wanglab/gogpt-training-data huggingface dataset:
Protein: GH10454p (Q961Q8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASSKIPDWVTAEIFEDLLKANVDGYSKIKNFKADIGSAAGENYATIMLRVKIEVELQDGKSKSVSYMVKLPHQVEAIQEMMKRTNIFEIERTMYNEVVPELEALYKAVGVDITFGAKNYDLKNAKTDYVALEDLGLKGFKNANRLEGLDQEHTERVLRKLSQWHAASAVRVATKGPYPKILLQGFFKEESRPVMSEMIKGMGANFVKSCATYEGHEAYLDKVKALQPVAIDKIFEFAKVEPTEFNVLNHGDSWSNNIMFQYDAFGKIKEVYLVDYQLPKYGTVAQDLLYFLLSSTKLEDKLAKFDYYIKIYHDNLVEHLKILKYSKPIPSLRDIHLALFKYGYFGYTVATGVMSAVLLDPTDSASLENFIGGSDFQMQLYNSPRYRKHIQAVMPWLLNRGALEL
Protein: Probable alpha-galactosidase A (EC 3.2.1.22) (Melibiase A) (A2QL72)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MNQGTKSILLAATLAAIPWQVYGSIEQSSLLPIPPMGFNNWARFMCDLNETLFTETADAMAANGLRDAGYNRINLDDCWMAYQRSDNGSLQWNTTKFPHGLPWLAQYVKAKGFHFGIYEDSGNMTCGGYPGSYNHEEQDANTFALWGIDYLKLDGCNVYATQGRTLEEEYKQRYGHWHQVLSKMQHPLIFSESAPAYFAGTDNNTDWYTVMDWVPIYGELARHSTDILVYSGAGSAWDSIMNNYNYNTLLARYQRPGYFNDPDFLIPDHPGLTADEKRSHFALWASFSAPLIISAYIPALSKDEIAFLTNEALIAVNQDPLAQQATFASRDNTLDILTRNLANGDRLLTVLNKGNTTVTRDIPVQWLGLTETDCTYTAEDLWDGKTQKISDHIKIELASHATAVFRLGLPQGCSSVVPTGLVFNTASGNCLTAASNSSVAFQSCNGETSQIWQVTLSGVIRPVSQTTQCLAADGNSVKLQACDSTDSDGQNWTYAVTGNLKNAKTDGCLTEGSVQMKSCLYERDGQVFGLPSGVQLS
Protein: Rifin (Q8I4P2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVQYSKILLFPLLLNILSHNKNKPYITTHTPTTTSRVLIECNIYIPNYNNDPDMNSVRENFDRQTSQRFEEYEEHMQDKRQKCKEQCDKDIQKIILKDKMEKSLAEKVEKVCLICACGLGGGVAPVWGLVSGLWYVKWSQYVPVAVTKAGITEGIKEGLSQIMKLTTQWHPGAKTPPVDVTHILSSGKFTNTVTLYDIVHHINDSLYSTLDTQGYTQYCGAISSMASNNLSKFNRTYSTQLQLVSKAVTDAEIAESTKLAADTIILTNTIIASVVAIVVIALVMLIIYLILRYRRKKKNDEKTAI
Protein: Response regulator 23 (F4K554)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Two-component response regulator 24
- Two-component response regulator ARR18
- Two-component response regulator ARR3
- Two-component response regulator ARR1
Sequence:
MTAKDSSEPVTTLTQFNNIDVVITDYHMPGLNGVQLKKRIDEEFGNLPVIDLYRNIEHEELFRRALCFMHKPISRRDLNSLNVVCQQALRHRMNGETNLNGSGQNVTDDPDDWLRLREKPKLKWTKPLQHRFMSALKSLGVASKY
Protein: Probable eukaryotic translation initiation factor 2 subunit beta (eIF2-beta) (P56329)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit gamma
- Probable eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 3 subunit A
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 1A
Sequence:
MTETEAVVDQIDLNGALPEKKKKPKKSVAFDDEVDAVSKDGPEASSAGATDEDDSERKSSAKDLTTPVTEGEVDELKDMFSSMKKKKKSKKSSASAEEQTEDITTESGELDFSSMKKKKKKKKSADLSAFEKELEASSTGDATSDLSKQTFDSENMGEHAWLKSDRDYYYPELLNRFFTLLRTNNPELAGEKRKYTIVPPSVHREGKKTIFANISDISKRMHRSLDHVIQFLFAELGTSGSVDGSSRLIIKGRFQQKQIENVLRRYIVEYVTCKTCKSPDTILTKENRIFFMTCEACGSVRSVQAIKTGYQAQIGKRKHVS
