wanglab/gogpt-training-data huggingface dataset:
Protein: Sperm-egg fusion protein Juno (Folate receptor 4) (Folate receptor delta) (FR-delta) (Folate-binding protein 3) (IZUMO1 receptor protein JUNO) (Q9EQF4)
Organism: Mus musculus (Mouse)
Function: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:27309808}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:24739963}. Note=GPI-anchored at the oolemma. {ECO:0000269|PubMed:24739963}.
Interaction partners:
- Izumo sperm-egg fusion protein 1
- Folate receptor alpha
- Folate receptor beta
- Glutamate carboxypeptidase 2
Sequence:
MAQWWQILLGLWAVLPTLAGDKLLSVCMNSKRHKQEPGPEDELYQECRPWEDNACCTRSTSWEAHLEEPLLFNFSMMHCGLLTPACRKHFIQAICFHECSPNLGPWIQPVVPNGQEEQRVWGVPLCQEDCEDWWRACHSSLTCKSNWLHGWDWSEEKKHCPAHEPCLPFSYHFPTPDDLCEKIWNNTFKASPERRNSGRCLQKWFEPTLSNPNVEVALHFAGSALAPQLSYTLPAFSLCLLFHP
Protein: Direct IAP-binding protein with low pI (A0A8I6A7T3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAALRSWMTRSVTFLFRYGQRFPVSANSKKRCFSELIRPWHKTMLTGFGVTLCAVPIAQKSEPQSLSNEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLVSLYRQYTSLLGKMNSQEEDEVWQVIIGARVEVSGPVSHFQSALHYCN
Protein: Biopterin-dependent aromatic amino acid hydroxylase family profile domain-containing protein (Q2V4U7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MIANLPDHTRIKHLETRDSQDGSSKTMDVLLEIELFHYGKQEAMDLMRLNGLDVHEVSSTIRPTAIKEQYTEPGSDDATTGSEWFPKSIYDLDICAKRVIMYGAGLDADHPGFKDTEYRQRRMMFAELALNYKHGEPIPRTEYTSSERKTWGIIYRKLRELHKKHACKQFLDNFELLERHCGYSENNIPQLEDICKFLKAKTGFRVRPVAGYLSARDFLAGLAYRVFFCTQYVRHHADPFYTPEPDTVHELMGHMALFADPDFAQFSQEIGLASLGASEEDLKKLATLYFFSIEFGLSSDDAADSPVKENGSNHERFKVYGAGLLSSAGELQHAVEGSATIIRFDPDRVVEQECLITTFQSAYFYTRNFEEAQQKLRMFTNNMKRPFIVRYNPYTESVEVLNNSRSIMLAVNSLRSDINLLAGALHYIL
Protein: Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Rab geranyl-geranyltransferase subunit alpha) (Rab GG transferase alpha) (Rab GGTase alpha) (Rab geranylgeranyltransferase subunit alpha) (Q92696)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Rab proteins geranylgeranyltransferase component A 2
- Rab proteins geranylgeranyltransferase component A 1
- Ras-related protein Rab-1A
- Ras-related protein Rab-31
- Ras-related protein Rab-32
- Ras-related protein Rab-7b
- Ras-related protein Rab-1B
- Ras-related protein Rab-9B
- Ras-related protein Rab-27A
Sequence:
MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVPPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPEDVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRADPQDALRCLHVSRDEACLTVSFSRPLLVGSRMEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTAGDVQKECVLLKGRQEGWCRDSTTDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFLLENSVLKMEYAEVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGNPLCQAVGILEQLAELLPSVSSVLT
Protein: FERM domain-containing protein 4A (Q8BIE6)
Organism: Mus musculus (Mouse)
Function: Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex. Plays a redundant role with FRMD4B in epithelial polarization. May regulate MAPT secretion by activating ARF6-signaling (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Colocalized with CYTH1 at adherens junction and tight junction (PubMed:20080746). Colocalized with PARD3 during the process of epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:20080746}.
