wanglab/gogpt-training-data huggingface dataset:
Protein: EF-hand domain-containing family member C2 (Q32TF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A0A3Q1N1R0}.
Interaction partners:
- PARK2 co-regulated.
- WD repeat-containing protein 90
- Calaxin
- Cilia- and flagella-associated protein 161
- Tektin
- EF-hand domain
- Tektin 2
- Enkurin
- Cilia and flagella-associated protein 52.
- EF-hand domain family, member B
Sequence:
MALPMLPGNSVNRNLGKDKFHKSQHFDYSNGVAMMVGTEKPGIGGDLLLGQSARAKYSRFPKGEGSGAPAWLAFDKQVLCFDAYFNEAVPQRREEKYRVRKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYNVHHFNINQEVLFYSRNFMITDCDPFTRNFLVKMGVRLNPPASTPADPYTTLRQELEENMKPLRPYERLDTLKQFLEHDRQVLRFYCYWDDSESMFGDPRELILHYFLADDTMEMYEVVPPNSGRDTVPKFLHRGKLPKHAPIPKRQPGEITDRTVLNVFGPVGQGGPYILDSLKTGALEEEFYKDSDLTIGAVINVWGRRVLICDCDYFTKEYYRSKYGIEDFPSISYKASPPPKPAKQVPPYTGFGSEEDSLCSCQGLLPKPPQKDFKKLMEKDRRGLVSNVLRFVGKMLTDSPVDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGQELFKSEMSEYFTAQDLYVGAHLLLNSQPFQLVDADDFTFSYMEQHADEFPKANIGTIISKVKSISEEQQKTVKQFFTMSDPSSTGSLPYESFRTLLADLDVELSEHEIMTLGRVYSVRQQPEVNVGLMLAVAQDHLKKKNFEKFSEMIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDYHAFLSGINWRENPVPAVLPEDTVKFDADWRGEAPEPAVKTINYSLLLEDVFGSATNINDS
Protein: Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) (O42849)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phenylalanine--tRNA ligase alpha subunit
- Phenylalanine--tRNA ligase, mitochondrial
- Elongation factor 1-beta
- Putative leucine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, cytoplasmic
- Eukaryotic translation initiation factor 3 subunit H
- Isoleucine--tRNA ligase, cytoplasmic
- GMP synthase
- tRNA
Sequence:
MPTISCDKEELYKALGREYTTQEFDELCFQFGIELDEDTTNDPERSPSERPSLKIDIPANRYDMLCLEGIAQALNVFNRRMATPQYKLLPSTTSLTISPETSEIRPYAAAAILRGVKLDPIRYQSFIALQDKLHANLCRNRTLVAIGTHDFSVMEGPFTYEALKPEEINFVPLNQTQEINGSNLLEFYKDSKHLSRYLHIIANSPRYPVILDAKRRVCSLPPIINSEFSKISVDTRDIFIDVTATDKTKLEIVVNMMTTMFSCYCEEPFTIEPVNIISEHNGCTRVTPNLNPTCFKADIDYLNEACGLSLPEDEICHLLTRMMLTAKPNPNDSKTLLVYVPPLRADILHQCDIMEDLGIAYGYDNLKHTYPAHSVTFGKPFEVNRLADIIRNEVAYAGWSEVMPFILCSHDENYAWLRKTDDSKAVQLANPKTLEFQVVRSSLLPGILKTVRENKNHALPIKIFEVSDVAFCDYSRERMTRNERHLCAIFAGLNSGFEQIHGLLDRVMLMLNTKRIMNPKDSDAVGYWIEAEDDSTFFPGRCAAVYYRKDFGTAGIRVGVFGVLHPLVLEKFELTSAASAVEIDLTLWV
Protein: E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP) (xXIAP) (A5D8Q0)
Organism: Xenopus laevis (African clawed frog)
Function: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins. Acts as a direct caspase inhibitor. A key apoptotic suppressor in eggs. Acts as a positive regulator of Wnt signaling.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P98170}. Nucleus {ECO:0000250|UniProtKB:P98170}.
Interaction partners:
Sequence:
MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS
Protein: Glial cell line-derived neurotrophic factor (Astrocyte-derived trophic factor) (ATF) (Q07731)
Organism: Rattus norvegicus (Rat)
Function: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. May also modulate local neuronal effects in distal regions of the motor neuron.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P39905}.