Protein: ATP-dependent RNA helicase MAK5 (EC 3.6.4.13) (Maintenance of killer protein 5) (P38112)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:13680366, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nucleolar protein 4
- Ribosome biogenesis protein NSA1
- rRNA-processing protein EBP2
- Ribosome biogenesis protein ERB1
- Nucleolar GTP-binding protein 1
- 25S rRNA
- Ribosome biogenesis protein MAK21
- Ribosome biogenesis protein YTM1
- Nucleolar complex protein 2
- ATP-dependent RNA helicase HAS1
Sequence:
MGKKRAPQKGKTVTKPQEIIVDESKLNWKPVDIPDTLDDFGGFYGLEEIDGVDVKVVDGKVTFVTKKDSKVLKDSNKEKVGDDQESVENESGSDSESELLEFKNLDDIKEGELSAASYSSSDEDEQGNIESSKLTDPSEDVDEDVDEDVLKENVFNKDINIDDISPVNLPEWTNLAPLSMTILQSLQNLNFLRPTEIQKKSIPVIMQGVDVMGKASTGSGKTLAYGIPIVEKLISNFSQKNKKPISLIFTPTRELAHQVTDHLKKICEPVLAKSQYSILSLTGGLSIQKQQRLLKYDNSGQIVIATPGRFLELLEKDNTLIKRFSKVNTLILDEADRLLQDGHFDEFEKIIKHLLVERRKNRENSEGSSKIWQTLIFSATFSIDLFDKLSSSRQVKDRRFKNNEDELNAVIQHLMSKIHFNSKPVIIDTNPESKVSSQIKESLIECPPLERDLYCYYFLTMFPGTTLIFCNAIDSVKKLTVYLNNLGIPAFQIHSSMTQKNRLKSLERFKQQSAKQKTINHSNPDSVQLSTVLIASDVAARGLDIPGVQHVIHYHLPRSTDIYIHRSGRTARAGSEGVSAMICSPQESMGPLRKLRKTLATKNSVSTDLNSRSTNRKPIKWQNTVPLLPIETDILSQLRERSRLAGELADHEIASNSLRKDDNWLKKAADELGIDVDSDEDDISKSNSDTFLLKNKNKKMQKTINKDKVKAMRATLNELLSVPIRKDRRQKYLTGGLVNLADNLVKKRGHNSIIGHEKTNALETLKKKKKRNN
Protein: DnaJ homolog subfamily C member 22 (Q8N4W6)
Organism: Homo sapiens (Human)
Function: May function as a co-chaperone.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAKGLLVTYALWAVGGPAGLHHLYLGRDSHALLWMLTLGGGGLGWLWEFWKLPSFVAQANRAQGQRQSPRGVTPPLSPIRFAAQVIVGIYFGLVALISLSSMVNFYIVALPLAVGLGVLLVAAVGNQTSDFKNTLGSAFLTSPIFYGRPIAILPISVAASITAQRHRRYKALVASEPLSVRLYRLGLAYLAFTGPLAYSALCNTAATLSYVAETFGSFLNWFSFFPLLGRLMEFVLLLPYRIWRLLMGETGFNSSCFQEWAKLYEFVHSFQDEKRQLAYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRKPWGSRR
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) (P11151)
Organism: Bos taurus (Bovine)
Function: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2142941}; Peripheral membrane protein {ECO:0000269|PubMed:2142941}; Extracellular side {ECO:0000269|PubMed:2142941}. Secreted {ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2142941, ECO:0000269|PubMed:2674142, ECO:0000269|PubMed:2885834, ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:9188470, ECO:0000269|PubMed:9555944}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9188470}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:9188470). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (PubMed:9555944). {ECO:0000269|PubMed:9188470, ECO:0000269|PubMed:9555944}.
