wanglab/gogpt-training-data huggingface dataset:
Protein: Polyadenylate-binding protein-interacting protein 1 (PABP-interacting protein 1) (PAIP-1) (Poly(A)-binding protein-interacting protein 1) (Q9H074)
Organism: Homo sapiens (Human)
Function: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Polyadenylate-binding protein 1
- Eukaryotic initiation factor 4A-I
- Eukaryotic initiation factor 4A-II
- Polyadenylate-binding protein 4
- Polyadenylate-binding protein 1-like
- Heterogeneous nuclear ribonucleoprotein Q
- Polyadenylate-binding protein-interacting protein 2
- Polyadenylate-binding protein 3
- Eukaryotic translation initiation factor 4E
- Heterogeneous nuclear ribonucleoprotein D0
Sequence:
MSDGFDRAPGAGRGRSRGLGRGGGGPEGGGFPNGAGPAERARHQPPQPKAPGFLQPPPLRQPRTTPPPGAQCEVPASPQRPSRPGALPEQTRPLRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSVNAPEFYPSGYSSSYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGCVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEVKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDAWKEKGKMDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ
Protein: RE34144p (Ubiquitin conjugating enzyme 7, isoform A (EC 2.3.2.23)) (Ubiquitin conjugating enzyme 7, isoform B) (Q9VXE8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- E3 ubiquitin-protein ligase HRD1
- E1 ubiquitin-activating enzyme
- E2 ubiquitin-conjugating enzyme
- E2 ubiquitin-conjugating enzyme
- Protein TRC8 homolog
- RING-type E3 ubiquitin transferase
- ER membrane protein complex subunit 3
- LP20373p
- ER membrane protein complex subunit 4
- Ubiquitin-conjugating enzyme E2 J2
Sequence:
MAGSALRRLMAEYKQLTLDPPEGIVAGPISEDNFFEWEALIAGPEGTCFEGGVFPARLIFPTDYPLSPPKMKFTCDMFHPNIFADGRVCISILHAPGDDPMGYELSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDAAIMWREQRDEFNAIARRLVRKTLGLPA
Protein: Humanin-like 5 (HN5) (MT-RNR2-like protein 5) (P0CJ72)
Organism: Homo sapiens (Human)
Function: Plays a role as a neuroprotective and antiapoptotic factor.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8IVG9}. Cytoplasm {ECO:0000250|UniProtKB:Q8IVG9}.
Interaction partners:
- Humanin-like 4
- Lipase member N
- Humanin-like 7
- MARVEL domain-containing protein 1
- Humanin-like 6
Sequence:
MATPGFSCLLLSTSEIDLPMKRRV
Protein: Dolabella-3,7-dien-18-ol synthase TPS06 (EC 4.2.3.167) (Terpenoid synthase 6) (AtTPS06) (Q84UU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in terpene biosynthesis in roots. Possesses sesquiterpene (C15) synthase activity and diterpene (C20) synthase activity in vitro. Possesses dolabella-3,7-dien-18-ol synthase activity in vitro. Catalyzes the formation of dolabella-3,7-dien-18-ol from geranylgeranyl diphosphate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Geranylgeranyl pyrophosphate synthase 3, chloroplastic