Interaction partners:
- GDNF family receptor alpha-1
- Proto-oncogene tyrosine-protein kinase receptor Ret
- GDNF family receptor alpha-2
- BDNF/NT-3 growth factors receptor
- NT-3 growth factor receptor
- Neurotrophic factor BDNF precursor form
- High affinity nerve growth factor receptor
- GDNF family receptor alpha-3
- Ciliary neurotrophic factor
- Beta-nerve growth factor
Sequence:
MKLWDVVAVCLVLLHTASAFPLPAGKRLLEAPAEDHSLGHRRVPFALTSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI
Protein: Transcription factor myb109 (Q70SX1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLPAAMAAAGIRLWPGIQERDYGRGYKKGLWAMEEDKLLIDYVNVHGKGQWNKIANRTGLKRSGKSCRLRWMNYLSPNVKKGDFSEEEEDLVIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNSHLRKKLGIIDQNKTRIDFCQSSKQVKVCHVDEAATDPSPGHGTTTETTGITVDQSNQQEVIDHRVLNNTTQESMTSESYINTFWIPDHDYELSTLAMIDHFHECSSFHLS
Protein: Centrosomal protein CEP57L1 (Centrosomal protein 57kDa-like protein 1) (Centrosomal protein of 57 kDa-related protein) (Cep57R) (Cep57-related protein) (Q8IYX8)
Organism: Homo sapiens (Human)
Function: Centrosomal protein which may be required for microtubule attachment to centrosomes.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Interaction partners:
Sequence:
MDSELMHSIVGSYHKPPERVFVPSFTQNEPSQNCHPANLEVTSPKILHSPNSQALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELIKQKKDISIQLSSAQSRCTLLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLEISKIIMSSVSNLKHSKEKKKSSKKTKCIKRRPPWQICSKFGALPFVAEKMRQHRDPHILQKPFNVTETRCLPKPSRTTSWCKAIPPDSEKSISICDNLSELLMAMQDELDQMSMEHQELLKQMKETESHSVCDDIECELECLLKKMEIKGEQISKLKKHQDSVCKLQQKVQNSKMSEASGIQQEDSYPKGSKNIKNSPRKCLTDTNLFQKNSSFHPIRVHNLQMKLRRDDIMWEQ
Protein: Acetyl-CoA carboxylase, isoform B (Acetyl-CoA carboxylase, isoform C (EC 6.4.1.2)) (Acetyl-CoA carboxylase, isoform F) (Acetyl-CoA carboxylase, isoform G) (GH12002p) (Q7JV23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSETNESNDTAAQSAEGERPSFLVGDEIDERAAEAGEACDEFPLKMQNDVRQNGDISERRKRLRPSMSRGTGLGQDRHQDRDFHIATTEEFVKRFGGTRVINKVLIANNGIAAVKCMRSIRRWAYEMFKNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGSNNNNYANVELIVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPWSGSDLKAQYSGKKIKISSELFARGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVPGSPIFVMKLARGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGIPLYRLKDIRLLYGESPWGSSVIDFENPPNKPRPSGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAASGGLHEFADSQFGHCFSWGENRQQARENLVIALKELSIRGDFRTTVEYLITLLETNRFLDNSIDTAWLDALIAERVQSEKPDILLGVMCGSLHIADRQITESFSSFQTSLEKGQIQAANTLTNVVDVELINDGIRYKVQAAKSGANSYFLLMNSSFKEIEVHRLSDGGLLISLEGASYTTYMKEEVDRYRIVIGNQTCVFEKENDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVRRPGAVLDAGSLLGHLELDDPSLVTKAQPFKGQFLQPENAPVPEKLNRVHNTYKSILENTLAGYCLPEPFNAQRLRDIIEKFMQSLRDPSLPLLELQEVIASISGRIPISVEKKIRKLMTLYERNITSVLAQFPSQQIASVIDSHAATLQKRADRDVFFLTTQSIVQLVQRYRNGIRGRMKAAVHELLRQYYDVESQFQYGHYDKCVGLVREHNKDDMQTVVNTIFSHSQVAKKNLLVTLLIDHLWANEPGLTDELANTLSELTSLNRAEHSRVALRSRQVLIAAHQPAYELRHNQMESIFLSAVDMYGHDFHPENLQRLILSETSIFDILHDFFYHSNRAVCNAALEVYVRRAYTSYELTCLQHLELSGGLPLVHFQFLLPTAHPNRLFSRMSSPDGLDQAAAESLGNSFVRTGAIAAFDSFEHFEMYSDEILDLLEDFVSPAMVNAKVLEAVEAADSISDSRHSTSINVSLSDPVTRANAAEEAKSTEPIHIVSVAVRETGELDDLQMAQIFGNYCQEHNEELFQRRIRRITFAALKKRQFPKFFTFRARDKFTEDRIYRHLEPASAFHLELNRMKTYDLEALPTANQKMHLYLGKAKVSKGQEVTDYRFFIRSIIRHSDLITKEASFEYLQNEGERVLLEAMDELEVAFSHPHAKRTDCNHIFLNFVPTVIMDPAKIEESVTKMIMRYGPRLWKLRVLQAELKMVIRQSPQSPTQAVRLCIANDSGYFLDISMYTEQTEPETGIIKFKAYGEKQGSLHGHPISTPYMTKDFLQQKRFQAQSNGTTYVYDVPDMFRQMTERHWREFSKARPTVDIRTPDKILIECKELVLEGDNLVEMQRLPGENNCGMVAWRIVLATPEYPNGREIIVIANDLTYLIGSFGIKEDVLFAKASQLARQLKVPRIYISVNSGARIGLAEEVKAMFKIAWEDPEEPDKGFKYLYLSTEDYAQVANLNSVRAILIEDEGEQRYKITDIIGKDDGLGVENLRYAGLIAGETSQAYEEIVTIAMVTCRTIGIGSYVVRLGQRVIQIDNSHIILTGYAALNKLLGRKVYASNNQLGGTQIMFNNGVTHKTEAIDLDGVYTILDWLSYIPAYIGCDLPIVLPNDRIERPVDFMPTKSPYDPRWMLGGRVNPVNANDWENGFFDRDSWSEIMASWAKTVVTGRARLGGVPVGVIAVETRTVEVEMPADPANLDSEAKTLQQAGQVWYPDSSYKTAQAIKDFGREELPLIVFANWRGFSGGMKDMYEQIVKFGAYIVDGLREYKKPVLIYLPPNAELRGGAWAVLDSLINPRYMETYADPEARGGVLEPEGIVEIKYKEKDLVKTIHRLDPTTIALKKELDEANASGDKVRAAQVDEKIKARIAVLMHVYHTVAVHFADLHDTPERMLEKECISEIVPWRDSRRWLYWRLRRLLLEDAYIKKILRAQDNLSVGQAKQMLRRWLVEEKGATEAYLWDKNEEMVSWYEEQINAESIVSRNVNSVRRDAIISTISKMLEDCPDVALDAVVGLCQGLTPVNRGVVVRTLAQMQLNEETSNSNQG
Protein: Integrin beta-6 (P18564)
Organism: Homo sapiens (Human)
Function: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalization of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion. ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17545607}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}.
Interaction partners:
- Integrin alpha-V
- Transforming growth factor beta-1 proprotein
- Fibronectin
- Integrin beta-1
- Integrin alpha-3
- Integrin alpha-2
- Integrin alpha-1
- Integrin alpha-4
- Integrin alpha-5
- Integrin alpha-10
Sequence:
MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC
Protein: Actin-related protein 7 (Actin-like protein ARP7) (Chromatin structure-remodeling complex protein ARP7) (SWI/SNF complex component ARP7) (Q12406)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP7 and ARP9 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex protein RSC58
- Regulator of Ty1 transposition protein 102
- SWI/SNF complex subunit SWI3
- Chromatin structure-remodeling complex subunit RSC9
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Chromatin structure-remodeling complex subunit RSC4
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit RSC7
Sequence:
MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAILERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLTLDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGTSHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYKLTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATN
Protein: Taste receptor type 2 member 105 (T2R105) (Taste receptor type 2 member 9) (T2R9) (Q9JKT5)
Organism: Rattus norvegicus (Rat)
Function: Gustducin-coupled cycloheximide receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 3
Sequence:
MLSAAEGILLSIATVEAGLGVLGNTFIALVNCMDWAKNKKLSKIGFLLFGLATSRIFIVWILILDAYAKLFFPGKYLSKSLTEIISCIWMTVNHMTVWFATSLSIFYFLKIANFSHYIFLWLKRRTDKVFAFLLWCLLISWAISFSFTVKVMKSNPKNHGNRTSGTHWEKREFTSNYVLINIGVISLLIMTLTACFLLIISLWKHSRQMQSNVSGFRDLNTEAHVKAIKFLISFIILFILYFIGVAVEIICMFIPENKLLFIFGLTTASVYPCCHSVILILTNSQLKQAFVKVLEGLKFSENGKDLRAT
Protein: Protein ecdysoneless (Q9W032)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required in both the follicle cells and the germline for oocyte development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15128659}.