Interaction partners:
- Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
- Apolipoprotein C-II
- Angiopoietin-related protein 4
- Angiopoietin-related protein 3
- Patatin-like phospholipase domain-containing protein 2
- phosphatidate phosphatase
- Apolipoprotein E
- Hepatic triacylglycerol lipase
- Bile salt-activated lipase
- Prolow-density lipoprotein receptor-related protein 1
Sequence:
MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG
Protein: Cilia- and flagella-associated protein 53 (Coiled-coil domain-containing protein 11) (Q96M91)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). May play a role in the beating of primary cilia and thereby be involved in the establishment of organ laterality during embryogenesis.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25504577, ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D439}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28621423}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:26538025}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26538025}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28621423}. Cell projection, cilium {ECO:0000269|PubMed:38538594}. Note=In tracheal cell cilia, localizes prominently to both centriolar satellites and axonemes (By similarity). Tightly associated with microtubules in tracheal cilia (By similarity). In embryonic node cells, localizes to the base of the node cilia at the centriolar satellites and, to a lesser extent, to the cilium axoneme (By similarity). Localizes to centriolar satellites through G1, S phase, G2 and mitosis (PubMed:26538025). Enriched on the spindle poles in mitosis (PubMed:26538025). Relocalizes from the centriolar satellite to the ciliary transition zone upon ciliogenesis (PubMed:26538025). In skin fibroblast cells, locates predominantly to the centriole with much lower levels associated with the actin cytoskeleton (PubMed:28621423). Localizes to the sperm flagellum and manchette (By similarity). {ECO:0000250|UniProtKB:Q9D439, ECO:0000269|PubMed:26538025, ECO:0000269|PubMed:28621423}.
Interaction partners:
- Cilia- and flagella-associated protein 52
- Meiosis-specific nuclear structural protein 1
- Piercer of microtubule wall 2 protein
- Tektin-2
- Tektin-3
- Piercer of microtubule wall 1 protein
- EF-hand domain-containing family member C2
- Cilia- and flagella-associated protein 45
- Cilia- and flagella-associated protein 90
- Sperm-associated antigen 8
Sequence:
MYSQRFGTVQREVKGPTPKVVIVRSKPPKGQGAEHHLERIRRSHQKHNAILASIKSSERDRLKAEWDQHNDCKILDSLVRARIKDAVQGFIINIEERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAYQQQSQEAEKEEKRREFEAGVAANKMCLDKVQEVLSTHQVLPQNIHPMRKACPSKLPP
Protein: QKR58E-3 (Quaking related 58E-3, isoform B) (Quaking related 58E-3, isoform C) (Quaking related 58E-3, isoform D) (O44434)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- Pre-intermoult gene 1 protein
- LD36772p
- Quaking related 54B, isoform E
- GH05812p
Sequence:
METPSEFTEKQPPTHDHQPRLNEVAQKFLADLDEERQRLSADFPLCALLIDEAVDRVYCTGRIPGKEFYADVYKQKPMKITQKVFVPVKQYPKFNFTGKILGPKGNSLRRLQEETQCKIAIKGRSSIRDRNKEEQLRSTGDPRYAHLQKDLFLEVSTVATPAECYARIAYALAEIRKYLIPDKNDEVSHEQLRELMEMDPESAKNIHGPNLEAYRSVFDKKFGGNSNGAPKYINLIKRAAENPPEVDDVEEVAYEYEHRMPPKRPPTGYEYSKPRPSIIPTNAAAYKRPYPTDMKRMREPPIKSYKPNPYTILKKYK
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (H0Y547)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
XYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRYHPPNSLS
Protein: TRAPP-associated protein TCA17 (17 kDa TRAPP complex-associated protein) (P32613)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19220810}.
