wanglab/gogpt-training-data huggingface dataset:
Protein: Histidinol dehydrogenase (HDH) (EC 1.1.1.23) (P9WNW9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Phosphoribosyl-AMP cyclohydrolase
- Histidinol-phosphate aminotransferase
- Phosphoribosyl isomerase A
- Imidazole glycerol phosphate synthase subunit HisH
- Imidazole glycerol phosphate synthase subunit HisF
- ATP phosphoribosyltransferase
- Phosphoribosyl-ATP pyrophosphatase
- Aromatic amino acid aminotransferase
- Histidinol-phosphatase
Sequence:
MTAPPPVLTRIDLRGAELTAAELRAALPRGGADVEAVLPTVRPIVAAVAERGAEAALDFGASFDGVRPHAIRVPDAALDAALAGLDCDVCEALQVMVERTRAVHSGQRRTDVTTTLGPGATVTERWVPVERVGLYVPGGNAVYPSSVVMNVVPAQAAGVDSLVVASPPQAQWDGMPHPTILAAARLLGVDEVWAVGGAQAVALLAYGGTDTDGAALTPVDMITGPGNIYVTAAKRLCRSRVGIDAEAGPTEIAILADHTADPVHVAADLISQAEHDELAASVLVTPSEDLADATDAELAGQLQTTVHRERVTAALTGRQSAIVLVDDVDAAVLVVNAYAAEHLEIQTADAPQVASRIRSAGAIFVGPWSPVSLGDYCAGSNHVLPTAGCARHSSGLSVQTFLRGIHVVEYTEAALKDVSGHVITLATAEDLPAHGEAVRRRFER
Protein: Large ribosomal subunit protein uL6A (60S ribosomal protein L9-A) (Q10232)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL37B
Sequence:
MGRDIYKDETLTIPKGVTVDIKARNVTVTGPRGTLKQNLRHVDIEMKKQGNTIKFIVWHGSRKHNACIRSVYSIINNMIIGVTQGFRYKMRLVYAHFPININLTENGTVVEIRNFLGERITRVIKCLPGVTVSISSAVKDEIILEGNSLENVSQSAANIKQICNVRNKDIRKFLDGIYVSERGNIEELEE
Protein: Riboflavin transporter RibJ (Riboflavin/flavin transporter) (Q57VW6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- FAD synthase
- riboflavin kinase
Sequence:
MLPSFTRKPADHPIGYLVALSGLLMQLMSYGIDNSYSIFSEDMHNDPSLGFPSITAISLGNSVSLGLSPAFGVLAGFCVDRLPPRFMMALSTILLFTGLWISSTLAANIYVVTFTYCLFASIGTACMLSPGAAATSSWFNRYQGLAMGINFAGGGIGSAIIPPLAGKWVVAYGWRKAFQLMSIFCAIGVLATALSARRREPKRDDSSADDETREGNKSGNGSLVRRSNEPATVGGEGAANNGHNEGKEDVREMGRKNGSHTNTSKVPPNGRGVGTNQQNGNDGEGLDVTEQSQRNNTFASAIDVDMDTSMDADEPQVIRSLHTHKLTPWELFLSMFTLPFMGNFLCWFIYSWAFYSLIYAAVPYISSMGKPGTVYAGVPPIPTDVAATLFTFYGVFQVVGSVLVGWLASLVTAEFAYVFCATVGGIGCGLLALGRSYVAFALLLCIIGFCMAGMFAVMPTLIATHLYGPNLGFYFGAVFLAGVVGGFVAPPMQATIQLRNNGSYAFVCVVMSVSMTLSALVCYATLWRSKRSGIVLAARKTKLVEIM
Protein: Small ribosomal subunit protein uS14 (40S ribosomal protein S29) (O74329)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL18A
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL14
Sequence:
MAHENVWFSHPRKYGKGSRQCAHTGRRLGLIRKYGLNISRQSFREYANDIGFVKYR
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial (Complex I-AGGG) (NADH-ubiquinone oxidoreductase AGGG subunit) (Q9Y6T4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
Sequence:
MESHERQPLVLHEEMGECRSSLSAGGGVHIEPRYRQFPQLTRSQVFQSEFFSGLMWFWILWRFWHDSEEVLGHFPYPDPSQWTDEELGIPPDDED
Protein: Kinetochore protein Nuf2-A (xNuf2) (Cell division cycle-associated protein 1-A) (Q8AWF4)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (By similarity). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (By similarity).
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores from late prophase to anaphase.
Interaction partners:
Sequence:
MDKLTFPIFPAADLVNFFRQNILTGTEAKNFNKNDIFPNPKPEMVQKLYMRILQQVFNYGVEQFYMVPMDLDIQYPHLVEGFAPVANILKLMARFLPMCRVYDFHPSDVLNPKGKRTLHSLSGIVNFLHFSATRKEVYFEYCSSYKSALENVRQLQKANQEAEIKIEKLTTVPPEQQAEFKALSSEIHDLQQIISQEYRAKDVAFQEKIAQRKTEFAEKNKRLNEQKLAIATMKEEQERMKSQIVESPEQRKSKTERMKETVHRLKQARQETNDKCDYYRDRVAFACMWQTDVQGYLKKLQGIDTNLEIHRKIREEIRHSEEQVVNLNLELKSLSNEDAQLKRIILVKKEKLAKVDIKNKKKQEDFNQQKQEILEVCSRIQEKRQVVHGRVAQVLQEIQQTIGKKEQLLETTEAGKKKCQEVITDFRAALEKYHDSLQKASERSADRRREKIAELNRRLSRR
Protein: CEntrosomal Protein (A2A266)
Organism: Caenorhabditis elegans
Interaction partners:
- Centriolar and ciliogenesis-associated protein hyls-1
- NePHronoPhthisis
- Nephrocystin-1-like protein
- B9 domain-containing protein 2
- MecKel-Gruber Syndrome
- Spindle-defective protein 2
- Rhodanese domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- B9 domain-containing protein 1
- C2 domain-containing protein
Sequence:
MSQLAAINYPQLEEFLQNDGPTEEEVRVWYDKLAEYEIEGSESPPEIELLYNGARYLMGFGFTAAEELRNVAEQEAVTMAEKEDQWEEQKTALNLEIESLRDRITSKADVGDSTEAFRAQIDSLKEENRQLQQSNRDRDREMADQRDRFENLASRVDTLTRERDALSEHKAQLEDTIRELNRRLSAKTEDTGAEWESKKLKLRNEQVLTISRQMQAVVSQNEELREEIDRVSYALEEATRIIEQSAVRYTEMTNKLEISQLRIEELFNQNRRLTQILPEELVEHVSQCISAAETMLSGRPIDKVNFLIEVGDLLAPKFLNEDDKKALEDATGLTEAEEQKEKLERAEDRVKGLQDELNAVVEESNKMRTMIREDRTGEKEQELEQLKKELVDATTLARNLFGEAMSEVPGQDPTMTLQMRILQLEHSIEQLNDEKEKQKKVMEELQFTIEQKDENNGEVLSELNRLKDAKFGSAREEITRLEKQMKFRDEQIGKLQQHCTLLQVELGRYAEGTYEPIVKPSLPRRIRRPDMLLATKTVKPEIQKIDSPVAPSSPLKPSPRVIEDEPRNAPNAPNPKEPPRFVHSGDYSDIAQQAVLISNLYYELMQLLEEISYKDEKLVEIHKSWKSTQKSYQEMKAQLEMAYGEIQSLKKENLMIEERTLEELKQTESVELQRLVESINVEGSEMERRLGEATRMLVTERMERMRFTRQCTILRTKTERLEEATRKSKEMLRTKELNAQRAIGRLKYEVETTTIEIGRLQTRLLQSVPTEEYDKLMRKYKRLIKETTGVETNNEEVMARQEMTVYAKSPVEAELEARENMLKKMIDVVSDQSDFWNQESAMLQAENEELKKFIEDVENESDLKSVLGAVERRLLSTIRELRENEREYLREKKKSRGNDIESSRDSERLRQERVALINVIIVLQRENKTLRDQAVGTVSLQQLELLRSNIFQARQKEAEIAAKMENIDKLKEESETEMLRIRALRTANEVLSNFDGHEMQPQGNNEVAERQLQLAYFTSSQQSAKAKQFERMVHLKEQRVAELNDEMRELKQWNLELITTLENIKTFKGERRESQHIKPEISLKPRESIAVDQLEDSMDKESDYEMDIKSETSSSEASSDRIIVRTIVQDNVDAFENRIKEIKASAQLAVQGYKEQLELKEIAIDRYKKLLREKIDEGVQIIEKVEIVHQEVEIPDRSTEEQLRKTEVKLKELESEMRKLKAKRAEIVKNDDEQDDVSERIERFKEFLDEEVQTEWEYPQVSSRLNNEEEVEQLPKSAKSEKVRRLEEEMQLLQELVAKSDSKDGENMRQKTEIRDLKARIQRLTKTNKELLVTCEQIKEDALAELSTFRRNNENSDERRMTDLRVELDRLRTTNRTLRNANEEMKNELSRLKQTVERRDTKNEPDEWERRKRQDEIIASLKEKLKKRDIAEKDYLEKLKKREMVIETMRNDQGLRSSEIERLQRKLKANDPSVIKLQLNKEWKEKLDVLEANITKKNEELTACNRTLLRLKSELETNRKRHASEIEKIRVDNNSNVQKEVKRAREEVKKAMTVIKPQMSTVEIQADLLEKRHSGSTKSHRSETVSHNKIELSTISSSSSSISSPASSSKSHRSKTLKSISRDSILEERRLSQKSFDEQPNIPAPKSDTSDYYQLRESLQMTQERLIESQEKLIQMERDYSSLHEKFDRLKLRFDRDEKPTGAVLVLSDKLAAKDREIAQLKNRIAHLQNTVHLPQ
Protein: Ceramide transfer protein (Collagen type IV alpha-3-binding protein) (A0A2R8Y5H3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLK
Protein: Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme (ATP:glutamine synthetase adenylyltransferase) (ATase) [Includes: Glutamine synthetase adenylyl-L-tyrosine phosphorylase (EC 2.7.7.89) (Adenylyl removase) (AR) (AT-N); Glutamine synthetase adenylyl transferase (EC 2.7.7.42) (Adenylyl transferase) (AT) (AT-C)] (P9WN27)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Interaction partners:
- Glutamine synthetase
- Glutamine synthetase
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Nitrogen regulatory protein P-II
- Glutamate synthase large chain
- Carboxylesterase B
- RNA polymerase-binding protein RbpA
- Serine protease Hip1
Sequence:
MVVTKLATQRPKLPSVGRLGLVDPPAGERLAQLGWDRHEDQAHVDLLWSLSRAPDADAALRALIRLSENPDTGWDELNAALLRERSLRGRLFSVLGSSLALGDHLVAHPQSWKLLRGKVTLPSHDQLQRSFVECVEESEGMPGSLVHRLRTQYRDYVLMLAALDLAATVEDEPVLPFTVVAARLADAADAALAAALRVAEASVCGEHPPPRLAVIAMGKCGARELNYVSDVDVIFVAERSDPRNARVASEMMRVASAAFFEVDAALRPEGRNGELVRTLESHIAYYQRWAKTWEFQALLKARPVVGDAELGERYLTALMPMVWRACEREDFVVEVQAMRRRVEQLVPADVRGRELKLGSGGLRDVEFAVQLLQLVHARSDESLRVASTVDALAALGEGGYIGREDAANMTASYEFLRLLEHRLQLQRLKRTHLLPDPEDEEAVRWLARAAHIRPDGRNDAAGVLREELKKQNVRVSKLHTKLFYQPLLESIGPTGLEIAHGMTLEAAGRRLAALGYEGPQTALKHMSALVNQSGRRGRVQSVLLPRLLDWMSYAPDPDGGLLAYRRLSEALATESWYLATLRDKPAVAKRLMHVLGTSAYVPDLLMRAPRVIQQYEDGPAGPKLLETEPAAVARALIASASRYPDPERAIAGARTLRRRELARIGSADLLGLLEVTEVCRALTSVWVAVLQAALDVMIRASLPDDDRAPAAIAVIGMGRLGGAELGYGSDADVMFVCEPATGVDDARAVKWSTSIAERVRALLGTPSVDPPLELDANLRPEGRNGPLVRTLGSYAAYYEQWAQPWEIQALLRAHAVAGDAELGQRFLRMVDKTRYPPDGVSADSVREIRRIKARIESERLPRGADPNTHTKLGRGGLADIEWTVQLLQLQHAHQVPALHNTSTLQSLDVIAAADLVPAADVELLRQAWLTATRARNALVLVRGKPTDQLPGPGRQLNAVAVAAGWRNDDGGEFLDNYLRVTRRAKAVVRKVFGS
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (H0YBH3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
XIKAQPFKDRCEWFYEHLHSGQPDSDMVHRPVNENDILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMGQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGAMEEVPLKPGGGSILVTQNNKELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDRLLVALHCGSYGYTMA
Protein: Phosphoinositide 3-kinase regulatory subunit 5 (L7RT34)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLTPLALLFYSTVLCTPHFPPDSDLLLKAASTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLPIRSHRSSTVTVLLLNPVEVQAEFLAVANKLSTPGHSPHSAYTTLLLHAFQATFGAHCDVPGLHCRLQAKTLAELEDIFTETAEAQELASGIGDAAEARRWLRTKLQAVGEKAGFPGVLDTAKPGKLHTIPIPVARCYTYSWSQDSFDILQEILLKEQELLQPGILGDDEEEEEEEEEVEEDLETDGHCAERDSLLSTSSLASHDSTLSLASSQASGPALSRHLLTSFVSGLSDGMDSGYVEDSEESSSEWPWRRGSQERRGHRRPGQKFIRIYKLFKSTSQLVLRRDSRSLEGSSDTALPLRRAGSLCSPLDEPVSPPSRAQRSRSLPQPKLGTQLPSWLLAPASRPQRRRPFLSGDEDPKASTLRVVVFGSDRISGKVARAYSNLRRLENNRPLLTRFFKLQFFYVPVKRSHGTSPGACPPPRSQTPSPPTDSPRHASPGELGTTPWEESTNDISHYLGMLDPWYERNVLGLMHLPPEVLCQQSLKAEAQALEGSPTQLPILADMLLYYCRFAARPVLLQVYQTELTFITGEKTTEIFIHSLELGHSAATRAIKASGPGSKRLGIDGDREAVPLTLQIIYSKGAISGRSRWSNLEKVCTSVNLNKACRKQEELDSSMEALTLNLTEVVKRQNSKSKKGFNQISTSQIKVDKVQIIGSNSCPFAVCLDQDERKILQSVVRCEVSPCYKPEKSDLSSPPQTPPDLPAQAAPDLCSLLCLPIMTFSGALP
Protein: U11/U12 small nuclear ribonucleoprotein 48 kDa protein (U11/U12 snRNP 48 kDa protein) (U11/U12-48K) (Q6IEG0)
Organism: Homo sapiens (Human)
Function: Likely involved in U12-type 5' splice site recognition.
Subcellular location: Nucleus {ECO:0000269|PubMed:15146077}.
Interaction partners:
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Zinc finger matrin-type protein 5
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- Zinc finger CCHC-type and RNA-binding motif-containing protein 1
- Small nuclear ribonucleoprotein F
- U11/U12 small nuclear ribonucleoprotein 25 kDa protein
- RNA-binding region-containing protein 3
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein E
- Programmed cell death protein 7
Sequence:
MEGEPPPVEERRRLQEELNEFVESGCRTLEEVTASLGWDLDSLDPGEEEAAEDEVVICPYDSNHHMPKSSLAKHMASCRLRKMGYTKEEEDEMYNPEFFYENVKIPSITLNKDSQFQIIKQARTAVGKDSDCYNQRIYSSLPVEVPLNHKRFVCDLTQADRLALYDFVVEETKKKRSDSQIIENDSDLFVDLAAKINQDNSRKSPKSYLEILAEVRDYKRRRQSYRAKNVHITKKSYTEVIRDVINVHMEELSNHWQEEQEKAEDDAEKNEERRSASVDSRQSGGSYLDAECSRHRRDRSRSPHKRKRNKDKDKNCESRRRKERDGERHHSHKRRKQKI
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Q2G028)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
- Phosphoglycerate kinase
- Pyruvate kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoenolpyruvate carboxykinase
- Glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSKRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK
Protein: Phospholipase D2 (PLD 2) (mPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2) (P97813)
Organism: Mus musculus (Mouse)
Function: Function as phospholipase selective for phosphatidylcholine. May have a role in signal-induced cytoskeletal regulation and/or endocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9395408}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor 6
- 5'-3' exonuclease PLD3
- Ras-related protein Ral-A
- 5'-3' exonuclease PLD4
- ADP-ribosylation factor 1
- Transforming protein RhoA
- Cholinephosphotransferase 1
- Sphingosine kinase 2
- Ras-related protein Ral-B
- Protein kinase C alpha type
Sequence:
MTVTQKNLFPYGDYLNSSQLHMEPDEVDTLREGEDPADRMHPYLAIYDLQPLKAHPLVFAPGVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLQRHKVLMSLLPLARFAVTHSPAREAAAEDIPSLPRGGSEGSARHTASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGSKGLEGVIRKRSGGHRVPGFTFCGRDQVCYRWSKRWLVVKDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTETRYGVRIDTSHRSLILKCSSYRQARWWGQEITELAQGSGRDFLQLHQHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEIYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRTLMLLHPNIKVMRHPDLVTLWAHHEKLLVVDQVVAFLGGLDLAFGRWDDVQYRLTDLGDPSEPVHLQTPTLGSDPAATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGVAARDLARHFIQRWNFTKTTKARYKTPLYPYLLPKSTSTANNLPFMIPGGQCATVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHEQGQCFRVYLLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEHSILHRLKAAMGTAWRDYMSICGLRTHGELGGHPISELIYIHSKMLIADDRTVIIGSANINDRSLLGKRDSELAILIKDTEMEPSLMDGVEYQAGRFALSLRKHCFSVILGANTWPDLDLRDPVCDDFFQLWQETAENNATIYEQIFRCLPSNATRSLRALREYVAVESLATVSPSLAQSELAHIQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Protein: Peroxiredoxin-6 (EC 1.11.1.27) (Q8BG37)
Organism: Mus musculus (Mouse)
Interaction partners:
- Glutathione synthetase
- Glutathione hydrolase 6
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 7
- Peroxiredoxin-6
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione S-transferase Mu 5
- Glutathione S-transferase omega-1
Sequence:
MPGGLLLGEEAPDFEANTTIGRIRFHDFLGNSWGMLFSHPKDFTPVCTTELGRAAKLAPEFAKRNVKLIALSVDSVEDHLAWSKDINAYNGATPKEKLPFPIIDDKDRDISILFCMLDPVEKDANSMPLTARGVFIFGPDKKLKMSLLYPNSTGRNFDEILRVIDSLQLTETKPVATPVDWKKGESVMVLPDLPEEEAKRCFPKGISTTKLPSGKNYLRYTPQP
Protein: Uncharacterized protein (Q3UZ16)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VSRSGAIIHTIALGPSAARELETLSDMTGGLRFYANKHVSSLIDAFSRISSTSGSVSQQALQLESKAFNVRAGAWINSTVPVDSTVGNDTFFVITWTVQKPEIILQDPKGKKYITSDFQDDELNIRSARLQIPGTAETGTWTYSITGTKSQLITMTVTTRARSPTMEPLLATAHMSQSTAQYPSRMIVYVRVSQGFLPVLGANVTAIIEAEHGHQVTLELWDNGAGADTVKNDGIYTRYFTDYHGNGRYSLKVRVQARKNKARLSLRQKNKSLYIPGYVENGKIVLNPPRPDVQEEAIEATVEDFNRVTSGGSFTVSGAPPDGDHARVFPPSKVTDLEAEFIGDYIQLTWTAPGKVLDKGRAHRYIIRVSQHPLGLQEDFNNATLVNASSLIPKEAGSKETFKFKPETFKIANDTQLYIAIQAYNEAGLTSEVSNIAQAVKFTSLEDSISALGADISAISMTVWGLAVIFNSILN
Protein: Beta-galactosidase (EC 3.2.1.23) (Q56A50)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAPVVGLVSVLLLIIPATTYATTPTFSVDYHRNCFLKDGEPFRYISGSIHYSRIPRVYWKDRLLKMYMAGLNAIQTYVPWNFHEAVPGQYDFSGDRDLEQFLQLCQDIGLLVIMRPGPYICAEWDMGGLPAWLLKKKDIVLRSSDPDYLAAVDKWMGKLLPIIKRYLYQNGGPIITVQVENEYGSYFACDFNYMRHLSQLFRFYLGEEAVLFTTDGAGLGYLKCGSLQGLYATVDFGPGANVTAAFEAQRHVEPRGPLVNSEFYPGWLDHWGEKHSVVPTSAVVKTLNEILEIGANVNLYMFIGGTNFGYWNGANTPYGPQPTSYDYDSPLTEAGDLTEKYFAIREVIKMYKDVPEGILPPSTPKFAYGKVQMKKLKTVSETLDVLSFSGPVKTLYPPTFIEMNQAFGFVLYQTVLPVNCVKPTPLSSPLNGVHDRAYISIDGIAAGILERNKALSINITGKAGSHVDVLVENMGRINYGKGINDFKGLVFNLTLGADVLVNWTVYSLSVDEAVSKGLLSASGSSSTSSTSTPPPALSPPTFYTGSFIIPDGIPDLPQDTYIQFPDWRKGQVWINGFNVGRYWPSRGPQITLFVPAHLLSTSVQNNITVLELEASPCSSGSCMVEFTDTPILNGTVNSQYKRQLFNKQDLL
Protein: Defective proboscis extension response 20 (GH16485p) (Q9W0L9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable G-protein coupled receptor CG31760
- Dpr-interacting protein epsilon
- Protein DPCD
- LD06737p1
- MIP29328p
- Dpr-interacting protein zeta, isoform A
- Glutamate [NMDA] receptor subunit 1
- RE57134p
Sequence:
MRLNEPAARTRPRTKSTTDATKFSSSRGDLHLDCAVPNLIRLLLLIATIMGSGLVQAKTIYDSVNMIQSLDALVEPRETTKVPLQTTPATPPTAHAHIHNQVSTLRSSYEDSDDGVDGDYVIPESQTSTVAILDQDSSMKGQDMESLSLQAGSGTVSPKSSPDSSGHKKNASFQQIGSQNVNALVPATVATTSSGLPSSSNASLATPTEPARNRSTGLVRNSAVKVDSKHPLSKGQKTDAPMLNYIFDTFSSANKHHHHDQRYGPHFEDVQRIGQATNLTVQAGSSIHLNCRISLLQDKTVSWVRHNTQDEGKDNGNALDLLTVGMHTYTGDKRYKMEFQYPNNWRLKITNVKKDDEAIYECQISTHPPRVIQINLHVNAPKVMIVDEVGDPLQEKYYEIDSTLQLSCVVRNVAMTSSVVFWKHMDNILNYDVTRGGVSVKTELMEDGANSTLSIAKISKTDSGNYTCSISEFQNFTIVVHILNGESFAELHHGGAVGWHSTWWNMVMLHAMALLVLNSLRGEFS
Protein: Glutamine-rich protein 2 (Q9H0J4)
Organism: Homo sapiens (Human)
Function: Has an essential role in the formation of sperm flagella and flagellar structure maintainance. It acts as a suppressor of ubiquitination and degradation of proteins involved in flagellar development and motility.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q3V2A7}. Nucleus {ECO:0000250|UniProtKB:Q3V2A7}. Cytoplasm {ECO:0000250|UniProtKB:Q3V2A7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:30683861}. Note=Localization varies during spermatozoa development. The protein is distributed in the nuclear membrane of the spermatogonia, in the nucleus of round spermatids, in the nucleus and cytoplasm of early elongating spermatids, in the cytoplasm of late elongating spermatids, and in the flagella of epididymal spermatozoa. {ECO:0000250|UniProtKB:Q3V2A7}.
Interaction partners:
- Cilia- and flagella-associated protein 44
- Cilia- and flagella-associated protein 43
- Transcriptional regulator QRICH1
- Cilia- and flagella-associated protein 69
- Dynein axonemal heavy chain 1
Sequence:
MKDAAEELSFARVLLQRVDELEKLFKDREQFLELVSRKLSLVPGAEEVTMVTWEELEQAITDGWRASQAGSETLMGFSKHGGFTSLTSPEGTLSGDSTKQPSIEQALDSASGLGPDRTASGSGGTAHPSDGVSSREQSKVPSGTGRQQQPRARDEAGVPRLHQSSTFQFKSDSDRHRSREKLTSTQPRRNARPGPVQQDLPLARDQPSSVPASQSQVHLRPDRRGLEPTGMNQPGLVPASTYPHGVVPLSMGQLGVPPPEMDDRELIPFVVDEQRMLPPSVPGRDQQGLELPSTDQHGLVSVSAYQHGMTFPGTDQRSMEPLGMDQRGCVISGMGQQGLVPPGIDQQGLTLPVVDQHGLVLPFTDQHGLVSPGLMPISADQQGFVQPSLEATGFIQPGTEQHDLIQSGRFQRALVQRGAYQPGLVQPGADQRGLVRPGMDQSGLAQPGADQRGLVWPGMDQSGLAQPGRDQHGLIQPGTGQHDLVQSGTGQGVLVQPGVDQPGMVQPGRFQRALVQPGAYQPGLVQPGADQIDVVQPGADQHGLVQSGADQSDLAQPGAVQHGLVQPGVDQRGLAQPRADHQRGLVPPGADQRGLVQPGADQHGLVQPGVDQHGLAQPGEVQRSLVQPGIVQRGLVQPGAVQRGLVQPGAVQRGLVQPGVDQRGLVQPGAVQRGLVQPGAVQHGLVQPGADQRGLVQPGVDQRGLVQPGVDQRGLVQPGMDQRGLIQPGADQPGLVQPGAGQLGMVQPGIGQQGMVQPQADPHGLVQPGAYPLGLVQPGAYLHDLSQSGTYPRGLVQPGMDQYGLRQPGAYQPGLIAPGTKLRGSSTFQADSTGFISVRPYQHGMVPPGREQYGQVSPLLASQGLASPGIDRRSLVPPETYQQGLMHPGTDQHSPIPLSTGLGSTHPDQQHVASPGPGEHDQVYPDAAQHGHAFSLFDSHDSMYPGYRGPGYLSADQHGQEGLDPNRTRASDRHGIPAQKAPGQDVTLFRSPDSVDRVLSEGSEVSSEVLSERRNSLRRMSSSFPTAVETFHLMGELSSLYVGLKESMKDLDEEQAGQTDLEKIQFLLAQMVKRTIPPELQEQLKTVKTLAKEVWQEKAKVERLQRILEGEGNQEAGKELKAGELRLQLGVLRVTVADIEKELAELRESQDRGKAAMENSVSEASLYLQDQLDKLRMIIESMLTSSSTLLSMSMAPHKAHTLAPGQIDPEATCPACSLDVSHQVSTLVRRYEQLQDMVNSLAVSRPSKKAKLQRQDEELLGRVQSAILQVQGDCEKLNITTSNLIEDHRQKQKDIAMLYQGLEKLEKEKANREHLEMEIDVKADKSALATKVSRVQFDATTEQLNHMMQELVAKMSGQEQDWQKMLDRLLTEMDNKLDRLELDPVKQLLEDRWKSLRQQLRERPPLYQADEAAAMRRQLLAHFHCLSCDRPLETPVTGHAIPVTPAGPGLPGHHSIRPYTVFELEQVRQHSRNLKLGSAFPRGDLAQMEQSVGRLRSMHSKMLMNIEKVQIHFGGSTKASSQIIRELLHAQCLGSPCYKRVTDMADYTYSTVPRRCGGSHTLTYPYHRSRPQHLPRGLYPTEEIQIAMKHDEVDILGLDGHIYKGRMDTRLPGILRKDSSGTSKRKSQQPRPHVHRPPSLSSNGQLPSRPQSAQISAGNTSER
Protein: peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) (P71971)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTRPKLELSDDEWRQKLTPQEFHVLRRAGTERPFTGEYTDTTTAGIYQCRACGAELFRSTEKFESHCGWPSFFDPKSSDAVTLRPDHSLGMTRTEVLCANCDSHLGHVFAGEGYPTPTDKRYCINSISLRLVPGSV
Protein: (11Z)-hexadec-11-enoyl-CoA conjugase (Bmpgdesat1) (EC 1.14.19.15) (Acyl-CoA Delta(11) desaturase) (EC 1.14.19.5) (Acyl-CoA Z11/delta10,12 desaturase) (Q75PL7)
Organism: Bombyx mori (Silk moth)
Function: Fatty acid desaturase that catalyzes 2 consecutive steps in the biosynthesis of bombykol, a sex pheromone produced by the moth. First acts as an acyl-CoA Delta(11) desaturase (1) by catalyzing the formation of Delta(11) fatty acyl precursors. Then acts as a (11Z)-hexadec-11-enoyl-CoA conjugase (2) by converting a single cis double bond at position 11 of (11Z)-hexadec-11-enoyl-CoA into conjugated 10 trans and 12 cis double bonds.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPPNSVDKTNETEYLKDNHVDYEKLIAPQASPIKHKIVVMNVIRFSYLHIAGLYGLYLCFTSAKLATSVFAIVLFFLGNFGITAGAHRLWSHNGYKVKLPLEILLMVFNSIAFQNTIFTWVRDHRLHHKYTDTDADPHNATRGFFFSHIGWLLVRKHPMVKIAGKSLDMSDIYCNPLLRFQKKYAIPFIGTICFIIPTLAPMYFWGESLNNAWHITVLRYIFSLNGTFLVNSAAHLWGYKPYDKSLKATQSGMANAFTFGEGFHNYHHVFPWDYRADELGDRYINLTTRFIDFFAWMGWAYDLKTASTNIIEKRALRTGDGTYKRPNGMN