Interaction partners:
- Cytohesin-1
Sequence:
MTEGRRCQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSGPVVLYFCVRFYIESISYLKDNATIELFFLNAKSCIYKELIDVDSEVVFELASYILQEAKGDFSSNEVVRSDLKKLPALPTQALKEHPSLAYCEDRVIEYYKKLNGQTRGQAIVNYMSIVESLPTYGVHYYAVKDKQGIPWWLGLSYKGIFQYDYHDKVKPRKIFQWRQLENLYFREKKFSVEVHDPRRASVTRRTFGHSGIAVHTWYACPALIKSIWAMAISQHQFYLDRKQSKSKIHAARSLSEIAIDLTETGTLKTSKLANMGSKGKIISGSSGSLLSSGSQESDSSQSAKKDMLAALKSRQEALEETLRQRLEELKRLCLREAELTGKLPVEYPLDPGEEPPIVRRRIGTAFKLDEQKILPKGEEAELERLEREFAIQSQITEAARRLASDPNVSKKLKKQRKTSYLNALKKLQEIENAINENRIKSGKKPTQRASLVIDDGNIASEDSSLSDALVLEDEDSQVTSTISPLQSPHKGLPPRPPSSHNRPPPPQSLEGLRQLHYHRTDYDKSPLKPKMWSESSLDEPYEKVKKRSSHGHSSSHKRFPSTGSCTEAGVSSSLQNSPIRSLPHWNSQSSMPSTPDLRVRSPHYVHSTRSVDISPTRLHSLALHFRHRSSSLESQGKLLGSENDTGSPDFYTPRTRSSNGSDPMDDCSSCTSHSSSEHYYPAQMNANYSTLAEDSPSKARQRQRQRQRAAGALGSASSGSMPNLAARSGAASTGGGVYLHSQSQPSSQYRIKEYPLYIEGSATPVVVRSLESDQEGHYSVKAQFKTSNSYTAGGLFKESWRGGGDEGDAGRLTPSRSQILRTPSLGRDGAHDKGSGRAAVSDELRQWYQRSTASHKEHSRLSHTSSTSSDSGSQYSTSSQSTFVAHSRVTRMPQMCKATSAALPQSQRSSTPSSEIGATPPSSPHHILTWQTGEATENSPIMDGSESPTHQSTDE
Protein: Metaxin-1 (Mitochondrial outer membrane import complex protein 1) (A0A0G2JU49)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
- Sorting and assembly machinery component 50 homolog
- Metaxin-2
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM40B
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
- DnaJ
- Large ribosomal subunit protein uL2m
- Large ribosomal subunit protein mL37
Sequence:
MRLGGPPRNVRSGQRFERSRCSRGHVQFGKSPQRPLSRTRCPSSKPCLSPAVRGYARQRHRESPKRAWTAALLPYGGRLRTSPRRSSEGQCSTSSSAAASPAARSHASLDLKLRVATQAETRGCSSWREKADAYERVLPGQRMCKMAAPMELFCWSGGWGLPSVDLDSLAVLTYTRFTCAPLKVHKISNPWQSPSGTLPALRTSSGKVITEPHKIITHLRKEKYNADYDLSARQGADTLAFISLLEEKLLPMLIHTFWIDAKNYVEVTRKWYAEAMPFPLNFFLPGRMQRRHMERLQLLCGEHRLESEEELEKELYQEARECLTLLSHRLGSRKFFFGDAPASLDAFVFSHLVLLLQAKLPSGKLQAHLRGLQNLCVYCTHILNLYFPRDATDVPPPPCQTPAGPETEEEPYRRRTQILSVLAGLAAMVGYALLSGIVSIQRASPARAPCTQALDLAEEDEED
Protein: AT24801p (Q8T3Z3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRGVAIQRGHVGVVGATPYHHPHHPHHHPALLAASAAAAQQQQQRQLAAAAVATAAVAQQQQQQQQAVVQQQQQQVAAAAQQQHQQQQQQQQQAVQQQQAVQQQQQHQQQQQQQQQQHAAVAAAAAAASHPHMHAAHAHAHAHALGPQLAQLQAVAVPTAASNAAALQQSLAAAIQNPSGNPNAAAAAAAYAARLSAATGATQSPQTAAAAAAAASMAASANAANNAAALHGFAPVYYDPFLAAAASADPNLRFQICARICRSLSRTWHWTSSWIRGYHVPRWIQSFHAILRTIYASQPNNALELLSMKMLNI
Protein: Uncharacterized protein C8E11.06 (O42883)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MLLVSRNICRIKGNTIDWRNLKKDLSMTWIILK
Protein: RNA helicase (EC 3.6.4.13) (C9J081)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEIGRPRKDTWKLANLDLNSEKQSGGASTASKGRYIPPHLRNREASKGFHDKDSSGWSCSKDKDAYSSFGSRDSRGKPGYFSERGSGSRGRFDDRGRSDYDGIGNRERPGFGRFERSGHSRWCDKSVEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAVK
Protein: Sodium- and chloride-dependent GABA transporter 2 (GAT-2) (Solute carrier family 6 member 13) (P31646)
Organism: Rattus norvegicus (Rat)
Function: Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA). Mediates transport of taurine and is the major taurine transporter in hepatocytes. Can also mediate transport of beta-alanine and hypotaurine (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22896705}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P31649}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium- and chloride-dependent GABA transporter 3
- Cytosolic arginine sensor for mTORC1 subunit 2
Sequence:
MDNRVSGTTSNGETKPVCPVMEKVEEDGTLEREQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLIFLFTCGIPVFFLETALGQYTNQGGITAWRKICPIFEGIGYASQMIVSLLNVYYIVVLAWALFYLFSSFTTDLPWGSCSHEWNTENCVEFQKTNNSLNVTSENATSPVIEFWERRVLKISDGIQHLGSLRWELVLCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLVVLLIRGVTLPGAAQGIQFYLYPNITRLWDPQVWMDAGTQIFFSFAICLGCLTALGSYNKYHNNCYRDCVALCILNSSTSFVAGFAIFSILGFMSQEQGVPISEVAESGPGLAFIAYPRAVVMLPFSPLWACCFFFMVVLLGLDSQFVCVESLVTALVDMYPRVFRKKNRREILILIVSVVSFFIGLIMLTEGGMYVFQLFDYYAASGMCLLFVAIFESLCVAWVYGASRFYDNIEDMIGYKPWPLIKYCWLFFTPAVCLATFLFSLIKYTPLTYNKKYTYPWWGDALGWLLALSSMVCIPAWSIYKLRTLKGPLRERLRQLVCPAEDLPQKSQPELTSPATPMTSLLRLTELESNC
Protein: Palmitoyl thioesterase CPT1C (EC 3.1.2.22) (Carnitine O-palmitoyltransferase 1, brain isoform) (CPTI-B) (Carnitine palmitoyltransferase 1C) (Carnitine palmitoyltransferase I) (CPT I-C) (Q8BGD5)
Organism: Mus musculus (Mouse)
Function: May play a role in lipid metabolic process.
Subcellular location: Synapse {ECO:0000305|PubMed:22632720}. Cell projection, axon {ECO:0000269|PubMed:25751282}. Cell projection, dendrite {ECO:0000269|PubMed:22539351, ECO:0000269|PubMed:25751282}. Cell projection, dendritic spine {ECO:0000269|PubMed:22539351}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22539351, ECO:0000269|PubMed:25751282}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000269|PubMed:25751282}.
Interaction partners:
- Acetyl-CoA carboxylase 2
- Glutamate receptor 1
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Monoacylglycerol lipase ABHD6
- Phosphatidylinositol-3-phosphatase SAC1
- Glutamate receptor 2
- Glutamate receptor 3
- Protein-serine O-palmitoleoyltransferase porcupine
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-2 subunit
Sequence:
MAEAHQASSLLSSLSSDGAEVELSSPVWQEIYLCALRSWKRHLWRVWNDFLAGVVPATPLSWLFLFSTIQLACLLQLDPSLGLMEKIKELLPDWGGQHHQLQGFLSAAVFASCLWGALIFTLHVALRLLLSHHGWLLEPHGAMSSPTKTWLALVRIFSGRHPRLFSFQRALPRQPVPSAQETVRKYLESVRPVLGDDAFDRATALANDFLRLHAPRLQLYLQLKSWCTSNYVSDWWEEFVYLRSRGSLINSTYYMMDFLYVTPTPLQAARAGNAVHTLLLYRHLLNRQEISPTLLMGMRPLCSAQYERMFNTTRIPGVEKDHLRHLQDSRHVAVFHRGRFFRVGTHSPNGLLSPRALEQQFQDILDDPSPACPLEEHLAALTAAPRSMWAQVRESVKTHAATALEAVEGAAFFVSLDSEPAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPVSGHLWEFTLATECFQLGYATDGHCKGHPDPTLPQPQRLQWDLPEQIQPSISLALRGAKTLSGNIDCHVFPFSHFGKSFIKCCHVSSDSFIQLVLQLAHFRDRGQFCLTYESAMTRLFLEGRTETVRSCTREACQFVRAMDNKETDQHCLALFRVAVDKHQALLKAAMSGQGIDRHLFALYIMSRLLHMQSPFLTQVQSQQWLLSTSQVPVQQTHLIDVHNYPDYVSSGGGFGPAHDHGYGISYIFMGENAITFHISSKKSSTETDSHRLGQHIENALLDVASLFRVGQHFKRQFRGENSDYRYNFLSCKTVDPNTPTSSTNL
Protein: Choline/ethanolamine kinase, putative (EC 2.7.1.82) (Q57W59)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ethanolamine kinase
- Ethanolamine-phosphate cytidylyltransferase
- Raptor N-terminal CASPase-like domain-containing protein
- Raptor N-terminal CASPase-like domain-containing protein
- Ethanolaminephosphotransferase, putative
- Uncharacterized protein
Sequence:
MALRPFPLGNTPLHAVIRRSAREFECVEAVPASNAVRSPSTASWVSAESLDSIISLANRTSEEMEVDQLIYRLCRSLYHVAKKKSAQIHCHPNHQERQQQQQQASSSGWRSVECEGHFSNMRGREDWCPLLHLFDPRSYYKVMGQPSQHDGCKLCGDVVGTESSPEGVSQWLMSELSVTRLTGGNSNHVYRLGHASFPKKAVLLRVYGDGGGGDVIDRARDIKVMRLMSKSEMGPGLLHTFHWGRVEEFMDGVLTCTTEKLLTSPSLLADVYGGLSKMHQLDYTPLLPENMRTKGMSNGHNSSQSVSDTVSKSGGGQEGPDGTVGGVNELESTCHTSFERVCLRLLRLVSLNVVEEHRHSLESWLAGEVMFVRRELQYRGIPVVLSHNDLNPGNILLSDGAGEASGTVFSDEELRVENTPLSKRYVTRKGKNMNLVERRGFLFIDFEYADANYRCFDLGNTLCELDYDYTRGTEAGGRGFIKYLFVFPPPAMEEAWRGLGEEYPRMPELIYDAWRRGVCDGSSDIGSVALLAVRRYFAERDNVPLETVELSEAQVGEVLLGMLASHLYWTIWSMTMGSAPDNCVECEDCDDQMFAVGGSGLDYMRYGECRLREYIALRGWLAEKGLLS
Protein: Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (SMAD family member 2) (SMAD 2) (Smad2) (O70436)
Organism: Rattus norvegicus (Rat)
Function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 or with IPO7 (By similarity). On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (By similarity). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (By similarity). {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
Interaction partners:
- E3 ubiquitin-protein ligase
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 4
- TGF-beta receptor type-1
- Forkhead box protein H1
- Zinc finger FYVE domain-containing protein
- TGF-beta receptor type-2
- Forkhead box O3
- TGFB-induced factor homeobox 1
- Catenin beta-1
Sequence:
MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFSLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
Protein: Protamine (Q24402)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSNNVNECKSLWNGIISISAKDESPKGLTEMCNHPKRRAPPKCKPMKSCAKPRRKRACAKATRPKVKCAPSQKCSKQGPVTNNAYLNFVRFFRKKHCDLKPQELIAEAR
Protein: Adenylate kinase 4, mitochondrial (EC 2.7.4.4) (EC 2.7.4.6) (Adenylate kinase 3-like) (GTP:AMP phosphotransferase AK4) (P27144)
Organism: Homo sapiens (Human)
Function: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. Plays a role in controlling cellular ATP levels by regulating phosphorylation and activation of the energy sensor protein kinase AMPK. Plays a protective role in the cellular response to oxidative stress.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03170, ECO:0000269|PubMed:11485571, ECO:0000269|PubMed:19766732, ECO:0000269|PubMed:26980435}.