Interaction partners:
- Trafficking protein particle complex subunit 33
- Trafficking protein particle complex III-specific subunit 85
- Trafficking protein particle complex subunit 20
- Trafficking protein particle complex II-specific subunit 65
- Trafficking protein particle complex subunit 31
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex subunit BET5
- Trafficking protein particle complex II-specific subunit 120
- Trafficking protein particle complex II-specific subunit 130
- Trafficking protein particle complex subunit 23
Sequence:
MSLRPCFVSLIDESDKPILIYVPNEAENEMNDVLKYNVLSNISLDYFESALVEWHSLDSKPLLKSIFQLEGVSVFAMLIKQTGLKIVIGFEQKSLSGADDEFEAINQIFETVRKIYIRVKCNPLLVSGDEKSIIKSLERKFDELFISTEVEL
Protein: dipeptidyl-peptidase IV (EC 3.4.14.5) (H0YN53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPK
Protein: At2g22850 (Basic leucine-zipper 6) (Putative embryo-abundant protein) (O81002)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Proton pump-interactor 2
- Peptide methionine sulfoxide reductase B4
- LOB domain-containing protein 32
- At3g49930
Sequence:
MMSTVPAFTFTEPGLVNQLSDFQTGFTPWELNCSDLFSTIHLEPVVPSPCSGESDAGSVKINTDFNGFDESCIGSIKTNSGSDDSNLFHGVPSPQSDELDSKNTKIRSNATNHNRNKLNRSVLQVTDDRKRKRMESNRESAKRSRMRKQRHIDNLKDEANRLGLENRELANRLRIVLYNIALMCTDNNQLLSEQEILRRRFLEMRQILIFRQLQLNPSLIINHHHMI
Protein: Arabinosyltransferase RRA2 (EC 2.4.2.-) (Protein REDUCED RESIDUAL ARABINOSE 1) (Q9C9Q5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in the arabinosylation of cell wall components. Involved in the arabinosylation of extensin proteins in root hair cells. Extensins are structural glycoproteins present in cell walls and its arabinosylation is important for root hair cell development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21680836}; Single-pass type II membrane protein {ECO:0000305|PubMed:21680836}.
Interaction partners:
- Hydroxyproline O-arabinosyltransferase 2
- Hydroxyproline O-arabinosyltransferase 3
- Arabinosyltransferase RRA1
- Hydroxyproline O-arabinosyltransferase 1
- Arabinosyltransferase RRA3
- Cytochrome P450, family 77, subfamily A, polypeptide 9
- Exocyst complex component SEC15A
- Clathrin heavy chain 2
- Clathrin heavy chain 1
- Extensin-3
Sequence:
MAGRRDRIQQLRGSRIAIAIFVGILIGCVCSVLFPNGFFNSGSSLIANEERISKSTSTDGLASCESSERVKMLKSDFSIISVKNAELRKQVRELTEKVRLAEQETENARKQVLVLGSEIKAGPFGTVKSLRTNPTVVPDESVNPRLAKLLEKVAVNKEIIVVLANSNVKPMLELQIASVKRVGIQNYLIVALDDSMESFCESKEVVFYKRDPDKAVDMVGKSGGNHAVSGLKFRVLREFLQLGYSVLLSDVDIVFLQNPFSHLHRDSDVESMSDGHDNNTAYGFNDVFDEPSMGWARYAHTMRIWVFNSGFFYLRPTIPSIDLLDRVADTLSKSEAWDQAVFNEQLFYPSHPGYTGLHASKRVMDMYEFMNSKVLFKTVRKNQELKKLKPVIVHLNYHPDKLERMHAVVEFYVNGKQDALDSFPDGSD
Protein: Geranylgeranyl diphosphate synthase (GGPP synthase) (EC 2.5.1.29) (Farnesyltranstransferase) (P22873)
Organism: Pseudescherichia vulneris (Escherichia vulneris)
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Interaction partners:
Sequence:
MVSGSKAGVSPHREIEVMRQSIDDHLAGLLPETDSQDIVSLAMREGVMAPGKRIRPLLMLLAARDLRYQGSMPTLLDLACAVELTHTASLMLDDMPCMDNAELRRGQPTTHKKFGESVAILASVGLLSKAFGLIAATGDLPGERRAQAVNELSTAVGVQGLVLGQFRDLNDAALDRTPDAILSTNHLKTGILFSAMLQIVAIASASSPSTRETLHAFALDFGQAFQLLDDLRDDHPETGKDRNKDAGKSTLVNRLGADAARQKLREHIDSADKHLTFACPQGGAIRQFMHLWFGHHLADWSPVMKIA
Protein: Poly(RC) binding protein 4, isoform CRA_a (RNA binding protein MCG10) (Q9GZT1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPRCPALILYLQSSARITISEGSCPERITTITGSTAAVFHAVSMIAFKLDEDLCAAPANGGNVSRPPVTLRLVIPASQCGSLIGKAGTKIKEIREVRGEIYHPQGIRGKGAVVRGVLGLWRPPHLESSEPGQPFSGLWEQPEVAPVLCLQTTGAQVQVAGDLLPNSTERAVTVSGVPDAIILCVRQICAVILESPPKGATIPYHPSLSLGTVLLSANQGFSVQGQYGAVTPAEVTKLQQLSSHAVPFATPSVVPGLDPGTQTSSQEFLVPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQAEGAGERHVTITGSPVSIALAQYLITACLETAKSTSGGTPSSAPADLPAPFSPPLTALPTAPPGLLGTPYAISLSNFIGLKPMPFLALPPASPGPPPGLAAYTAKMAAANGSKKAERQKFSPY
Protein: Guanosine-diphosphatase (GDPase) (EC 3.6.1.42) (P32621)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:8391537}; Single-pass type II membrane protein {ECO:0000269|PubMed:8391537}.
Interaction partners:
- Golgi apyrase
- Alpha-1,2-mannosyltransferase MNN2
Sequence:
MAPIFRNYRFAIGAFAVIMLILLIKTSSIGPPSIARTVTPNASIPKTPEDISILPVNDEPGYLQDSKTEQNYPELADAVKSQTSQTCSEEHKYVIMIDAGSTGSRVHIYKFDVCTSPPTLLDEKFDMLEPGLSSFDTDSVGAANSLDPLLKVAMNYVPIKARSCTPVAVKATAGLRLLGDAKSSKILSAVRDHLEKDYPFPVVEGDGVSIMGGDEEGVFAWITTNYLLGNIGANGPKLPTAAVFDLGGGSTQIVFEPTFPINEKMVDGEHKFDLKFGDENYTLYQFSHLGYGLKEGRNKVNSVLVENALKDGKILKGDNTKTHQLSSPCLPPKVNATNEKVTLESKETYTIDFIGPDEPSGAQCRFLTDEILNKDAQCQSPPCSFNGVHQPSLVRTFKESNDIYIFSYFYDRTRPLGMPLSFTLNELNDLARIVCKGEETWNSVFSGIAGSLDELESDSHFCLDLSFQVSLLHTGYDIPLQRELRTGKKIANKEIGWCLGASLPLLKADNWKCKIQSA
Protein: Wnt inhibitory factor 1 (WIF-1) (Q9WUA1)
Organism: Mus musculus (Mouse)
Function: Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.
Subcellular location: Secreted.