Interaction partners:
- Protein AAR2 homolog
- Pre-mRNA-processing-splicing factor 8
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U5 small nuclear ribonucleoprotein TSSC4
- Protein ultraspiracle
- Ecdysone receptor
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MSKIPGSNLEFVREEDFVEYYIFPKIPDNVQDEGALRKLMLQIRNEISAIVREKSLERSYLWHKDEFQLQVRLGGAEERLLNEETNPEEEAELGDLPPHFHGVTHYGDNISDEWFVVYLLTEITRARGDCIARVSDSDGEFLLIEAADALPDWASPETCEQRVYLVGGHLQLLQNSAASSQDKPLTMAMAVQRIRMNPTLYRCSQEIQSCIDARLKEYQIAQPHFSIHRQVLELPHSAAQLLKQKPRLLSSAVRAFCERDSLDIKALRTMRYFPPEATRVRTNVRFTRCLYAMLSHQQYLPEKRLGWHLTDPVSEPERYKEQLLGLKLASGLEILATQAKRVEGQQLEDLPAWRSYLRSLLSKGYFRDNIEGSAEYQELLNKAKVYFRGNQERFRTASRAGAEILDLLLHPAEAASEELRDEENNLQPSDSDEWLNISAEDLDSMLQDRYGPKKLYKPNGQMNAEEFTKQLAEFLDRQSNYEGIEHRGLEEPELDSDDDEPPPQANGSTGLTAKVKKNPSMRKACQRNSVIQPEEPDSTHVRNFLDFVIPEDNWDSTSEMSDYADEDDMESNLNALSGGGSVFPLDRQIQSYMEQMDRELAQTSVGKSFHGKKKTAPQADEDDFDDIEDFEPININVNTLRNMMDSYQSQVGGAGPVSNLFSAMGVGMSAVEDKEQKDISESAV
Protein: Putative racemase protein (B3Q5L5)
Organism: Rhizobium etli (strain CIAT 652)
Interaction partners:
Sequence:
MKIDRMRVFMTRDKDRPRVIVALDTDDGLTGWGECYNHGPDKALPPLLDYLYGFISGQDPTRVEYLVNLLIQQSRFPPGALGLAAISALDHCLWDLAAKAANVPVYKLLGGEVRDRIKVYAGVYTAPDAPAARDEFDRLKEGWGFTAFKLSPWRIDMHSNRWGNVVKASADYFRSLRETVSDEYEIAFDAHAKIFEPIAARQLGNALAPYDPLFFEEPLRPENIEAWGDLKQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPMGPLATAVNVHFSAAAQNFRILEYRLPKGQAYVYGGLDVETRQGETRYVVDPYLPKDGYLELRPDRPGWGVEMDEKAMEAEGYIHWQRRVPKRPDGSYAFA
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (A0A8I6A4L5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATGLGEPIYGLSEEEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSEQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRSTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEASEGGGEGPEPWETISEEVNMAGDSLSLALPPPPASPVSRTSPQELSEELSRRLQITPDSNGEQFSALIQREPSSRLRSCSVTDTVAEQAHLPPPSTPTRRARSSTVTGGEESTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEGAKDSPIRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKASLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
Protein: Protein DEHYDRATION-INDUCED 19 homolog 3 (AtDi19-3) (Q84J70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000269|PubMed:16786289}.
Interaction partners:
- Cysteine proteinase inhibitor 2
- CBL-interacting serine/threonine-protein kinase 11
Sequence:
MDSDSWSDRLASATRRYQLAFPSRSDTFLGFEEIDGEEEFREEFACPFCSDYFDIVSLCCHIDEDHPMEAKNGVCPVCAVRVGVDMVAHITLQHANIFKMHRKRKPRRGGSYSTLSILRREFPDGNFQSLFGGSSCIVSSSSSSNVAADPLLSSFISPIADGFFTTESCISAETGPVKKTTIQCLPEQNAKKTSLSAEDHKQKLKRSEFVRELLSSTILDDSL
Protein: NADH dehydrogenase subunit 4L (Q8HCN5)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase subunit 2
- NADH dehydrogenase iron-sulfur protein 2
- NAD
- NADH-ubiquinone oxidoreductase chain 5
- Orf183 protein
- NAD
- NAD
Sequence:
MDLIKYFTFSMIIFILGIWGILLNRRNILIMLMSIELMLLAVNLNFLVFSVSLDDMMGQLFALLVLTVAAAESAIGLAIFVITFRVRGTIAVEFINCIQG
Protein: Hexokinase-2 (EC 2.7.1.1) (Hexokinase PII) (Hexokinase-B) (P04807)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Interaction partners:
- Glucokinase-1
- Glucose-6-phosphate isomerase
- Hexokinase-1
- Regulatory protein MIG1
- ATP-dependent 6-phosphofructokinase subunit alpha
- High glucose sensor RGT2
- Invertase 2
- Low glucose sensor SNF3
- Glucose-6-phosphate 1-dehydrogenase
- Carbon catabolite-derepressing protein kinase
Sequence:
MVHLGPKKPQARKGSMADVPKELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDAMRTTQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSAPMAINCEYGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKAANALKDIYGWTQTSLDDYPIKIVPAEDGSGAGAAVIAALAQKRIAEGKSVGIIGA
Protein: Isoaspartyl peptidase/L-asparaginase (EC 3.4.19.5) (EC 3.5.1.1) (Asparaginase-like protein 1) (Asparaginase-like sperm autoantigen) (Beta-aspartyl-peptidase) (Glial asparaginase) (Isoaspartyl dipeptidase) (L-asparagine amidohydrolase) [Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain] (Q8VI04)
Organism: Rattus norvegicus (Rat)
Function: Has both L-asparaginase and beta-aspartyl peptidase activity. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:12753071}. Note=Midpiece of sperm tail.