Interaction partners:
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Nucleoside diphosphate kinase, mitochondrial
- Deoxycytidine kinase
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Cancer-related nucleoside-triphosphatase
- Thiamine pyrophosphokinase 1
- Ectonucleoside triphosphate diphosphohydrolase 2
Sequence:
MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEKSLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLKDRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKPVIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY
Protein: alpha-amylase (EC 3.2.1.1) (Q8N0Q9)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGLLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAWL
Protein: Stardust, isoform P (EC 2.7.4.8) (X2JIZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQANSSRSNLSAQSSGTPSASTISSSQGKQQVVELSGYVIILVENVEGKIKLYGSPPDRDNLEVGDEILEVNGLTLENISRTEVIRHIHDCIKSCTICLRVRKKNDSRLAWDIGNSVQDAFVIAVEEHARERLQRLAALNRVTPVDITQLSKKLLEDVIVHQASDVHSYSTSASAAAIASSSNRSQQQQQQQQQHQLLSAAYELQQQQQLQLQQQQQQQNSPTSSISIGRTELLLGDQSLRQDPRGNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQLNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: Transcription termination factor MTERF4, chloroplastic (Mitochondrial transcription termination factor 4) (B6TGN4)
Organism: Zea mays (Maize)
Function: Transcription termination factor required for processing and steady-state levels of plastid transcripts. Required for splicing of the chloroplastic group II intron. Required for the accumulation of 16S and 23S ribosomes.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:24500208}.
Interaction partners:
- Chloroplast RNA splicing1
- CRS2-associated factor 2, chloroplastic
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- Small ribosomal subunit protein uS12cz/uS12cy
Sequence:
MMKSLLFSAHPTSLLLPAPRLRRLLRLRAASSASASAPPRADRRSPGTPSRRPSSSLYARPSLLDMERDRATRRADVDAFLTSLGVDPGELAGLELPVTVDVMRERAEFLGSLGLTQEDLAAYPLALGCSVRKNMVPVLDYLGKLGVRRDALPDLLRRYPQVLHASVVVDLAPVVKYLQGMDVRPTDVPRVLERYPELLGFKLEGTMSTSVAYLVGIGVGRRQVGSVITRFPEVLGMRVGKIIKPFVEHLEGIGLQRLAIARIIEKKPYVLGFGLQEKVKPNIEALVDIGVRKEALASIVMQYPDVLGLELRDKLVAQQSLFESSILVSREDFGRVLERMPQAISLGRAAVLKHVNFLTACGFMLSQVSKMVVACPQLLALNIDIMRMNFEYFKNEMERDLEELVEFPAFFTYGIESTVRPRHEMVSRKGLTCSLAWLLNCSDAKFDERMKYDTIGVEEMEREDSSDMNASVDEVESEEYEDSDYGDSDDEFVR
Protein: Nudix hydrolase 9 (AtNUDT9) (EC 3.6.1.-) (Q8VYR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Interaction partners:
- Nudix hydrolase 25
- Nudix hydrolase 5
- Nudix hydrolase 11
- Nudix hydrolase 1
- Nudix hydrolase 10
- Nudix hydrolase 4
- Nudix hydrolase
- Nudix hydrolase 20, chloroplastic
- Nudix hydrolase 2
- Heavy metal-associated isoprenylated plant protein 20
Sequence:
MAKLAEEMNPEGSRYQLLLSCPSGLSPSQVSVDFSKSHDRIPRQDPGLEDSISQVWEQRSQGNSSLFNGQKFRYGGYCLDDDDGSTNEVPHVCLRLGLTDYRTFVGTNLSSLWEKFLVTSEDDSVRCRHTSSPLGNGAVIETSDKKIIVLRRSNNVGEFPGHYVFPGGHPEPTAVGIDYHQLENNVQTGEVLNKKVTQEMFDSIICEVVEETGIPASSLSSPLFIGISRRELNVRPAMFFYLKCSHHSDDIQRLYSSAEDGFESTQLHTVSLDELKMMTSRMPGCHHGGFALYELMLQRLKNTKETSLIAT
Protein: Cis-zeatin O-glucosyltransferase 1 (cisZOG1) (EC 2.4.1.215) (Q93XP7)
Organism: Zea mays (Maize)
Function: Utilizes UDP-glucose as the sugar donor and catalyzes the formation of O-beta-D-glucosyl-cis-zeatin from cis-zeatin. May regulate active versus storage forms of cytokinins and could have an impact on seed growth.