Interaction partners:
- Protein Wnt-3a
- Protein Wnt-5a
- Protein Wnt-2
- Protein Wnt-7a
- Proto-oncogene Wnt-1
- Protein Wnt-4
- Protein Wnt-11
- Protein Wnt-7b
- Protein Wnt-10b
- Protein Wnt-16
Sequence:
MARRRAFPAFALRLWSILPCLLLLRADAGQPPEESLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFRKAQQRMPAIPVNIHSMNFTWQAAGQAEYFYEFLSLRSLDKGIMADPTVNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVNVIVMNSEGNTILRTPQNAIFFKTCQQAECPGGCRNGGFCNERRVCECPDGFYGPHCEKALCIPRCMNGGLCVTPGFCICPPGFYGVNCDKANCSTTCFNGGTCFYPGKCICPPGLEGEQCELSKCPQPCRNGGKCIGKSKCKCPKGYQGDLCSKPVCEPGCGAHGTCHEPNKCQCREGWHGRHCNKRYGASLMHAPRPAGAGLERHTPSLKKAEDRRDPPESNYIW
Protein: Pre-mRNA-splicing ATP-dependent RNA helicase prp28 (EC 3.6.4.13) (Q9Y7T7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor spp42
- U1 small nuclear ribonucleoprotein C
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp22
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Pre-mRNA-processing factor 31
- LIN1-like protein
Sequence:
MTAQDSIPSLEQLVQQKRVKEEKAARPKFLSKAERARLALERRQKEVEEAKAKQNDKLLDLRKRTFTNHLENNELADDEKKSQVSSVSSNNSGTESSATDEAFSMTIRQRYMGIKPPVVKKRRRNADKKFVFDWDATDDTMKDAETSASPEATIAVFGRGKLGGFDDQSIRKAKSNSGLIQRLLQGTEQDKARAHELIQLQEKRAKKIDWDDVPWREKPLEAMKPRDWRILKEDYNISIKGDDLPNPLRNWEEAGLPSEMLKVLKKVNYKEPSSIQRAAIPVLLQRKDLIGIAETGSGKTAAFIIPLIIAISKLPPLTESNMHLGPYAVVLAPTRELAQQIQVEGNKFAEPLGFRCVSVVGGHAFEEQSFQMSQGAHIVVATPGRLLDCLERRLFVLSQCTYVVMDEADRMLDMGFEDDVNKILSSLPSSNASEKDGSILATANSSSSRRQTIMFSATLPPRVANLAKSYLIEPVMLTIGNIGQAVDRVEQRVEMISDDSKKWRRVEEILESNRFSPPIIIFVNLKRNIEAIAKQLNAIGWHAVTLHGSKSQEQRERAIEQLRNKTADILVATDIAGRGIDIPNVSLVLNYNMAKSIEDYTHRIGRTGRAGKSGTAITFLGPEDTDVYYDLRVLLSRSAKAHIPDELRNHEAAFVRHAAITQ
Protein: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein (RCc3-like protein) (Q9SUX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g63840/T12P18_14
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- AAA-ATPase At3g28580
- Putative cell wall protein
- ACD11 homolog protein
- AAA-ATPase ASD, mitochondrial
- VQ motif-containing protein 10
- Pectinesterase inhibitor 3
Sequence:
MASKSSTTISLIIILLISLAEANLLSSPTPTNNFGSCPRNPLQLGVCANVLGLANVTAGDPRARQCCTALNGLTNVQVTDCLCFIFRPIPLVFGIDVAVREIFFACNRVFPIGFQCPPPQ
Protein: LIM and SH3 domain protein 1 (LASP-1) (Metastatic lymph node gene 50 protein) (MLN 50) (Q61792)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity).
Subcellular location: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich cortical cytoskeleton. {ECO:0000250}.
Interaction partners:
- Zyxin
- Palladin
- Vasodilator-stimulated phosphoprotein
- Lipoma-preferred partner homolog
- C-X-C chemokine receptor type 1
Sequence:
MNPNCARCGKIVYPTEKVNCLDKYWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGVEPERREAQDSSSYRRPTEQQQPQPHHIPTSAPVYQQPQQQQMTSSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI