wanglab/gogpt-training-data huggingface dataset:
Protein: Tenascin C (Tenascin isoform 1 precursor) (Tenascin isoform X2) (E9QHI1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGMRGLLLASMAVAVLVHLSSAGLVKRVIRHRRESLSPTTENLTLPSPDQPVVFNHVYNINVPSGSLCSVDMDSPGTTEIKPKSEQSDQHIEHTTDGENQIVFTHRINIPKQACGCDNHMPDMKELLNRLEMLEAEVSSLREQCTSGAGCCSAQVTGEVTTKPYCSGRGNYSTDTCSCVCEPGWKGVNCSEPECPNYCQDQGRCEDGKCVCFEGFGGEDCGIELCPVDCGENGECIDGACICAEGFIGEDCSLSNCPSNCLGRGRCVDDECVCDEPWTGFDCSELICPNDCFDRGRCENGTCYCDEGFTGEDCGELTCPQNCNHHGRCVNGQCICNIGYSGEDCSKLTCLNDCSERGHCFNGKCICDPGFEGEDCSLLSCPDNCNGRGHCVNGECICGPGYEGDDCSELSCLNNCHDRGRCVNGKCICKAGFAGEDCSIKTCPHDCHGRGECVDGKCVCHDGFAGEHCGIKTCPHHCHGHGQCVDGKCICHKGFAGEDCSIKTCPNHCHGQGQCIDGKCICHDGFAGEDCSIKTCPNHCHGRGRCVDGKCICHDGFAGEDCNIKTCPNDCHDHGECVDGKCICHAGFTGHDCSELTCPNDCHNRGRCVNGQCVCNIGFTGEDCGTKTCPNNCLDRGFCEDGKCVCFEGYTGEDCSVLTCPADCNDQGQCLNGMCICDLGFTGDDCSEISPPRDLTVTEVDPETVDVAWVNEMLVTEYLITYVPTAPGGLEMEMRVSGEKKTATIRELEPGIEYLISVFAVLNSKMSVPVSARIATHLPEPEGLKFKSVKETSVEVEWDPLNIPFDGWNLIFRNTKEEDGEILNSLAPPETTFEQSGLGPGQEYEVKLEVVKNNTRGPPASKNVVTMIDAPSQVDVRDVTDTTALVTWLQPVAQVDGISVSYGPNTDSSDRNTIELSSIETQYHLAELSPDTEYEVSLMARRGEMSSFPIYETFTTDLDSPKHLKAIEQTDESITLEWRNSRANVLNYRVKYGPLSGGEHGELVFPSGLQDTTQAKITGLRPGTEYGMGVTSIKEERESLPATTNAVTDLDPPKDLQVSETTETTLALVWRRPVAKIDTYSLVFIPADGDKTELKIPGAANTYILTGLNPGMLHTITLTAERGRKMSAPATLSASTDEEKPQVGNITISDVSWDSFSMSWDLDRGEVEGFLIEVSDPDGLSDGQNHTLSGQEFSLAVTDLSPSTFYRVTLYGLYKGELLDPVFAEAITGLGTPKGIRFSDVTDTSATVHWTMPHTRVDNYRVIYVPIQGGSPLTLRVDGGESQAMLSNLTPGVTYQVTVIAVKGLEESEPGSERVTTALDKPRGLTAVNISDTEALLLWQPSIATVDGYVITYSADSVAPVMERVSGNTVEFEMSSLTPATLYTVKVYAFRDTAKSAATSTDFTTDVDAPQNLAASNIQTETAMLTWKPPRADISGYILSFESADGVVKEVVLSPTATFYSMSQLTASTEYTVKLQAIAGPKRSRVISTVFLTIGVLYKHPKDCSQALLNGDTTSGLYTIYLRGDESQPLQVYCDMTTDGGGWIVFVRRQSGKVEFFRNWKNYTAGFGDLNDEFWLGLSNLHKITSFGQYELRVDLRDKGESAYAQYDKFSISEPRARYKVHVGGYSGTAGDSMTYHHGRPFSTYDNDNDIAVTNCALSYKGAFWYKNCHRVNIMGRYGDNSHSKGVNWFHWKGHEHSVEFAEMKIRPANFRNFEGRKKRS
Protein: Xyloglucan glycosyltransferase 4 (EC 2.4.1.-) (Cellulose synthase-like protein C4) (AtCslC4) (Xyloglucan synthase 4) (Q9LJP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose. Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22665445, ECO:0000269|PubMed:25392066, ECO:0000305|PubMed:17488821}; Multi-pass membrane protein {ECO:0000305|PubMed:17488821}.
Interaction partners:
- Xyloglucan galactosyltransferase MUR3
- Xyloglucan 6-xylosyltransferase 1
- Probable xyloglucan 6-xylosyltransferase 5
- Xyloglucan galactosyltransferase XLT2
- Galactoside 2-alpha-L-fucosyltransferase
- Xyloglucan 6-xylosyltransferase 2
- Cellulose synthase A catalytic subunit 8
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Probable galacturonosyltransferase 7
- Beta-1,4-xylosyltransferase IRX14
Sequence:
MAPNSVAVTMEKPDNFSLLEINGSDPSSFPDKRKSISPKQFSWFLLLKAHRLISCLSWLVSSVKKRIAFSAKNINEEEDPKSRGKQMYRFIKACLVISIIALSIEIVAHFKKWNLDLINRPSWEVYGLVEWSYMAWLSFRSDYIAPLVISLSRFCTVLFLIQSLDRLVLCLGCFWIKFKKIEPKLTEESIDLEDPSSFPMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEEVSVWAEKGVNIIYRHRLIRTGYKAGNLKSAMTCDYVKDYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGPMQLFRLCLPSIIKSKISVWKKANLIFLFFLLRKLILPFYSFTLFCIILPLTMFIPEAELPLWIICYVPIFISLLNILPSPKSFPFLVPYLLFENTMSITKFNAMISGLFQFGSAYEWVVTKKTGRSSESDLLAFAEKEEKLHRRNSESGLELLSKLKEQETNLVGQETVKKSLGGLMRPKNKKKTNMVFKKELGLAFLLLTAAARSFLSAHGLHFYFLLFQGLSFLVVGLDLIGEQIS
Protein: Molybdate-binding protein ModA (Molybdate/tungstate-binding protein ModA) (P37329)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell. Binds molybdate with high affinity in vitro and with a similar affinity in vivo. Binds tungstate with high affinity in vitro. Binds unnatural anion perrhenate with high affinity in vitro. Does not bind sulfate, phosphate, arsenate, selenate, chlorate, metavanadate, nitrate, perchlorate, permanganate or carbonate.
Subcellular location: Periplasm {ECO:0000269|PubMed:8409926, ECO:0000269|PubMed:8576221, ECO:0000269|PubMed:9545596}.
Interaction partners:
- Molybdenum import ATP-binding protein ModC
- Molybdenum transport system permease protein ModB
- DNA-binding transcriptional dual regulator ModE
- Sulfate transport system permease protein CysT
- Molybdopterin molybdenumtransferase
- Pyridoxal phosphate phosphatase YbhA
- GTP 3',8-cyclase
- Vitamin B12-binding protein
- ABC transporter ATP-binding protein ModF
- High-affinity zinc uptake system protein ZnuA
Sequence:
MARKWLNLFAGAALSFAVAGNALADEGKITVFAAASLTNAMQDIATQFKKEKGVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKAIDTATRQTLLGNSLVVVAPKASVQKDFTIDSKTNWTSLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLSPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPVAVVEGHNNATVKAFYDYLKGPQAAEIFKRYGFTIK
Protein: GDPD5 protein (Q9HBR3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHAIPPVAMECVDAHLCHLSSCLCQEAPEFSAVILPQGPGPSLYLKQLCSSCQSQSTRRFSPGGSQLQCGDTSSSPTHLMPPPTPCPRSGPEPRPLGAAGDGQKSELRTTGSHAQVSSRPQGRRVT
Protein: Thiolase (P96838)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTEAYVIDAVRTAVGKRGGALAGIHPVDLGALAWRGLLDRTDIDPAAVDDVIAGCVDAIGGQAGNIARLSWLAAGYPEEVPGVTVDRQCGSSQQAISFGAQAIMSGTADVIVAGGVQNMSQIPISSAMTVGEQFGFTSPTNESKQWLHRYGDQEISQFRGSELIAEKWNLSREEMERYSLTSHERAFAAIRAGHFENEIITVETESGPFRVDEGPRESSLEKMAGLQPLVEGGRLTAAMASQISDGASAVLLASERAVKDHGLRPRARIHHISARAADPVFMLTGPIPATRYALDKTGLAIDDIDTVEINEAFAPVVMAWLKEIKADPAKVNPNGGAIALGHPLGATGAKLFTTMLGELERIGGRYGLQTMCEGGGTANVTIIERL
Protein: RIC3 acetylcholine receptor chaperone, isoform L (E1JGP6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGWREHQTRAATATAAAKKPAAKDTEKELYNASVSATEVASSLSASLKSHQQLKEAEQLMEIEKLRQKLESTERAMAQLVAEMNTDQYEAKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ
Protein: Adenine deaminase (ADE) (EC 3.5.4.2) (Adenine aminohydrolase) (AAH) (Q9P6I7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. Also exhibits a low activity towards N(6)-substituted adenines that are commonly known as the plant hormones cytokinins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03145, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03145, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenosine kinase
- Putative purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase
- IMP-specific 5'-nucleotidase 1
- Uncharacterized deaminase C1683.02
- Inosine-5'-monophosphate dehydrogenase
- Probable guanine deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenylate kinase
- Thymidylate kinase
Sequence:
MSNLPIYNFIRKLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPSTLLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYEYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKRNDFENGIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISGKRKEELLSSVQKCVKEYTAEIQQPKTLETAVEVQA
Protein: LD32918p (Undicht, isoform A) (Undicht, isoform B) (Q9VCI4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD29228p
- UPAR/Ly6 domain-containing protein crok
- Transferrin 2
- EG:80H7.2 protein
- Contactin
- GEO05642p1
Sequence:
MHYYLAAICLVGLMGSALGQYNLVQKDNCIIPKILQGSWFSWETGLPTLTVIDATSMSSRGYCINYMRHKGDEYSFVFKERSKDCYHCVRTIIRTLNVFEKFEGPCVGIPAGQEPTVDYVCRGVKDDQQLITLFNENFVPINCRSSLEGVWHFTYQNRFRFTGVCDKPDARIQSCQTAGTQFLIQNQKFNVTYQQCEGMEGTFTGTVEFSCLGDWFVGKNHYFAVANTKESRKDEKYRCFLKNRDDDLYVGVSITAECNTLKTPETSPERLKLTPVKAEFVEPGCTLPQNFSGEWVNTANIDADVSISETHINETYYPDKARYRKTIYVCRERRGNRVMMARLTVDGCQKDYVCFDFMPRHHNIIRYRKGLAVIKDDFSTVCSWVQFPNSEAWKYDLFLARNPVPVRCPVAGKFNFTQRGEHPFRTRILGGVTLSPRPDIHCKQNISDLSVCDTDQKELAVDENYCLSVDHLGRPVDIYSDPDYRMKCIGFWKENLKSYLITYDDLDPLSKYRCWVYQRADLNRVLMSQAVGAFCKLEQDVTSWNHSEGAAVAIDAVEYERERDDCPMHFDDGLNPWKPSDASNIIFDWDFYRAGAATLKFQLTGLVIVVLVQVRSLLA
Protein: Protein psi1 (Protein psi) (Q09912)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for nuclear migration during mitosis. It is required for the normal initiation of translation.
Interaction partners:
- Probable heat shock protein ssa1
- Probable heat shock protein ssa2
- Heat shock protein homolog pss1
- Mitochondrial protein import protein mas5
- Heat shock protein sti1 homolog
- Hsp70 nucleotide exchange factor fes1
- Ribosome-associated molecular chaperone sks2
- 40 kDa peptidyl-prolyl cis-trans isomerase
- Heat shock protein 104
- Heat shock protein 90 homolog
Sequence:
MVADTKLYDCLEVRPEASEAELKKAYRKLALKYHPDKNPNGEKKFKEISLAYEVLSDPQRRKLYDQYGITEGNAAPPPPGAEGGPGAGFGGFPGAGPGGARTFHFNMGGPGGAQFFSASDPNDIFERVFGHAFAGGGGMGGGMGGMGGMDDDMDMDGGFGTRTRGGGMPGGFANMFGGGGAGPHARRSHPSFGGSRPSQPPAQNEVITRPLNVSLEDLFTGCTKKMKISRHIIDASGQSVKADRILEIKVKPGWKAGTKIKFAGEGDEKPDGTVQDIQFVLAEKPHPVFTRSGDDLRMQVELSLKEALLGFSKQISTIDGKKLKVSSSLPTQPGYEITYPGFGMPLPKNPSQRGNMIIECKVKFPTELTPAQKTAAEAF
Protein: Bacterial histone-like protein (Q8I3A2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- indole-3-glycerol-phosphate synthase
Sequence:
MYVILYCVLFLFQVVYSRRAFINVHKNNIINNKLSVNNPYNKNALYQSSSKIPMSQAITKKQIIEEVSMETKENKKTVEKIMNGIFDNIYKHLENNEKIYIHKFGMFYNIFRKKRCIKNLRTKEDIEIESSHMPHFKFSKVFKELIKQNVKVKKGKGVSTNDHDLDEDDMNMDNINESFKENVNEKLIY
Protein: Fructose-bisphosphate aldolase 6, cytosolic (AtFBA6) (EC 4.1.2.13) (Cytosolic aldolase 2) (cAld2) (Q9SJQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis. Associates with GAPC1 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21782461}. Nucleus {ECO:0000269|PubMed:21782461}. Mitochondrion {ECO:0000269|PubMed:12953116}.
Interaction partners:
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Sedoheptulose-1,7-bisphosphatase, chloroplastic
- Transketolase-2, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- Transketolase-1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase])
Sequence:
MSSFTSKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSDGTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESAKVAPEVIAEHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCKANSEATLGAYKGDAKLGEGAAESLHVKDYKY
Protein: E3 SUMO-protein ligase PIAS1 (EC 2.3.2.27) (DEAD/H box-binding protein 1) (Protein inhibitor of activated STAT protein 1) (RING-type E3 ubiquitin transferase PIAS1) (O88907)
Organism: Mus musculus (Mouse)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA (By similarity). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB.
Subcellular location: Nucleus {ECO:0000269|PubMed:16600910}. Nucleus speckle {ECO:0000250|UniProtKB:O75925}. Nucleus, PML body {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O75925}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (By similarity). Interaction with MSX1 is required for localization to the nuclear periphery (PubMed:16600910). {ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:16600910}.
Interaction partners:
- Signal transducer and activator of transcription 1
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 1
- Signal transducer and activator of transcription 2
- Small ubiquitin-related modifier 3
- Signal transducer and activator of transcription 3
- Small ubiquitin-related modifier 2
- SUMO-activating enzyme subunit 1
- Androgen receptor
- Signal transducer and activator of transcription
Sequence:
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPPTLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD
Protein: GATA zinc finger domain containing 2A (C9JMI3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALK
Protein: Uncharacterized protein Rv2569c (P9WL93)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv2568c
- Uncharacterized protein Rv2567
- Uncharacterized protein Rv2411c
- Conserved protein
Sequence:
MSADSSLSLPLSGTHRYRVTHRTEYRYSDVVTSSYGRGFLTPRNSLRQRCVAHRLTIDPAPADRSTSRDGYGNISSYFHVTEPHRTLTITSDSIVDVSPPPPGLYTSGPALQPWEAARPAGLPGSLATEFTLDLNPPEITDAVREYAAPSFLPKRPLVEVLRDLASRIYTDFTYRSGSTTISTGVNEVLLAREGVCQDFARLAIACLRANGLAACYVSGYLATDPPPGKDRMIGIDATHAWASVWTPQQPGRFEWLGLDPTNDQLVDQRYIVVGRGRDYADVPPLRGIIYTNSENSVIDVSVDVVPFEGDALHA
Protein: Exported protein 1 (Q8IIF0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKILSVFFLALFFIIFNKESLAEKTNKGTGSGVSSKKKNKKGSGEPLIDVHDLISDMIKKEEELVEVNKRKSKYKLATSVLAGLLGVVSTVLLGGVGLVLYNTEKGRHPFKIGSSDPADNANPDADSESNGEPNAGPQVTAQDVTPEQPQGDDNNLVSGTEH
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q59181)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Subcellular location: Cytoplasm.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Enolase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Pyruvate kinase
- Probable protein-export membrane protein SecG
- tRNA pseudouridine synthase B
- Ribosomal RNA small subunit methyltransferase G
Sequence:
MSIKTVKDFSSFAGKRALVRCDFNVPLKEGSISDDTRIRAALSTIEYLKERGARIVLVSHLGRPDGKKNPKYSLKPVANRLSELLGQDVKMLSDCIGSEVVNSTLQMKDGDVVLLENVRFYAEEEKNDKNFAKKLSENGDVFVNDAFGAAHRAHASTVGVADYLPSVGGFLMEKEDKFLGGILKNPERPFVSIIGGSKVSSKIAVLESLLSKSNVVVIGGGMAYTFLHSEGYSIGKSLLEDEYIGIASSFLKKAKELGVKVILPLDHIVADDFNKNSIPEYIDSFNIPENKIGMDIGANTLKEIENVVKTAKTIIWNGPLGVFEFDSFSKGTAKVAEMVASCSGLTVVGGGDSVAAVNKFNLSDKITHVSTGGGASLEYLEGRILPGIKVLEN
Protein: Putative eukaryotic translation initiation factor 4 gamma (Q1MSJ2)
Organism: Oryza glaberrima (African rice)
Interaction partners:
Sequence:
MEKDHQPVISLRPGGGGGGPRPGRLFSPAFAAAASGSGDLLRSHVGGASKIGDPNFEVRERVRYTRDQLLELREIVDIPEAILRIKQEIDIELHGEDQIWGRPESDVQVQTQTQAQPHNRYGETDNRDWRARTVQPPAANEEKSWDNIREAKAAHASSGRQQEQVNRQDQLNHQFASKAQVGPTPALIKAEVPWSARRGNLSEKDRVLKTVKGILNKLTPEKFDLLKGQLMESGITTADILKDVISLIFEKAVFEPTFCPMYAQLCSDLNEKLPSFPSEEPGGKEITFKRVLLNNCQEAFEGDESLRAEIAKLTGPDQEMEKERIVKLRTLGNIRLIGELLKQKMVPEKIVHHIVQELLGSGPDKKACPEEENVEAICQFFNTIGKQLDENPKSRRINDTYFIQMKELTTNLQLAPRLRFMVRDVVDLRSNNWVPRREEIKAKTISEIHDEAMKTLGLRPGATGLTRNGRNAPGGPLSPGGFPMNRPGTGGMMPGMPGTPGMPGSRKMPGMPGLDNDNWEVPRSKSMPRGDSLRNQGPLLNKPSSINKPSSINSRLLPHGSGALIGKSALLGNGGPPTRPSSLMASPTHTPAQTAPSPKPVSAAPAVVPVTDKAAGSSHEMPAAVQKKTVSLLEEYFGIRILDEAQQCIEELQCPEYYSEIVKEAINLALDKGPNFIDPLVRLLEHLHTKKIFKTEDLKTGCLLYAALLEDIGIDLPLAPALFGEVVARLSLSCGLSFEVVEEILKAVEDTYFRKGIFDAVMKTMGGNSSGQAILSSHAVVIDACNKLLK
Protein: Heat shock protein 21, chloroplastic (25.3 kDa heat shock protein, chloroplastic) (AtHsp25.3) (P31170)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone protein required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:23922206}.
Interaction partners:
- Protein disulfide isomerase pTAC5, chloroplastic
- Chaperone protein ClpB1
- Heat shock 70 kDa protein 4
- Heat shock protein 90-1
- Heat shock 70 kDa protein 5
- Heat stress transcription factor A-2
- Protein HEAT-STRESS-ASSOCIATED 32
- L-ascorbate peroxidase 2, cytosolic
- 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic
- Heat shock 70 kDa protein 8
Sequence:
MASTLSFAASALCSPLAPSPSVSSKSATPFSVSFPRKIPSRIRAQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ
Protein: E3 ubiquitin-protein ligase WAVH1 (EC 2.3.2.27) (Protein WAV3 homolog 1) (RING-type E3 ubiquitin transferase WAVH1) (Q9ZQ46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in the regulation of root growth. Acts as positive regulator of root gravitropism. Possesses E3 protein ligase activity in vitro.
Interaction partners:
- Magnesium-chelatase subunit ChlI-2, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- RING-H2 finger protein ATL10
- Pollen Ole e 1 allergen and extensin family protein
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
Sequence:
MLNGWRRAFCTSIPKETNQNDVDDDGLVGLRHKSTSRFGFFSTPSTPRSDSGTGTYSLRCRTSTATAVSTTSSLPGTPKLKCKTTTTGETTPRNRSLVSLLTPSSSSISPASFTLLKSKLRFKQSSSNKCGICLQSVKSGQGTAIFTAECSHTFHFPCVTSRAAANHNRLASCPVCGSSLLPEIRNYAKPESQIKPEIKNKSLRVYNDDEALISSPISPAGFHTILESDENEDCEEFTGFSVNTPSPLTAKLLTDRNVDVKLSPESAIVASGKGYETYSVVMKVKSPPFPTARGFARRVPVDLVAVLDVSGRNSGGKLEMLKQTMRIVLSNLREMDRLSIIAFSSSSKRLSPLRRMTANGRRSARRIVDIITVPGSVSGVGIDFSGEGMSVNDALKKAVKVLDDRRQKNPFTAVFVLTDRQAHQVAQLAHSRIPIHTIWLSHAIPEDAFARTINGYLSLSVQDLGLQLGIVSGLGQGEITSVYSLSGRPAWLGTGSIRLGDMYAEEERALLVEIKSPVNNSLTGSRSHKIMTVRSRYVDPTTQELRNPEDRALLIPTPLTVRSSSNPNISRLRNLHVSTRAVAESRRLIERNHYSGAHRLLTSARALLVQHGLSSSDACIRGLDAEIADLNSVKGRHVAASESLESLTPTSAWKAAERLAKVAMVRKHMNRVSDLHGFENARF
Protein: Target of Nesh-SH3 (Q8BLU9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLSSLGCLLLCGSIALALGNAQKLPKGKKPSLKVHINTTSDSILLKFLRPNANVKLEGFLLGYGSNVSPNQYFPLPTEGKFTEAVVDAEPKYLIVVRPAPPPSQKKSCSGKSRPRKPLQLVVGTLTPSSVFLSWGFLINPHHDWTLPSHCPSDRFYTIR
Protein: Geranyl diphosphate synthase large subunit (Geranyl pyrophosphate synthase large subunit) (Gpp synthase large subunit) (Q9SBR3)
Organism: Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata)
Interaction partners:
Sequence:
MSALVNPVAKWPQTIGVKDVHGGRRRRSRSTLFQSHPLRTEMPFSLYFSSPLKAPATFSVSAVYTKEGSEIRDKDPAPSTSPAFDFDGYMLRKAKSVNKALEAAVQMKEPLKIHESMRYSLLAGGKRVRPMLCIAACELVGGDESTAMPAACAVEMIHTMSLMHDDLPCMDNDDLRRGKPTNHMAFGESVAVLAGDALLSFAFEHVAAATKGAPPERIVRVLGELAVSIGSEGLVAGQVVDVCSEGMAEVGLDHLEFIHHHKTAALLQGSVVLGAILGGGKEEEVAKLRKFANCIGLLFQVVDDILDVTKSSKELGKTAGKDLVADKTTYPKLIGVEKSKEFADRLNREAQEQLLHFHPHRAAPLIALANYIAYRDN
Protein: Fibroblast growth factor 16 (FGF-16) (O43320)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O54769}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibroblast growth factor-binding protein 1
- Decorin
- Vascular endothelial growth factor receptor 2
Sequence:
MAEVGGVFASLDWDLHGFSSSLGNVPLADSPGFLNERLGQIEGKLQRGSPTDFAHLKGILRRRQLYCRTGFHLEIFPNGTVHGTRHDHSRFGILEFISLAVGLISIRGVDSGLYLGMNERGELYGSKKLTRECVFREQFEENWYNTYASTLYKHSDSERQYYVALNKDGSPREGYRTKRHQKFTHFLPRPVDPSKLPSMSRDLFHYR
Protein: MYBPC1 protein (Myosin binding protein C1) (A6QP89)
Organism: Bos taurus (Bovine)
Interaction partners:
- Troponin T, slow skeletal muscle
- Troponin C, skeletal muscle
- Troponin T, fast skeletal muscle
- Troponin I, cardiac muscle
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Alpha-actinin-3
- MYH3 protein
- Alpha-actinin-2
- Troponin I, cardiac muscle
- Tropomyosin beta chain
Sequence:
MPEPTKKEENEVLAPAPAPPPEEPNKEKEAGTAPVKEPNKEKEAGTAPAKEPNKEKEAGTAPAKEPNKEKEAGTSPGKDEEDASPPGGLPPEWSIGESPAGEEQDKQNANSQLSILFVEKPQGGTVKVGENITFIAKVKAEDLLRKPTVKWFKGKWMDLASKAGKHLQLKETFERHSRVYTFEMQIIKAKENYAGNYRCEVTYKDKFDSCSFDLEVLESTGTTPNIDIRSAFKRSGEGQDDAGELDFSGLLKRREVKPQEEQPEVDVWELLKNAKPSEYEKIAFQYGITDLRGMLRRLKRMRRVEKKSAAFARILDPAYQVDKGGRVRFVVELADPKLEVKWYKNGQEIRPSTKYIFEHKGCERIMFINNCVLTDDSEYYVTAGDEKCSTELFVREPPVMVTKQLEDTKAYCGERVELECEVSEDDANVKWFKNGEEIIPGPKSRYHIRVEGKKHILIIDGATKADSAEYSVMTTGGQSSAKLSVDLKPLKILTPLTDQTVNLGKEICLKCEVSENITGKWTKNGLPVQETDHLKIVHKGRIHKLVIANALVEDEGDYVFTPDDYSVTLPAKVHVVDPPKINLDGLDADNTVTVIAGNKLRLEIPISGEPPPKALWSRADKAIMEGSGRIRSENYPDSTTLVIDIAEKDDSGVYHINLKNEAGEAHASIKIKVVDIPDPPVAPNVTDVGDDWCIMTWDPPLYDGGSPILGYFIERKKKQSSRWMRLNFDLCKETIFEPKKMIEGVAYEVRIFAVNAVGISKPSMPSKPFVPLAVTSPPTLLTVDSVTDTTVTMKWRPPDQIGAAGLDGYVLEYCFEGSTSAKQSDENGEAAYDLPADDWIAANTELIEKTKFTITGLPTDSRIYVRVKAVNAAGASEPKYYSQPILVKEIIEAPKIRIPRHLKQTYIRRVGEAINLVIPFQGKPRPELIWTKDGAPIDKNQINIRNSETDTIVFIRKAERSHSGKYDLQVKVEKFVETASIDIRVIDRPGPPQLVKIEDVWGENVALSWTPPRDDGNTAITGYTIQKADKKSMEWFTVIEHYHRTSATITELVIGNEYYFRVFAENMCGLSEDATMTKESAVIAKDGKIYKNPVYEDFDFTEAPMFTQPLVNTYAVAGYNATLNCSVRGNPKPKITWMKNKVVIKDDPRYRMFSNQGVCTLEIRKPSPYDGGTYCCKAVNDLGTVEIECKLEVKVVAQ