Interaction partners:
Sequence:
MAVDTMESVAVVAVPFPAQGHLNQLLHLSLLLASRGLSVHYAAPPPHVRQARARVHGWDPRALGSIRFHDLDVPPYDSPAPDLAAPSPFPNHLMPMFEAFAAAARAPLAALLQRLSTSYRRVAVVFDRLNPFAATEAARLANADAFGLQCVAISYNVGWLDPGHRLLSDYGLQFLPPDACMSREFVDLVFRMEEEEQGAPVAGLVMNTCRALEGEFLDVVAAQPPFQGQRFFAVGPLNPLLLDADAPTTPPGQARHECLEWLDRQPPESVLYVSFGTTSCLHADQVAELAAALKGSKQRFVWVLRDADRADIYAESGESRHAMFLSEFTRETEGTGLVITGWAPQLEILAHGATAAFMSHCGWNSTIESLSHGKPVLAWPMHSDQPWDSELLCKYFKAGLLVRPWEKHAEIVPAQAIQKVIEEAMLSDSGMAVRQRAKELGEAVRASVADGGNSRKDLDDFIGYITR
Protein: Cone transducin alpha subunit (Guanine nucleotide-binding protein (G protein), alpha transducing activity polypeptide 2) (Guanine nucleotide-binding protein G(T) subunit alpha-2) (Q90WX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Gnb1l protein, beta polypeptide 1, like), beta polypeptide 1b isoform X1), beta polypeptide 1b)
- Regulator of G-protein signaling 9a
- Rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Green-sensitive opsin-2
- Gnb3 protein, beta polypeptide 3), beta polypeptide 3b)/G
- Rhodopsin
- Regulator of G-protein signaling 9
- Green-sensitive opsin-4
Sequence:
MGSGASAEDKEMAKKSKELEKQLQEDADKEAKTVKLLLLGAGESGKSTIVKQMKILHQGGYTKEEQMEFRSIIFGNILQSALAIIRGMEMLSINFGSPSAQEDSQKLQNLSDSIEEGTMPPELADVIKRLWKDAGVQASFDRAAEYQLNDSAGYYLNEMDRICKPDYLPTEQDVLRSRVKTTGIIEEQFGCKELHFRMFDVGGQRSERKKWIHCFEGVTCIIFCGALSAYDMVLVEDDEVNRMHESLHLFNSICNHRFFATTSIVLFLNKKDLFQEKIKKVHLSICFPDYDGPNTYEDASNYIKTQFQDLNMKKGVKEIYSHMTCATDTKNVEIVFNAVTDIIIKENLKDCGLF
Protein: Izumo sperm-egg fusion protein 4 (Sperm 22 kDa protein c113) (Q1ZYL8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Izumo sperm-egg fusion protein 3
- Izumo sperm-egg fusion protein 2
- Izumo sperm-egg fusion protein 1
Sequence:
MALLLCLVCLTAALAHGCLHCHSNFSKKFSFYRHHVNFKSWWVGDIPVSGALLTDWSDDTMKELHLAIPAKITREKLDQVATAVYQMMDQLYQGKMYFPGYFPNELRNIFREQVHLIQNAIIESRIDCQHRCGIFQYETISCNNCTDSHVACFGYNCESSAQWKSAVQGLLNYINNWHKQDTSMRPRSSAFSWPGTHRATPAFLVSPALRCLEPPHLANLTLEDAAECLKQH
Protein: Bacterial microcompartment shell vertex protein EutN (Ethanolamine catabolic microcompartment shell protein EutN) (Ethanolamine utilization protein EutN) (P41792)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Probably forms vertices in the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC. Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. It may be involved in transporting positively charged molecules into and out of the BMC (By similarity).
Subcellular location: Bacterial microcompartment {ECO:0000250|UniProtKB:P0AEJ8}.
Interaction partners:
- Bacterial microcompartment shell protein EutK
- Bacterial microcompartment shell protein EutM
- Ethanolamine utilization protein EutJ
- Acetaldehyde dehydrogenase
- Bacterial microcompartment shell protein EutL
- Bacterial microcompartment shell protein EutS
- Bacterial microcompartment shell protein PduA
- Probable alcohol dehydrogenase EutG
- Ethanolamine ammonia-lyase reactivase EutA
- Bacterial microcompartment shell protein PduJ
Sequence:
MEADMKLAVVTGQIVCTVRHQGLAHDKLLMVEMIDAQGNPDGQCAVAIDSIGAGTGEWVLLVSGSSARQAHRSELSPVDLCVIGIVDEVVAGGKVVFHK