRAQERIDAWAQLNSIPGQFTGSTGVQVLTQEQLANTGAQAWIKKDQFLRAAPVTGGMGAVLMRKMGWREGEGLGKNKEGNKEPILVDFKTDRKGLVAVGERAQKRSGNFSAAMKDLSGKHPVSALMEICNKRRWQPPEFLLVHDSGPDHRKHFLFRVLRNGSPYQPNCMFFLNRY
Protein: TBCC domain-containing protein 1 (F4J4K6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- Auxin-responsive protein SAUR50
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
Sequence:
MTEEQDLIDQSPPPSAPDPEPNSSTNPNSVIHPRRVSFEHGLLPIQKLVFTDPIQTLAPVKQKLADAASNNRVGSAAIADVLQISGDHARLVLETLGSVLHSESDPLVRAKPEEVDSVGADLRDLILFLYIQSYKKLLPRTHKDSAAVADVWPSTSAFDGYLSALSPIQSCNILFPVWYGCSIESFRKQSYNLKLFSVFYSHCSLLVRSNSRRFMPSQADDEAHQLSYLQKHLANIISLLAEPVEGEGDESLVFSMEAFEHLRFLVQFGDKGSDVSPLSQATPFFANSDPDMPAVPVPASQVHDWLLQNIASALESITERISGKENGPSNDQDDAMSDVCAAPNKVAPSTRGPCLIEGVSKTSLVKQASDLRGRSVKVVNCHDSVIYLLAPLRYATVHGCSDTTIVLGAVGKAIKVEHCERVHVIVAAKRVCIANCRECVFFLGVNQRPLIVGDNHKLQVAPYNTFYSHLEEHMREVGLEPTINKWDKPLALGAVDPHDSLSHPAGVADAQAESAASVDPDQFVNFLIPNWFSGAELGSTKDNPFPLPDAYMAAQQRNLKNFEETRRSLKEAPLEENRKRELSSALHVYFKDWLYASGNIRQLYCLQGD
Protein: Presenilin-associated rhomboid-like protein, mitochondrial (EC 3.4.21.105) (Mitochondrial intramembrane-cleaving protease PARL) [Cleaved into: P-beta (Pbeta)] (Q3B8P0)
Organism: Rattus norvegicus (Rat)
Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain (By similarity). Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H300}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H300}.; SUBCELLULAR LOCATION: [P-beta]: Nucleus {ECO:0000250|UniProtKB:Q9H300}. Note=Translocated into the nucleus by an unknown mechanism. {ECO:0000250|UniProtKB:Q9H300}.
Interaction partners:
- Serine/threonine-protein kinase PINK1, mitochondrial
- Stomatin-like protein 2, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- Mitofusin-2
- Metalloendopeptidase OMA1, mitochondrial
- Prohibitin-2
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
- Mitofusin-1
- E3 ubiquitin-protein ligase parkin
- Dynamin-like GTPase OPA1, mitochondrial
Sequence:
MALYSWVQRGWRCGQTWAPLLGGGYRELSATQARQLLGRRFNLLLQQKCGFRKAPRKVEPRRSDTGSSGEAYKRSALIPPLEETVFYPSPYPVRTLLKPFFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGNLRKEINKWWNSLSDGQRTVTGIIAANALVFCLWRVPSLHRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSTSIVNILGQEQFVAVYLSAGVISNFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPVFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYITYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK
Protein: Rho-related protein racF1 (O96390)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Might act in concert and/or share functions with other members of the RHO family in the regulation of a subset of cytoskeletal rearrangements that are required for these processes.
Subcellular location: Membrane; Lipid-anchor.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- Serine/threonine-protein kinase pakB
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Cofilin-1A
- Protein pirA
- Serine/threonine-protein kinase pakC
Sequence:
MQNIKCVVVGDGAVGKTCMLISYTTNGFPSEYIPTVFDNYCANLMLEGKPYSLGLWDTAGQEDYDRLRPLSYPHTDVFLICFSIISQASFENVTTKWFKEVNHHAPGVPIILVGTKQDIRNDNDSIKKLKEKNIELVPYEKGLEKAKEINAIYLEASALTQRGIKDVFDQCIRSVIYPNKLIKKPKKKSCTIM
Protein: Snta1 protein (B5DFL0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Dystrophin
- Dystroglycan 1
- Nitric oxide synthase 1
- Utrophin
- Dystrobrevin
- Caveolin-3
- Sarcoglycan, alpha
- Syntrophin, gamma 2
- Sarcoglycan, delta
- Gamma-sarcoglycan
Sequence:
MASGRRAPRTGLLELRSGAGSGAGGERWQRVLLTLAEDALTVSPADGEPGPEPEPAQLNGAAEPGAASPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQALKKTGKEVVLEVKYMKEVSPYFKNSAGGTSVGWDSPPASPLQRQPSSPGPQPRNLNEAKHVSLKMAYVSRRCTPTDPEPRYLEICAADGQDTLFLRAKDEASARSWAGAIQAQISTFIPWVKDELQALLTATGTAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYCSLPQTREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCNLSVHIDKGFTLWAAEPGATRAVLLRQPFEKLQMSSDDGMSLLFLDFGGAEGEIQLDLHSCPKTMVFIIHSFLSAKVTRLGLLA
Protein: N-terminal acetyltransferase B complex subunit arm1 (NatB complex subunit arm1) (Mitochondrial distribution and morphology protein 20) (Q9Y809)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase A complex catalytic subunit ard1
- Uncharacterized N-acetyltransferase C663.13c
- N-terminal acetyltransferase A complex subunit nat1
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-terminal acetyltransferase A complex subunit-like protein C418.02
- N-alpha-acetyltransferase 40
- Tropomyosin
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
Sequence:
MRRSGSKESTIVYSALSLAQAGRGPEALALLEPLKSTPINSLELLDIIQAVYDDQKKGEESFVFWEKFLQTYGKQEKNLLAYFKASIRIKSLSHQRKAAVELQKNFPSRKHTLWVISSLYLLSKKSENEVEQRLLKALAEKTAKLIFEKPTGYIDSCEEFHLYLDVLLLVGDKDRALDALIHQDADRFVDADADLLLRKLELLASCARWDSLFTFSLSLFQTGNTDWKVCKALLDSASNDDSKLVPLKDCILKALSTSSTKRNLHLLWIEASARFFPEEHESALLGYIKKLYMKPIVFEDLRPYLLKLNVDAQHRLLDAFKLADLGESNESQKVDKLYAEVLLLKIHFLLFESFTAESVVDYVRRCFVAFEKGLSLSKGLLPTDFTHGYEALLLAVHSLIYMWEGNKDLKPAEKQALIFDAICLLEKGITYSQHNFHLKLPLIRLYLLLDGGFPAAAKVYDTMSIKQIQNDTLDHYLLTRATTYYPSSVTSHYINSSLKIYGSNEFETPEMISMAYEDGAYSQIEDMRNFRSRLDHSTWKSISLVERARIHYLTAFKPPKQYLPKCSSPKDNRDLKVFADYGSDKLPTVEESLRNSPKPDTLWIHLTVIGHSLVQDSIVNGDFEKAVLSAKEMEVLCENNDLSKQLTSEEIVHMKLLIQLGLLSVKVKNGDYENSSFETIENLIESFDYENSTPLSQLTKYTEIINDLITCLNSFLYHVSATKKKEFTRQYQLLKNISSNKLGSISGITKHKKKAARKYVSELLSNSWLSNLSETQVPYDPKFAKQVGEGMIDSYIQTTDAVSKLPKFVKF
Protein: Squalene synthase 1 (SQS 1) (SS 1) (EC 2.5.1.21) (FPP:FPP farnesyltransferase 1) (Farnesyl-diphosphate farnesyltransferase 1) (P53799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18236008}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 1
- Squalene epoxidase 4
- Squalene epoxidase 6
- Squalene epoxidase 3
- Squalene epoxidase 5
- Farnesyl pyrophosphate synthase 2
- Hydroxymethylglutaryl-CoA synthase
- Putative sterol 14-demethylase-like protein
- Alpha-barbatene synthase
Sequence:
MGSLGTMLRYPDDIYPLLKMKRAIEKAEKQIPPEPHWGFCYSMLHKVSRSFSLVIQQLNTELRNAVCVFYLVLRALDTVEDDTSIPTDEKVPILIAFHRHIYDTDWHYSCGTKEYKILMDQFHHVSAAFLELEKGYQEAIEEITRRMGAGMAKFICQEVETVDDYDEYCHYVAGLVGLGLSKLFLAAGSEVLTPDWEAISNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPREIWGKYADKLEDLKYEENTNKSVQCLNEMVTNALMHIEDCLKYMVSLRDPSIFRFCAIPQIMAIGTLALCYNNEQVFRGVVKLRRGLTAKVIDRTKTMADVYGAFYDFSCMLKTKVDKNDPNASKTLNRLEAVQKLCRDAGVLQNRKSYVNDKGQPNSVFIIMVVILLAIVFAYLRAN
Protein: Nuclear fallout, isoform H (M9NE94)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MAPMPRIQLPNGNSSIKASTNDFLFAETMSGDSSPTPSSPPSSTGVAKSQCSSLSDGESFEGYGENEYPTQLREARSSNSNGSHNMSNHINNNSNISVGNNSGHNHSGHSNDGNNNLNGSTGVELDLAPHVGSSTPQDDDELNIMPRDNWARRSLRRTPTSNPDSLSQRRWGSMRHSGRRQISSNALASQLYRSSSFNSSGRSSNCDTTEDMYSDISLENRHDYDYRLELLQRKVDDLSDTQNIAEDRTTRTKTEYAVLQARYHMLEEQYRESELRAEERLAEEQKRHREILARVEREASLQNENCQMKIRATEIEATALREEAARLRVLCDKQANDLHRTEEQLELARDQIGVLQQEHEEQAQALRRHEQEKKSTEELMLELGRELQRAREESGARAMPTTSPESIRLEELHQELEEMRQKNRTLEEQNEELQATMLTNQATMLTNGVEQGRHLLNGTLNSLAQELEEMSQAQDSVDSATLASLSQLQQAFQEKEDENVRLKHYIDTILLNIVENYPQLLEVKPMERK
Protein: Iron regulatory protein 1B (SD12606p) (Q9NFX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361275}.
Interaction partners:
Sequence:
MSGANPFAQFEKTFSQAGTTYKYFDLASIDSKYDQLPYSIRVLLESAVRNCDNFHILEKDVQSILGWSPALKQGSNDVEVSFKPARVILQDFTGVPAVVDFAAMRDAVLDLGGDPEKINPICPADLVIDHSVQVDFARAPDALAKNQSLEFERNKERFTFLKWGAKAFNNMLIVPPGSGIVHQVNLEYLARVVFENDATDGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISMLLPEVIGYKLEGKLSPLVTSTDLVLTITKHLRELGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTLGYMKQTNRSEKKIDIIRQYLKATQQLRNYADAAQDPKFTQSITLDLSTVVTSVSGPKRPHDRVSVSDMPEDFKSCLSSPVGFKGFAIAPEAQSAFGEFQWDDGKTYKLHHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEKGLSILPYIKTSLSPGSGVVTYYLKESGVIPYLEKLGFDIVGYGCMTCIGNSGPLEENVVNTIEKNGLVCAGVLSGNRNFEGRIHPNTRANYLASPLLVIAYAIAGRVDIDFEKEPLGVDANGKNVFLQDIWPTRSEIQEVENKHVIPAMFQEVYSKIELGSQDWQTLQVSEGKLFSWSADSTYIKRPPFFEGMTRDLPKLQSIQKARCLLFLGDSVTTDHISPAGSIARTSPAARFLSERNITPRDFNSYGSRRGNDAIMSRGTFANIRLVNKLVEKTGPRTVHIPSQEELDIFDAAERYREEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGVKAVIAESYERIHRSNLVGMGIIPLQFLPGQSAETLNLTGREVYNIALPESGLKPGQKIQVEADGTVFETILRFDTEVDITYYKNGGILNYMIRKMLS
Protein: General transcription factor IIH subunit 2 (AtGTF2H2) (TFIIH basal transcription factor complex p44 subunit) (Atp44) (Q9ZVN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription (By similarity). Can restore UV resistance in the NER-deficient ssl1-1 yeast mutant.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cyclin-H1-1
- General transcription and DNA repair factor IIH subunit TFB4
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH helicase subunit XPD
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
- Transcription initiation factor IIA subunit 2
- General transcription and DNA repair factor IIH subunit TFB1-3
- Transcription initiation factor IIF subunit alpha
- General transcription and DNA repair factor IIH subunit TFB1-1
Sequence:
MSNQRKRSNDEREEEDDEDAEGIGEWERAYVDDRSWEELQEDESGLLRPIDNSAIYHAQYRRRLRMLSAAAAGTRIQKGLIRYLYIVIDFSRAAAEMDFRPSRMAIMAKHVEAFIREFFDQNPLSQIGLVSIKNGVAHTLTDLGGSPETHIKALMGKLEALGDSSLQNALELVHEHLNQVPSYGHREVLILYSALCTCDPGDIMETIQKCKKSKLRCSVIGLSAEMFICKHLCQETGGLYSVAVDEVHLKDLLLEHAPPPPAIAEFAIANLIKMGFPQRAAEGSMAICSCHKEVKIGAGYMCPRCKARVCDLPTECTICGLTLVSSPHLARSYHHLFPIAPFDEVPALSSLNDNRRKLGKSCFGCQQSLIGAGNKPVPCVTCRKCKHYFCLDCDIYIHESLHNCPGCESIHRPKSVSLMEE
Protein: Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A (EC 3.2.1.151) (Glycosyl hydrolase family protein 5A) (BoGH5A) (A7LXT7)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides.
Subcellular location: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MEKQSFSDGLFSPLGIKRVIFMLVLLTTSFISCSNSDEKGGSLEVAQEYRNLEFDARGSRQTIQIDGPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQSLYSVPAYDEYIAPDNTGMRDLTSMQLSALMKAGVNVGNTFEAVIVGNDGSLSGDETCWGNPTPNKVLFEGIKAAGFDVVRIPVAYSHQFEDAATYKIKSAWMDKVEAAVKAALDAGLYVIINIHWEGGWLNHPVDANKEALDERLEAMWKQIALRFRDYDDRLLFAGTNEVNNDDANGAQPTEENYRVQNGFNQVFVNTVRATGGRNHYRHLIVQAYNTDVAKAVAHFTMPLDIVQNRIFLECHYYDPYDFTIMPNDENFKSQWGAAFAGGDVSATGQEGDIEATLSSLNVFINNNVPVIIGEYGPTLRDQLTGEALENHLKSRNDYIEYVVKTCVKNKLVPLYWDAGYTEKLFDRTTGQPHNAASIAAIMKGLN
Protein: Phospholipid-transporting ATPase FetA (EC 7.6.2.1) (ATPase class I type 8B member 2-like protein) (ATPase class I type 8B member 5) (Flippase expressed in testis A) (A3FIN4)
Organism: Mus musculus (Mouse)
Function: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in phospholid transport across membranes and in acrosome formation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:19657017}; Multi-pass membrane protein {ECO:0000269|PubMed:19657017}.
Interaction partners:
Sequence:
MKYVKAFVSEISWDCSWYCSAMQERRNEDRQKEEEERILQANNRRFNSLFEYPDNSIKTSKYGFFNFLPMNLFEQFQRLANAYFLILLFLQLVPQISSLAWYTTVIPLIVVLSITGVKDAIDDVKRHRSDQQINNRSVSILVNGRVEEIKWRNVQVGDIIKLENNHPVTADMLLLSSSEPYGLTYIETADLDGETNLKVKQAISVTSAMEDNLELLSSFNGEVRCDPPNNKLDKFSGTLSYLGNTYLLNHERLLLRGCVIRNTDWCYGLVVYTGQDTKLMQNSGRSTFKRTHIDHLMNVLVVWIFMFLGGMCFLLSIGHGIWENSRGYYFQAFLPWKHYITSSATSSALIFWSYFIVLNTMVPISLYVSVEIIRLGNSYYINWDRKMFYAPKNMPAQARTTTLNEELGQVQYVFSDKTGTLTENVMIFNKCSINGKTYGYSYDDNGEYVPKSPKDKVDFSYNHLADPKFSFYDKTLVEAVKSEDPLVYLFFLCLSLCHTVMSEEKVEGELVYQAQSPDEGALVTATRNFGFVFCSRTPETITVIEMGKIRVYRLLAILDFSNERKRMSVIVRTPEDRVMLFCKGADTIIYELLHPSCASLSEVTMDHLDDFASEGLRTLMVAYRELDKAYFQTWIKKHGEAWLTLENRERKLALVYEEIERDLMLLGATAIEDKLQRGVPETIVTLSKAKIKIWVLTGDKQETAVNIAYSCRIFKDEMDGVFMVEGTDRETVLEELRTARKKMKPESLLESDPINMYLARKPKMPFKSLDEVANGNYGLVISGYSLAYALEGSLEFELLRTACMCKGVVCCRMTPLQKAQVVDLVKRYKKVVTLAIGDGANDISMIKAAHIGVGISNQEGMQATLSSDFSFCQFHFLQRLLLVHGRLSYNRMCKFLSYFFYKNFAFTLVHFWYAFFNGFSAQTVYDIWFITFYNLIYTSLPVLGLSLFEKDVNETWSLCYPELYEPGQHNLYFNKKEFVKCLLHGIYNSFVLFFVPMGTVFNSERNDGKDISDFQSFSLLVQTTLIGVMTMQIALRTTSWTMINHTFTWGSLGLYFCILILLCSDGLCLRYPSIFNFLGVARNSLSQPQIWLCLILSTILCMIPLIGYNFLRPLLWPINADKVLNRIHFCLKHPIPTQVQTKIKHPSLRRSAYAFSHKQGFGALITSGKTLKSSALAKSKRFL
Protein: Apolipophorin-1 (Apolipophorin-I) (apoLp-I) (C0HKF3)
Organism: Galleria mellonella (Greater wax moth)
Function: Constitutes the major component of lipophorin, which mediates transport for various types of lipids in hemolymph. Acts by forming lipoprotein particles that bind lipoproteins and lipids (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:29289504}. Note=Secreted into hemolymph. {ECO:0000269|PubMed:29289504}.
Interaction partners:
Sequence:
SVKSEVDNFDKHLKAESAPFNNE
Protein: KRAB domain-containing protein 4 (KRAB box domain-containing protein 4) (Q5JUW0)
Organism: Homo sapiens (Human)
Interaction partners:
- Carbohydrate sulfotransferase 7
- Sodium/hydrogen exchanger 7
Sequence:
MAMSQESLTFKDVFVDFTLEEWQQLDSAQKNLYRDVMLENYSHLVSVGYLVAKPDVIFRLGPGEESWMADGGTPVRTCAGEDRPEVWQVDEQIDHYKESQDKLPWQAAFIGKETLKDESGQESRTCRKSIYLSTEFDSVRQRLPKYYSWEKAFKTSFKLSWSKWKLCKKER
Protein: Aminopeptidase (EC 3.4.11.-) (A2QIL3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MCGARRGEVTGSTNVPGGREVLPTNVKPLHYDLTLEPNFANFSYDGTVVIDLDVAEDTTSISLNSNEIKIHNAVVSSQGAVVASNPEITLNQDQQVATIKFADTIPAGSSAQLKLTFTGELNDNMAGFYRSSYKAADGQTKYIATTQMEPTDARRAFPCFDEPALKAKFTVTLVADKSMTCLSNMDVASETEVAGGKKAVKFNTSPVMSTYLLAFIVGHLNYIETKAFRVPIRVYATPDQDIEHGRFSLDLAARTLAFYEKAFDNEFPLPKMDMVAVPDFSAGAMENWGLITYRVVDVLLDEKTSGAARKERIAETVQHELAHQWFGNLVTMDFWDGLWLNEGFATWMSWYSCNSFFPEWKVWQTYVIDTLQGALSLDSLRSSHPIEVPVKRADEINQIFDAISYSKGSSVLRMISKYMGEDVFIQGVRDYIKKHAYGNTQTGDLWAALANASGKPVEEVMDIWTKKVGFPVVTVSENPSNSTIKLKQNRFLRTGDVRPDEDTTLYPVMLGLRTKNGIDEDTMLTEREGEFKVPDLDFFKLNADHSAIYRTSYTPERLSKLGEAAKGGLLSVEDRAGMIADAGALAASGFQSTSGLLSLLKGFDSEAEFIVWNEILTRVGSLRAAWLFEDVSTRDALKAFQRSLVSHKAHELGWEFSEKDGHILQQFKALMFGSAGMAEDPVVVKAAQDMFQQFAAGDENAIHPNIRGSVFSIVLKNGGEKEYNVVLDRFRNAPTSDEKTTALRCLGAAEDPALIQRTLDLASGDEVKNQDIYMPLGGLRSHPAGIEARWSWLKNNWDAIYKRLPPSLGMLGTVVQLSTASFCTEEQLKDVQDFFQSKDTKGFDRAVEQSLDSIRAKVNWVKRDRADVESWLKANSYNGKL
Protein: Tryptophan-rich protein TspO (Q81BL7)
Organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
Function: Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX. Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation. May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:25635100}. Membrane {ECO:0000269|PubMed:25635100}; Multi-pass membrane protein {ECO:0000269|PubMed:25635100}.
Interaction partners:
- Deoxyribodipyrimidine photolyase
- Ribonuclease BN
- ATP synthase A chain
- Dehydrogenase.
Sequence:
MFMKKSSIIVFFLTYGLFYVSSVLFPIDRTWYDALEKPSWTPPGMTIGMIWAVLFGLIALSVAIIYNNYGFKPKTFWFLFLLNYIFNQAFSYFQFSQKNLFLATVDCLLVAITTLLLIMFSSNLSKVSAWLLIPYFLWSAFATYLSWTIYSIN
Protein: Ribonucleoside-diphosphate reductase 2 subunit beta (EC 1.17.4.1) (R2F protein) (Ribonucleotide reductase 2) (P37146)
Organism: Escherichia coli (strain K12)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis.
Interaction partners:
- Ribonucleoside-diphosphate reductase 2 subunit alpha
- Protein NrdI
- Glutaredoxin-like protein NrdH
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Thymidylate kinase
- Adenylate kinase
- Cytidylate kinase
- Nucleoside diphosphate kinase
- Pyruvate kinase II
Sequence:
MKLSRISAINWNKISDDKDLEVWNRLTSNFWLPEKVPLSNDIPAWQTLTVVEQQLTMRVFTGLTLLDTLQNVIGAPSLMPDALTPHEEAVLSNISFMEAVHARSYSSIFSTLCQTKDVDAAYAWSEENAPLQRKAQIIQQHYRGDDPLKKKIASVFLESFLFYSGFWLPMYFSSRGKLTNTADLIRLIIRDEAVHGYYIGYKYQKNMEKISLGQREELKSFAFDLLLELYDNELQYTDELYAETPWADDVKAFLCYNANKALMNLGYEPLFPAEMAEVNPAILAALSPNADENHDFFSGSGSSYVMGKAVETEDEDWNF
Protein: Putative GTP-binding protein ara-3 (Rab-type small GTP-binding protein-like) (Ras-related small GTP-binding family protein) (Q9FJF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
Sequence:
MAAPPARARADYDYLIKLLLIGDSGVGKSCLLLRFSDGSFTTSFITTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGILLVYDVTDESSFNNIRNWIRNIEQHASDNVNKILVGNKADMDESKRAVPKSKGQALADEYGIKFFETSAKTNLNVEEVFFSIAKDIKQRLADTDSRAEPATIKISQTDQAAGAGQATQKSACCGS