- Probable alpha,alpha-trehalose-phosphate synthase 7
- Putative inactive
Sequence:
MEAITKYGSYFNVRFLSRLCWRLNLSSSYHYPLLKSSLSFSRFQSPKKLCLVRATTNPTDDNSTTRSFTPHPPSLWGHHFLSASVNQTEMDDLWRQIEALKPIVNAMLLPCNGADAKKITCFIHTLVSLGVSYHFEEKIVEFLKDAFENIEDMIIDCKEDDLYTVSIIFRVFRLYGHYITPDIFNRFKGDDGNFKKCLNDDVRGMLSFYEASHFGTTTEDILEEAMSFTQKHLELFLVGEKAKHYPHITKLIQAALYIPQNFNLEILVAREYIDFYELETDHNEMLLKLAKLNFRFLQLQYIQDLKTLTTWWKELDLVSKIPVYFRERLAEPYFWATGIYYEPQYSAARIMLAKSIILVDIVDNTFDVYGTIDEVKSLVQAIERWDSDAVDVLPDYLKVVFRTTFDLFKELEEYVSSEARSFTMQYAYEQLRILMKGYLQEAEWSNRGHLPSHEEYIEVGVASTAGEVLLAMTFIPMGDAAGVGVYEWLRSRPKLTHALFVKSRLRDDIATYKEEMKRGDVCNGINCYTKQHKVSEEEACIEFEKKTNHMSKVMNEEFLKAAKFIPLHILRPVLNYGRLADVCYKYGDGYTFAGEKIKDYITSLYVDLITL
Protein: 5'-adenylylsulfate reductase 3, chloroplastic (EC 1.8.4.9) (3'-phosphoadenosine-5'-phosphosulfate reductase homolog 26) (PAPS reductase homolog 26) (Prh-26) (Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 3) (APS sulfotransferase 3) (Thioredoxin-independent APS reductase 3) (P92980)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Assimilatory sulfite reductase
- ATP-sulfurylase 3, chloroplastic
- Adenylyl-sulfate kinase 1, chloroplastic
- Adenylyl-sulfate kinase 2, chloroplastic
- ATP sulfurylase 4, chloroplastic
- ATP sulfurylase 1, chloroplastic
- Adenylyl-sulfate kinase 3
- ATP sulfurylase 2
- Adenylyl-sulfate kinase 4, chloroplastic
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
Sequence:
MALAINVSSSSSSAISSSSFPSSDLKVTKIGSLRLLNRTNVSAASLSLSGKRSSVKALNVQSITKESIVASEVTEKLDVVEVEDFEELAKRLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGLHKGNIKENTNGNATANVNGTASVADIFNSENVVNLSRQGIENLMKLENRKEAWIVVLYAPWCPFCQAMEASFDELADKLGGSGVKVAKFRADGDQKDFAKKELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR
Protein: Alkaline phosphatase (ALPase) (EC 3.1.3.1) (PiALP) (P81800)
Organism: Prevotella intermedia
Function: Acts against tyrosine-phosphatases.
Interaction partners:
- Deoxyadenosine kinase
- Putative deoxynucleoside kinase
Sequence:
TDMLAVSVSSTDAIGHKYGT
Protein: Cyclic nucleotide-gated channel beta-1 (Cyclic nucleotide-gated cation channel 4) (CNG channel 4) (CNG-4) (CNG4) (A0A8I5ZN27)
Organism: Rattus norvegicus (Rat)
Subcellular location: [Isoform 2]: Cell projection, cilium membrane {ECO:0000269|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLGWVQRVLPQPPGTPQKTEEGAGPQPETESKPEANPQPEPEVQPEPEPEPEPAPEEAAPEVQTLPPEEPVEGEDVAEAGPSLQETQEADPPQPTSQAQVAVVKVNRPSSWMLSWFWKGMEKVVPQPVYSSSGGQNLAAGEGGPDQDGAQTLEPCGTGDPGSEDGSDKTSKTQDTEPSLWLLRWLELNLEKVLPQPPTPSQAWKVEPEGAVLEPDPPGTPMEVEPTENPSQPNPGPVEPEEEPAAEPQPGFQASSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPSCPGTCDVQTISILPVEQAEHDLVLEDVDSCWEDTQQEDGASLQETELAPIYEDESEAMVEMPRELPQIQEEEEEEKEEKEEKEEEEEKEEEEKREEEKKKEKEEEKKEKEKEEKEEKEEKEEEEKEEKEEEEKEEKEEEEKEEKEEEEEEEEEEEEEEPIVLLDSCLVVQADVDQCQLERAQPETASIQELPEEEEEKEEEKKEEEEEKEEEEEKEEEEEKEEEGEATNSTVPATKEHPELQVEDTDAEAGPLIPEETIPPPERPPVSPAKSDTLAVPGAATHRKKLPSQDDEAEELKALSPAESPVVAWSDPTTPQEADGEDRAASTASQNSAIINDRLQELVKMFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPDSAPAQKPAEAEAAEEEHYCDMLCCKFKRRPWKMYQFPQSIDPLTNLMYILWLFFVVLAWNWNCWLIPVRWAFPYQRADNIHLWLLMDYLCDFIYLLDITVFQMRLQFVKGGDIITDKKEMRNNYLKSQRFKMDLLCLLPLDFLYLKLGVNPLLRLPRCLKYMAFFEFNNRLEAILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAFQGIGSTHWVYDGVGNSYIRCYYWAVKTLITIGGLPDPQTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPRSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYNIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKAVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRNNNKPKEEKSVLILPPRAGTPKLFNAALAAAGKMGPRGAKGGKLAHLRARLKELAALEAAARQQQLLEQAKSSQEAGGEEGSGATDQPAPQEPSEPKEPPEPPAPSSPPPASAKPEGSTEEAAGPPEPSVRIRVSPGPDPGEQTLSVEMLEEKKEEVE
Protein: E3 SUMO-protein ligase TRIM60 (RING finger protein 33) (Q8VI40)
Organism: Mus musculus (Mouse)
Interaction partners:
- Kinesin-like protein KIF3B
- Kinesin-like protein KIF3A
Sequence:
MDSTALKILQDKCICYICSDFMEDPVTSRCGHNFCFACLRLLWDDLQGNIFCPVCQTPFPPKSFSRNYQFRNMTETIRLLQKRQSKRKRQEEHTVCPKHDQPLVLFCVRDRDVLCTQCSLSVEHQGHYTCPIKKASSYHRKVLESAIATLKFGVKQVEEKLAVQHRRVLGLREEAQYQKIEIRYEIGQIKLFLQSEYEAHLNESHMEELRSFSELNGYLETLLDHVSTAKDLLKEVEAIHERSDVTLLRAYHKLQNLKSPKPWLFRTKQYGLSLPAQYSGLSRIIKQFQADVTFDRDTAHPQLVISEDRKSVFYKEAWPCVCASPQKFHLWPALLGCKGFDSGRQYWEVKVGDKPRWTLGVCQAHFSGDWSNQSSGFWAIGRYAENSYVTYGPLRTEFLPVVRPSKVGIFLDYELGELSFYNMNDRSLLYTFRNSFTSTLWPYFYIGTDSESLEILTHPTPDTGSY
Protein: Protein FlxA (P77609)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YnjH
- Uncharacterized protein YdfR
- Flagellar brake protein YcgR
- Flagellar secretion chaperone FliS
- Negative regulator of flagellin synthesis
- Flagellar hook-associated protein 3
- Flagellar hook-associated protein 2
- Flagella synthesis protein FlgN
- Methyl-accepting chemotaxis protein II
Sequence:
MSVTIQGNTSTVISNNSAPEGTSEIAKITRQIQVLTEKLGKISSEEGMTTQQKKEMAALVQKQIESLWAQLEQLLRQQAEKKNEDATVQPDKKEEKKDDTNTAGTIDIYV
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (A0A1D8PK87)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU361143}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU361143}.
Interaction partners:
- Protein transport protein SEC61 subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit delta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Translocon subunit
- Mannosyl-oligosaccharide glucosidase
- Protein transport protein Sec61 subunit beta
Sequence:
MWKFFITLGVIFSICSAQLLDTVSFDSNWENLHYIRNVDLNKGFVKETDLIEIKNINSKPQDEYYFTINDGFDSVNELSVFSAFLNDNLLEVKVDEIVANKVFKLKLPVPIAPNSNVELKINYVYIDTLVPIPTKISMDAVQQLLFKTNKFPYSPYLTKEYTLSLTGMSKGQEMQLHIDVNATEGTPDLKPRVDNQTLKYGPIAEDIQAFTLSPMGLLYDHNRPVTKAVNLNRSIWLPASDVNKVSIEEYYELTHVGAALDSGFSRIDWMKGRYEGTRNHWALSHLELPLLDRDLDGYYYTDKVGVVSSHKVVKNHLLLSPRYPLFGGWNYNFTFGWSEDLSRFLHKLHDTSDEYIIKFPILNSLRDVTYGDVYLEFYLPENAEFQNVSSPIPFESITIDNELSYLDVSKGHTKVTVHYKNLFDDLHKLDVFVKYKYTKINFVYKIVRISGFVFIGLISYYLLGLLDLSI
Protein: Protein E6 (P24835)
Organism: Human papillomavirus 39
Function: This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MARFHNPAERPYKLPDLCTTLDTTLQDITIACVYCRRPLQQTEVYEFAFSDLYVVYRDGEPLAACQSCIKFYAKIRELRYYSDSVYATTLENITNTKLYNLLIRCMCCLKPLCPAEKLRHLNSKRRFHKIAGSYTGQCRRCWTTKREDRRLTRRETQV
Protein: Superkiller protein 7 (Q08491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Represses the expression of non-poly(A) mRNAs like L-A or M viruses and is therefore involved in antiviral system. Mediates interactions via its N-terminus between the exosome and the SKI complex which operate in the 3'-to-5' mRNA-decay pathway. By interacting with NAM7, is also required for nonsense-mediated 3'-to-5' mRNA-decay (NMD). May recognize a stalled 80S ribosome at the 3'-end of a nonstop mRNA which leads to the recruitment of the exosome and SKI complexes to the mRNAs to be degraded.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11532933, ECO:0000269|PubMed:12730603}.
Interaction partners:
- Exosome complex component MTR3
- Exosome complex component RRP45
- Exosome complex component SKI6
- Exosome complex component RRP43
- Exosome complex component RRP4
- Exosome complex component CSL4
- Exosome complex exonuclease RRP6
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
- Exosome complex component RRP46
Sequence:
MSLLEQLARKRIEKSKGLLSADQSHSTSKSASLLERLHKNRETKDNNAETKRKDLKTLLAKDKVKRSDFTPNQHSVSLSLKLSALKKSNSDLEKQGKSVTLDSKENELPTKRKSPDDKLNLEESWKAIKEMNHYCFLKNDPCINQTDDFAFTNFIIKDKKNSLSTSIPLSSQNSSFLSLKKHNNELLGIFVPCNLPKTTRKVAIENFNRPSPDDIIQSAQLNAFNEKLENLNIKSVPKAEKKEPINLQTPPTESIDIHSFIATHPLNLTCLFLGDTNAGKSTLLGHLLYDLNEISMSSMRELQKKSSNLDPSSSNSFKVILDNTKTERENGFSMFKKVIQVENDLLPPSSTLTLIDTPGSIKYFNKETLNSILTFDPEVYVLVIDCNYDSWEKSLDGPNNQIYEILKVISYLNKNSACKKHLIILLNKADLISWDKHRLEMIQSELNYVLKENFQWTDAEFQFIPCSGLLGSNLNKTENITKSKYKSEFDSINYVPEWYEGPTFFSQLYLLVEHNMNKIETTLEEPFVGTILQSSVLQPIAEINYVSLKVLINSGYIQSGQTIEIHTQYEDFHYYGIVSRMKNSKQILETNTKNNISVGLNPDILEVLVKIHNTEDFTKKQFHIRKGDIIIHSRKTNTLSPNLPNTLKLLALRLIKLSIQTHALSDPVDLGSELLLYHNLTHNAVKLVKILGTNDISINPNQSLIVEVEIIEPDFALNVIDSKYITNNIVLTSIDHKVIAVGRIACQ
Protein: Histone H2B type 1-H (H2B-clustered histone 9) (Histone H2B.j) (H2B/j) (Q93079)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A type 1-C
- Histone H2A type 1-D
- Histone H4
- Histone H3.2
- Histone H3-like centromeric protein A
- Histone H2B type 1-D
- Histone H2B type 1-C/E/F/G/I
- Histone H2A.J
- Histone H2B type 1-O
- Centromere protein N
Sequence:
MPDPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Amino acid permease, putative (O07192)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSKLSTAARRLLIGRPFRSDRLSHTLLPKRIALPVFASDAMSSIAYAPEEIFLVLSVAGLAAYSMAPLIGLAVAAVLLVVVSSYRQNVHAYPSGGGDYEVVTTNLGATGGLVVASALMVDYVLTVAVSISSAASNIGSVSPFVYEHKVLFAVGAIVLIMAMNLRGVRESGLAFAIPTYAFIAGIGTMLVWGLFRIFVLGNPVRAESAAFEMHAEHGQIVGFALVFLVARSFSSGCAALTGVEAISNGVPAFQKPKSRNAATTLLMLGIIAVSMFMGMIVLAVETGVQVVDDPDTQLTGAPPGYQQKTLVAQLAQAVFGGFYLGFLLIAAVTALILVLAANTAFNGFPVLGSVLAQHSYLPRQLHTRGDRLAFSNGILFLAAAAIGAVVAFRAELTALIQLYIVGVFISFTMSQVGMVRHWTRLLSAETDPRARRAMLRSRAVNTVGFVSTGTVLLIVLVTKFLAGAWIAIVAMGGFFMMMKLIHRHYDAVNRELAEQAEEAEITLPSRNHAVVLVSKLHLPTLRALTYARATRPDVLEAVTVNVDDAETRELVRQWQDSDVSVPLKVIASPYREITRPVLDYVKRVSKESPRTVVTVFIPEYVVGRWWEQLLHNQSALRLKGRLLFMPGVMVTSVPWQLTSSERIKTLQPHAAPGDT
Protein: DNA 5'-3' helicase (EC 5.6.2.3) (Q6TY68)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
AELQNLMVYYERHCPNPPPFTGLVLSSRKNMCIHPEVSKEREGKAVDGKCYGLTASYIRERHEMDTETPICQYFEGFSLEGKESTLPVGVYSIDDLKEYGRSRNWCPYFLARYAIAHAHIVVYSYHYLLDPKIAQVVSKEMSRESCVVFDEAHNIDNVCIDSMSVKINRRTVERSTNALNHLTKLVQDIREEDTNRLNEEYQRMVQGLKDASVQRDTDMILANPVLPNDVLTEVVPGNIRNADHFLSFLRRFIEYIKTRLRVHHVVQESPAGFLKDISSKICIERKPLRFCAERLSSLLRTLEISDLTEYGALTLITHFATLVSTYTKGFTIIIEPFDDKTPTVSNPILHFSCLDSSIAMAPVFSRFQTVVITSGTLSPMDMYPKILDFDPVVMSSFTMTLARPCLLPMIVSKGNDQVTISSKFETREDTAVIRNYGQLLVEVAKTVPDGIVCFFTSYLYLESVVASWYDQGIVDTLLRYKLLFIETQDNAETSYALMNYVKACDCGRGAVLLAVARGKVSEGVDFDHHYGRAVLMFGIPYVYTQSRILKARLDYLRDQFQIRENDFLTFDAMRHAAQCVGRALRGKTDYGIMIFADKRFSRHDKRSRLPKWIQEHLVDSFCNLSTEEAVQLARRWLRRMAQPFTREDQLGISLLTLAQLENMEQEKLERQAXGKQGVGGEVQEL
Protein: PelF (Q9HZE9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PelG
- PelD
- PelE
- PelC
- PelA
- PelB
- PslD
- PslA
- GDP-mannose 6-dehydrogenase
- Mannuronan synthase
Sequence:
MTEHTAPTAPVADVCLLLEGTWPYVRGGVSSWVNQLILGLPDLTFSVFFIGGQKDAYGKRHYPIPDNVLHIEEHFLETAWSSPNPQTRQGSSETEKALRDLHRFFHYPETPDVEEGDALLDLLAEGRIGREDFLHSKASWEAITAGYERYCTDPSFVNYFWTLRSMQAPVFMLAEAARRMPRARMLHSISTGYAGLLGCILQRRWGCRYLLSEHGIYTKERKIDLAQANWIAENPDEQLSTGLDAEVSYIRRLWIRFFERVGLLTYRAANPIVALYEGNRQRQVLDGAEPRRTRVIPNGIDLDAWTGALERRPPGIPPVVGLVGRVVPIKDVKTFIRAMRGVVSAMPEAEGWIVGPEEEDPDYASECRSLVASLGLQDKVKFLGFRRIGEVLPQLGLMVLTSISEAQPLVILEAWAAGAPVVSSDVGSCRELIEGADAEDRALGRAGEVVAIADPQATSRAILALLRNPQRWQAAQAVGLQRVERYYTEALMLGRYRGLYREATEIA
Protein: Class-E vacuolar protein-sorting protein 24 (Vps24p), putative (Q383S9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Charged multivesicular body protein 6
- ESCRT-II complex subunit VPS22
- SNF-7-like protein, putative
- Vacuolar protein sorting-associated protein 28 homolog
- Uncharacterized protein
- Dolicholphosphate-mannose synthase
- Vacuolar protein-sorting-associated protein 36
- SB domain-containing protein
Sequence:
MFSGWFKRVPPEEKAKEWRRQLNSEMRKLDLQIRKIQREEMKVKQTARQAAKKGDTVVLRMLAKEIIHSRKAVRRLHTARTQMNSVSMQLQQQVSQIKLAGRIEASAVVMTQMNQLMHIREVRESIQSLGREMTKAGLIEEMMNDTIDDVLDGDISDTELEDEVEKVVVEVTQGKMEGTVVGTSRLPEVQQEQEVENEGELESDDELVARLNMLRGTVS
Protein: Sec1 family domain-containing protein 1 (SLY1 homolog) (Sly1p) (Syntaxin-binding protein 1-like 2) (Q8WVM8)
Organism: Homo sapiens (Human)
Function: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Golgi SNAP receptor complex member 1
- BET1 homolog
- Syntaxin-5
- Golgi SNAP receptor complex member 2
- Syntaxin-18
- Vesicle-trafficking protein SEC22b
- Synaptobrevin homolog YKT6
- Alpha-soluble NSF attachment protein
- General vesicular transport factor p115
- Vesicle-fusing ATPase
Sequence:
MAAAAAATAAAAASIRERQTVALKRMLNFNVPHIKNSTGEPVWKVLIYDRFGQDIISPLLSVKELRDMGITLHLLLHSDRDPIPDVPAVYFVMPTEENIDRMCQDLRNQLYESYYLNFISAISRSKLEDIANAALAASAVTQVAKVFDQYLNFITLEDDMFVLCNQNKELVSYRAINRPDITDTEMETVMDTIVDSLFCFFVTLGAVPIIRCSRGTAAEMVAVKLDKKLRENLRDARNSLFTGDTLGAGQFSFQRPLLVLVDRNIDLATPLHHTWTYQALVHDVLDFHLNRVNLEESSGVENSPAGARPKRKNKKSYDLTPVDKFWQKHKGSPFPEVAESVQQELESYRAQEDEVKRLKSIMGLEGEDEGAISMLSDNTAKLTSAVSSLPELLEKKRLIDLHTNVATAVLEHIKARKLDVYFEYEEKIMSKTTLDKSLLDIISDPDAGTPEDKMRLFLIYYISTQQAPSEADLEQYKKALTDAGCNLNPLQYIKQWKAFTKMASAPASYGSTTTKPMGLLSRVMNTGSQFVMEGVKNLVLKQQNLPVTRILDNLMEMKSNPETDDYRYFDPKMLRGNDSSVPRNKNPFQEAIVFVVGGGNYIEYQNLVDYIKGKQGKHILYGCSELFNATQFIKQLSQLGQK
Protein: Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Lipoyltransferase 2) (EC 2.3.1.181) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) (A6NK58)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes, which catalyze essential redox reactions. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28628643, ECO:0000269|PubMed:28757203}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Acyl carrier protein, mitochondrial
- Fatty acid synthase
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Glycine cleavage system H protein
- Ecto-ADP-ribosyltransferase 3
Sequence:
MRQPAVRLVRLGRVPYAELLGLQDRWLRRLQAEPGIEAPSGTEAGALLLCEPAGPVYTAGLRGGLTPEETARLRALGAEVRVTGRGGLATFHGPGQLLCHPVLDLRRLGLRLRMHVASLEACAVRLCELQGLQDARARPPPYTGVWLDDRKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSKELQRHVTVEEVMPPFLVAFKEIYKCTLISEDSPN
Protein: Serine and arginine repetitive matrix 1 (A9Z1X7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDAGFFRGTSAEQDNRFSNKQKKLLKQLKFAECLEKKVDMSKVNLEVIKPWITKRVTEILGFEDDVVIEFIFNQLEVKNPDSKMMQINLTGFLNGKNAREFMGELWPLLLSAQENIAGIPSAFLELKKEEIKQRQIEQEKLASMKKQDEDKDKRDKEEKESSREKRERSRSPRRRKSRSPSPRRRSSPVRRERKRSHSRSPRHRTKSRSPSPAPEKKEKTPELPEPSVKVKEPSVQEATSTSDILKVPKPEPIPEPKEPSPEKNSKKEKEKEKTRPRSRSRSKSRSRTRSRSPSHTRPRRRHRSRSRRRPSPRRRPSPRRRTPPRRMPPPPRHRRSRSPVRRRRRSSASLSGSSSSSSSSRSRSPPKKPPKRTSSPPRKTRRLSPSASPPRRRHRPSPPATPPPKTRHSPTPQQSNRTRKSRVSVSPGRTSGKVTKHKGTEKRESPSPAPKPRKVELSESEEDKGGKMAAADSVQQRRQYRRQNQQSSSDSGSSSSSEDERPKRSHVKNGEVGRRRRHSPSRSASPSPRKRQKETSPRMQMGKRWQSPVTKSGRRRRSPSPPPTRRRRSPSPAPPPRRRRTPTPPPRRRTPSPPPRRRSPSPRRYSPPIQRRYSPSPPPKRRTASPPPPPKRRASPSPPPKRRVSHSPPPKQRSSPVTKRRSPSLSSKHRKGSSPSRSTREARSPQPNKRHSPSPRPRAPQTSSSPPPVRRGASSSPQRRQSPSPSTRPIRRVSRTPEPKKIKKAASPSPQSVRRVSSSRSVSGSPEPAAKKPPAPPSPVQSQSPSTNWSPAVPVKKAKSPTPSPSPPRNSDQEGGGKKKKKKKDKKHKKDKKHKKHKKHKKEKAVAAAAAAAVTPAAIAAATTTLAQEEPVAAPEPKKETESEAEDNLDDLEKHLREKALRSMRKAQVSPQS
Protein: C2H2-type domain-containing protein (O45950)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein lin-56
- Protein lin-8
- Protein lin-15A
- Myb_DNA-bind_3 domain-containing protein
Sequence:
MSLQTIEEMDAYPAVDDSGDHLLDPNMIPTAATEVVMSGDGIERQFGDEEDTYQYEYTYEDDPQLEIGEEEVVVTDEAEYQEHWKDEEKKMNLYDVLGSKMYLEDDEKGGPKRSRIDDDEASFSDVYHHHQPPPPPHPRAGAPGDYRYAVDDYREYTVYPTSGGPKQQHGGAHNSVDRTCQGCGMMLRRSVFYHHARMIREKGACNLFTPQRFPCTQCDARIGTLEKLCQHMEQIHQAPTQIKTMVFTNEEDFKQFRIELEGKGGNFRMARGNKKNKKGMVQYFRCNRLQTLSRSQTFRPVDNPSLEELPTNRKRGRLHQQELRQQSAKQVIRTENSCTAFYNKAYLDNGTIEVRFCDHHLHDDEKLRLPEAVRARVIELARKNLPHVVILMIVKDERFKYCERNSANDRRIQDMKTQDIRQVLAGNNRSVKTRISRGEQVEQFDRFAHLGHVDEDPTRPWNDVRPSAKVDRLSLSHSELRYLDLFDTNREEIMAKLNERSRVEQSKKMLYDSFIHRLSSSNEVIKQIDYRDLIPNESTLLKLKKAYNYLAKIENELLNPRREQINPIRVTSYIRMMEEEARLIERTRQAASAPGAAAGDEIDVVGIDEEDYHHHHHMDLHEVVEEEEVGYHQEDLELEQELQEHVEEDYLPVEEELVEEELVVEEEALPVEQHQEEEEDGEPTVTRAGRVVKKKPQFDS
Protein: Linoleate 13S-lipoxygenase 3-1, chloroplastic (EC 1.13.11.12) (O24371)
Organism: Solanum tuberosum (Potato)
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids.
Subcellular location: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid.
Interaction partners:
- Fatty acid hydroperoxide lyase
- phospholipase A2
- Triacylglycerol lipase SDP1
- Sugar-dependent1
- Allene oxide synthase 2
- Allene oxide synthase
- Alpha-DOX1
- Alpha-DOX2
- Alpha-DOX2
- 12-oxophytodienoate reductase
Sequence:
MALAKEIMGISLLEKSSSFMNSSSMALFNPNNYHKENHLWFNQQFQGRRNLSRRKAFRQSTMAAISENLIKVVPEKAVRFKVRAVVTVRNKNKEDLKETIVKHLDAFTDKIGRNVTLELISTDMDPNTKGPKKSNQAVLKDWSKKSNLKTERVNYTAEFIVDSNFGNPGAITVTNKHQQEFFLESITIEGFACGPVHFPCNSWVQPKKDHPGKRIFFSNQPYLPDETPAGLKSLRERELRDLRGDGKGVRKLSDRIYDYDIYNDLGNPDKGIDFARPKLGGDDNVPYPRRCRSGRVPTDTDISAESRVEKPNPTYVPRDEQFEESKMNTFSTSRLKAVLHNLIPSLMASISSNNHDFKGFSDIDNLYSKGLLLKLGLQDEVLKKLPLPKVVSSIKEGDLLKYDTPKILSKDKFAWLRDDEFARQAIAGVNPVSIEKLQFFPPVSKLDPEIYGPQESALKEEHILGHLNGMTVQEALDANKLFIVDHHDVYLPFLDRINALDGRKAYATRTIFFLSDVGTLKPIAIELSLPQTGPSSRSKRVVTPPVCATGNWTWQIAKAHVCANDAGVHQLVNHWLRTHASLEPFILAAHRQLSAMHPIYKLLDPHMRYTLEINGLARQSLINADGVIEACFTPGRYCMEISAAAYKNWRFDLEGLPADLIRRGMAVPDSTQPHGLKLLIEDYPYAADGLMIWGAIESWVRDYVNHYYPSSAQVCSDRELQAWYAETINVGHVDLRNEEWWPTLATPEDLISILTTLIWLASAQHAALNFGQYPYGGYVPNRPPLMRRLIPDENDPEYAVFLADPQKYFFSALPSLLQATKFMAVVDTLSTHSPDEEYLGERHQPSTWTGDAEIVEAFYKFSAEIGRIEKEIDERNANTKLKNRCGAGVLPYELLAPSSGPGVTCRGVPNSVSI