Interaction partners:
- Asparagine synthetase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Adenylosuccinate synthetase isozyme 2
- Amine oxidase
- Argininosuccinate synthase
- Aspartoacylase
- Adenylosuccinate synthetase isozyme 1
- Multifunctional protein CAD
- Amine oxidase
Sequence:
MATARPSSCGRDSVPATPRASIDVSLVVVVHGGGASNISPGRKELVSEGIAKAATEGYNILKAGGSAVDAVEGAVTMLENDPEFNAGYGSVLNADGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGRGAEKFAADMGIPQTPAEKLITERTKKHLEKEKLEKGAQKADCPKNSGTVGAVALDCKGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVDEAATLALDYMKSKLKGLGGLILINKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETKTRNLPTC
Protein: Protein ERP2 (P39704)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in vesicular protein trafficking.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- Protein ERP4
- Protein ERP1
- Endosomal protein P24B
- Protein ERP6
- Protein ERP5
- ER-derived vesicles protein ERV29
- Endoplasmic reticulum chaperone BiP
- Protein EMP47
- ER-derived vesicles protein ERV14
Sequence:
MIKSTIALPSFFIVLILALVNSVAASSSYAPVAISLPAFSKECLYYDMVTEDDSLAVGYQVLTGGNFEIDFDITAPDGSVITSEKQKKYSDFLLKSFGVGKYTFCFSNNYGTALKKVEITLEKEKTLTDEHEADVNNDDIIANNAVEEIDRNLNKITKTLNYLRAREWRNMSTVNSTESRLTWLSILIIIIIAVISIAQVLLIQFLFTGRQKNYV
Protein: Protein rogdi homolog (Leucine-zipper-containing LZF) (Q3TDK6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
Interaction partners:
- DmX-like protein 2
- DmX-like protein 1
- S-phase kinase-associated protein 1
- WD repeat-containing protein 7
Sequence:
MATAMAASAAERAVLEEEFRWLLHAEVHAVLRQLQDILKEASLRFTLPGPSTEGPAKQENFILGSCGTDQVKGTLTLQGDALSQADVNLKMPRNNQLLHLAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFKTGAEVLKLMDAVMLQLTRARSRLTTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHALQPTSTKNFRPAGGAVLHSPGAMFEWGSQRLEVSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKIAVFSSYWSSRPF
Protein: Nucleoside diphosphate kinase II, chloroplastic (NDK II) (NDP kinase II) (NDPK II) (NDPK Ia) (EC 2.7.4.6) (O64903)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. May activate MPK3 and MPK6. May be involved in the regulation of cellular redox state and hydrogen peroxide-mediated MAP kinase signaling.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Mitogen-activated protein kinase 3
- Thymidylate kinase
- Mitogen-activated protein kinase 6
- Inosine triphosphate pyrophosphatase
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 1
- UMP kinase
- Guanylate kinase 2
- At5g66005
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
Sequence:
MVGATVVSKWTPLCVASPPERNSASLNPHCSPARVNFRTALAAFRPQFRLFSRNSASRRRLRASSSAESGIFLPHLVASMEDVEETYIMVKPDGIQRGLVGEIISRFEKKGFKLIGLKMFQCPKELAEEHYKDLSAKSFFPNLIEYITSGPVVCMAWEGVGVVASARKLIGKTDPLQAEPGTIRGDLAVQTGRNIVHGSDSPENGKREIGLWFKEGELCKWDSALATWLRE