wanglab/gogpt-training-data huggingface dataset:
Protein: Amino acid transporter (Q9NA91)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- alpha-glucosidase
- Glycosyl hydrolase family 13 catalytic domain-containing protein
- Na
Sequence:
MSSIEDLPTVGDVAATRHQMGLWSCMSYVIANIIGAGIFITPGTVLKLALTNGMALVVWLGCGLISLIGGICYIELGTSIRDPGCDFAYNVYVGWEGIAFSFMWVGVIMSFPASAAVQAQTFGQYIVAGLSPIWHLGSPYDVILERGLGFALIIILTVLNLYAIDKYASKFQIFVTIAKLLSLAIIIVTGFWYLIVKGETEHFKDAFTPLPNEKYDIGQISLAFYGALWSFAGWDILNYGTPEIKNPRRTMPIALLGGISAVTLVYMAMNVSYMTVLDTETLKNSSAVAADFARITLGDFSYAIPFMISILLIGTLNSNIFCGSRFTHAAAREGHLPTFLSCINAESNSPRAALLFQLICTIAVTFVDTESLITYVTFVMFGQRVFTMAALLWIRYRNIPVHPDAIRVPLIFSILFFMITIALVVTPFIEDFTTTIVGVGLVLMGFLLYMIFMKPKQLPGFLYRFNDGITRVTCKILFTTPDLKHASEIETLKSDGELNRGETLSSRFHNESVVSNDERTTLSTSQIDTAAAGTAEPMTRL
Protein: NF-kappa-B inhibitor alpha (ECI-6) (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Q08353)
Organism: Sus scrofa (Pig)
Function: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25963}. Nucleus {ECO:0000250|UniProtKB:P25963}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. {ECO:0000250|UniProtKB:P25963}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- RELA proto-oncogene, NF-kB subunit
- Nuclear factor NF-kappa-B p105 subunit
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B essential modulator
- Nuclear factor NF-kappa-B p100 subunit
- S-phase kinase-associated protein 1
- NFKB inhibitor beta.
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- REL proto-oncogene, NF-kB subunit.
Sequence:
MFQPAEPGQEWAMEGPRDALKKERLLDDRHDSGLDSMKDEEYEQMVKELREIRLEPQEAPRGAEPWKQQLTEDGDSFLHLAIIHEEKALTMEVVRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLEAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQPRGTQHLHSILQATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEDELPYDDCVLGGQRLTL
Protein: MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 2 (MA3 domain-containing protein 8) (O80548)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytosol {ECO:0000269|PubMed:29084871}.
Interaction partners:
- Initiation factor eIF-4 gamma, MA3
- F-box protein At5g18160
- Eukaryotic translation initiation factor isoform 4G-2
- Cytochrome P450, family 705, subfamily A, polypeptide 18
- Probable protein phosphatase 2C 23
Sequence:
MEHQDLTDSRKDPLCISQLKISSSSLDPLPQANMAEDLTKSRRHSPIKVEGSEETWGVEDDDDLTDPIFDTIEGNGHSDPTSCFDADLSEYKKKATVIVEEYFGTNDVVSVVNELKELGMAEYRYYFVKKLVSMAMDRHDKEKEMAAFLLSTLYADVIDPPEVYRGFNKLVASADDLSVDIPDAVDVLAVFVARAIVDDILPPAFLKKQMKLLPDNSKGVEVLRKAEKSYLATPLHAEVVEKRWGGTDNWTAEDVKARINDLLKEYVMSGDKKEAFRCIKGLKVPFFHHEIVKRALIMAMERRKAQVRLLDLLKETIEVGLINSTQVTKGFSRIIDSIEDLSLDIPDARRILQSFISKAASEGWLCASSLKSLSADAGEKLLENSSANVFKDKAKSIIREYFLSGDTSEVVHCLDTELNASSSQLRAIFVKYLITLAMDRKKREKEMACVLVSTLGFPPKDVRSAFSMLIESADDTALDNPVVVEDLAMFLARAVVDEVLAPRDLEEVLNQTPEAGSSVGEKVIQMAKTLLKARLSGERILRCWGGGGIETNSPGSTVKEVKEKIQILLEEYVSGGDLREASRCVKELGMPFFHHEVVKKSVVRIIEEKENEERLWKLLKVCFDSGLVTIYQMTKGFKRVDESLEDLSLDVPDAAKKFSSCVERGKLEGFLDESFASEDSQSKKQNGSSSSSG
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (Somatomedin) (Q0PPT3)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MGKISSLPTQLFKCCFCDFLKVKMHITSSSHLFYLALCLLSFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKARKEVHLKNTSRGSSGNKNYRM
Protein: Hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase (EC 2.5.1.15, EC 2.7.6.3) (Q8IAU3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Dihydrofolate synthase/folylpolyglutamate synthase
- GTP cyclohydrolase 1
- aminodeoxychorismate synthase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, putative
- 6-pyruvoyltetrahydropterin synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- indole-3-glycerol-phosphate synthase
- Coronin
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
Sequence:
METIQELILSEENKTNIAVLNLGTNDRRNAVLILETALHLVEKYLGKIINTSYLYETVPEYIVLDKKESCEKINKDCRIYDVNYINELMQNLEESKYEENKELIDKCEEYETFLKNGKVDNSILKEVNVENYLLECNNIIVKNDEIMKNNLSKYKDKYYTSYFYNLTVVVKTFVNDPLSMLVVIKYIEELMKRENVKEKEKFENRIIDIDILFFNDFTIFMKNIKLEKNMIYKILSKYIHLERDIKNGNDNMSKVNMDKDINLNNNNNIKKKNNNDIDCDCVDQKMNNHVNNKNYINSFRDPQEIINNMVDNIEFLSIPHVYTTHRYSILLCLNDMIPEYKHNVLNNTIRCLYNKYVSRMKEQYNINIKENNKRIYVLKDRISYLKEKTNIVGILNVNYDSFSDGGIFVEPKRAVQRMFEMINEGASVIDIGGESSGPFVIPNPKISERDLVVPVLQLFQKEWNDIKNKIVKCDAKPIISIDTINYNVFKECVDNDLVDILNDISACTNNPEIIKLLKKKNKFYSVVLMHKRGNPHTMDKLTNYDNLVYDIKNYLEQRLNFLVLNGIPRYRILFDIGLGFAKKHDQSIKLLQNIHVYDEYPLFIGYSRKRFIAHCMNDQNVVINTQQKLHDEQQNENKNIVDKSHNWMFQMNYMRKDKDQLLYQKNICGGLAIASYSYYKKVDLIRVHDVLETKSVLDVLTKIDQV
Protein: Pharyngeal muscle protein 2 (O62203)
Organism: Caenorhabditis elegans
Function: Involved in pharyngeal muscle development and ensures pharyngeal grinder function during feeding. Plays a role in the defense against the accumulation of ingested live pathogenic bacteria in the intestine. Has a role in the determination of life span.
Subcellular location: [Isoform a]: Nucleus {ECO:0000269|PubMed:30965033}.
Interaction partners:
- Glycosyltransferase
- Probable peptidyl-glycine alpha-amidating monooxygenase pamn-1
Sequence:
MPLESGKLINDLRVSELKTELEKRGLSTQGVKVVLTVRLNKALRDEGLDPADHVFEHAVSPMKKSTRRSNEMARAAAAAAAEKVEKGAGDEGNDENVLVEEKEEEEEEEDSHDLQIIEDHELEVPSDEKDDTLVEDEEFEEAEQVEPEPEAVEPVVEEKPEEKLEEKPEEKLEEKPEEKPVEPEVVTVEEPVAEVIEVEKAVAEPVELKEKPEKEPEVVLVEEPVEQLENEPEVVPMEVEEAKKSDEQDGEDEFEEDDSSSDIEIIEPTLQESEPLAEEKVEKKEKKPEEIPHNLEQNEPISMETEEKVEEEVIILNSSINNVSQDDEIVLDYEEDLLEDPLDEPIEQKEPKAAEPTPKQLQKVEASTPQATPSKAASSSAGSGKSMLFGDDVKKTSIWIRGMTPATKASSVKQLASQYGKVIQSKIFNSKAADANGDVKNCFALIQFADVTAMELAMTSLHQKNYQGRVLRVEKVSESHLTSSAEKLAREKHVAEAASTMSTSPAPTPTPEPVVTTTTTTSAAPKRKEPIHAPESSSSEGQRAKRRAIEAPVRSRSRSRGGGGEPRSSRKPITFDREEESNRDSRRTIAAAPPARTSRMARSPLRAPLRAARGSESSRSSTRGGGGGGESLTISSRVDTSGCRGGAIKRSVERSVPNNISTSELRRKHHQIHVTVQQDAPRASYQTEQYARERSSSTTTSSRRRQVSPDRSEQRRHRDEPPPRRAPQEQPSRRRGASPPEPPRRQEGARRSEEPERRRLFDEREQLAHIMAAKDMYAEQQKIRAEKALIAFQMQQLEKKKLEAELQIAQKALLMQQAALGGGGALVVDGGALVAGGGAVGYHHQEHRSSYGGGGSSSNGGSSNRRRQTRRSPSPPQQHHSSSRRQRRDSGGAGRYRQSTSSSNSNRNSNSGGRNLVVTATTTNNTNATNAGRSYGIQSVPDASSYSTNNYQQRSSAASAYDLQITATMPQAGAANSGAAYHQPYGNVYQHNTAAYPVWGGLDAQGHMAMDTNWSQNAATPSTSTSSGGGGGQQWQQQSYGSNQHQHHQNNNSSQPSSSNRRGNDYGNYRGNY
Protein: Protein fluG (P38094)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: May function as a GSI-related enzyme in synthesizing a small diffusible factor that acts as an extracellular signal directing asexual sporulation and perhaps other aspects of colony growth. May be involved in brlA activation (an early transcriptional regulator for conidiation specific gene).
Subcellular location: Cytoplasm.
Interaction partners:
- Developmental regulator flbA
- C2H2 type master regulator of conidiophore development brlA
- C2H2-type domain-containing protein
- MYB family conidiophore development protein FlbD
- Conidiophore development regulator abaA
- SfgA
- BZIP-type transcription factor
- FlbE
- Putative urea carboxylase
- Multifunctional tryptophan biosynthesis protein
Sequence:
MATLSSLRHLIQTHPLIDNHAHNLLSQSAACKYAKYPFEQIISEAQGVALANAPSTLSFHRAASQLATLYQSSSSDWDSVRAARDQSVQRDYEGLIRKCLEGTQVLLLDDLLTENDVELFDWHDRFTASATKRIVRIEALAASVLSQIVHGGPVPQDSSDLSAFQTLWESFSRNFSALVSDAIADPAVVGFKSVICYRTGLDVQPTDDRDTERLIRSFARTISQAAVSTPRVEDKPLNDWLVRQTLNLLKAAKVTQPNKPLQLHTGLGDNDINLLKSNPAHLQSLIAQYPEVDFVLLHSSYPYTREAGYLACVYPNVYLDLGEVFPMVSRDAQESILRESLEIVPSTRLLWSTDGHFFPETFWLANRQFRDALEKVFVDYVQNGDYTIEQAMQAAADILFHNSNRLYELNEQPPSAALSSGHQTVSRISSTDLLEKFIRSNPGVKYVWTQFIDYTATVRVRMFPVMEFAKIVRKQRRLGISMATFWMLQDDEVVGGSTTGQFYLIPDLSTLSPNVGIDSKSATVMTWWKSEQGESLEECPRTNLLNINNKLKDEFGIQATCGFEIEVVFLKPTTDPSTGEEDWAPSVTNHSWSQMTRETRRMLPLLEEIAETLASIGIHLQQFHAESAPGQFEFILPPDNPVAAVDTLIKSRQVIANIVEKHGLRATLYPRPYPSAAGTASHAHVSISPSTKEESFLAGVLQHYPAVLAFTLSGDASYDRVKSGIWAGSEWVTWGTQNREAPIRKISPGHWEIKSLDGLANMYLAMAAFLAAGYTGVKENLPLTIKDCPYDAASLPESERAALGITTKLPNTLAKSLAALESDEILRSLLGENLVEDYIIVKRAESKKLSAMDEKARRKWLVERY
Protein: Putative monooxygenase p33MONOX (EC 1.-.-.-) (Brain-derived rescue factor p60MONOX) (Flavin monooxygenase motif-containing protein of 33 kDa) (Q96A73)
Organism: Homo sapiens (Human)
Function: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MASRQPEVPALEASAPLGKMSLPIGIYRRAVSYDDTLEDPAPMTPPPSDMGSVPWKPVIPERKYQHLAKVEEGEASLPSPAMTLSSAIDSVDKVPVVKAKATHVIMNSLITKQTQESIQHFERQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGEVTKEERQPASAQSTPSTTPHSSPKQRPRGWFTSGSSTALPGPNPSTMDSGSGDKDRNLSDKWSLFGPRSLQKYDSGSFATQAYRGAQKPSPLELIRAQANRMAEDPAALKPPKMDIPVMEGKKQPPRAHNLKPRDLNVLTPTGF
Protein: Telomere elongation protein est1 (Ever shorter telomeres protein 1) (O74804)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Directly involved in telomere replication. Associates with telomerase and during its interaction with trt1, telomerase activity is promoted.
Subcellular location: Nucleus {ECO:0000269|PubMed:12676088}. Chromosome, telomere {ECO:0000305|PubMed:12676088}.
Interaction partners:
- Telomerase reverse transcriptase
- Coiled-coil quantitatively-enriched protein 1
- Protection of telomeres protein poz1
- ATP-dependent helicase upf1
- Serine/threonine-protein kinase tel1
- La-related protein 7 homolog
- Protection of telomeres protein tpz1
- Telomere length regulator taz1
- Trehalose-phosphatase
- DNA-binding protein rap1
Sequence:
MSQQLSSNEICEEQGKLVKALCEAAQGGFKHDLYEKIIAIEIEVEKKLLNRLKSIQTNTFERPDIIWSCCHYKIIQHFRSRFREIHPRHVVEKKKTKKVFFKFLKTCAIFYQTCISELISKFQLDSYRPFFCKWTSSATVSSTISNDEMSSIPEASYSRNHMEALECVYNCFIYLGDMARYSSTCLKKRGAYDRALGFYDLAHRTLPGNGMHRNQIAVVWASDECIVESIYWFSSALCSEDPPKSALLNLLKQLIAFYRRCFAVHFEFVSPMMILLFIISDCCIHSLKEIQPFKCPSIMVKDLENSLLQSNIRNVGYEKKNLYYISSAFSNLLHCRYFNCNDRLRSFYYRFSSWLFHQTLACAKEVESERAPTSYLTSCLPSIKVILARVLESSPAFGFIERNELEQLSYHFRICEKFFKESSENKMLNLFEDYNEFGLCKSFICLFKRLNEDIIGPKLNINPPDYTTHPFSESIKRFYQISKILNLLLS
Protein: Probable protein phosphatase 2C 6 (OsPP2C06) (EC 3.1.3.16) (ABI1-like protein 1) (OsABI-LIKE1) (OsABIL1) (Q0JLP9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable protein phosphatase that may function in abscisic acid (ABA) signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:26491145}. Cytoplasm, cytosol {ECO:0000269|PubMed:26491145}. Note=Localizes predominantly in nucleus. {ECO:0000269|PubMed:26491145}.
Interaction partners:
- Abscisic acid receptor PYL9
- Serine/threonine-protein kinase SAPK9
- Serine/threonine-protein kinase SAPK10
- Abscisic acid receptor PYL10
- Serine/threonine-protein kinase SAPK8
- Serine/threonine-protein kinase SAPK2
- Serine/threonine-protein kinase SAPK1
- Serine/threonine-protein kinase SAPK3
- Serine/threonine-protein kinase SAPK6
- Serine/threonine-protein kinase SAPK7
Sequence:
MEDVAVAAALAPAPATAPVFSPAAAGLTLIAAAAADPIAAVVAGAMDGVVTVPPVRTASAVEDDAVAPGRGEEGGEASAVGSPCSVTSDCSSVASADFEGVGLGFFGAAADGGAAMVFEDSAASAATVEAEARVAAGARSVFAVECVPLWGHKSICGRRPEMEDAVVAVSRFFDIPLWMLTGNSVVDGLDPMSFRLPAHFFGVYDGHGGAQVANYCRERLHAALVEELSRIEGSVSGANLGSVEFKKKWEQAFVDCFSRVDEEVGGNASRGEAVAPETVGSTAVVAVICSSHIIVANCGDSRAVLCRGKQPVPLSVDHKPNREDEYARIEAEGGKVIQWNGYRVFGVLAMSRSIGDRYLKPWIIPVPEITIVPRAKDDECLVLASDGLWDVMSNEEVCDVARKRILLWHKKNGTNPASAPRSGDSSDPAAEAAAECLSKLALQKGSKDNISVIVVDLKAHRKFKSKS
Protein: Amino acid ABC transporter ATP binding protein (Q9I488)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004417}.
Interaction partners:
- Amino acid ABC transporter periplasmic binding protein
- Amino acid ABC transporter membrane protein
- Probable permease of ABC transporter
- Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase
- Glutamate/aspartate import permease protein GltK
- Amino acid ABC transporter membrane protein
- Putative glutamine transport system permease protein GlnP
- Cis-3-hydroxy-L-proline dehydratase
- Glutamate/aspartate import permease protein GltK
- Arginine ABC transporter permease protein ArtM
Sequence:
MIEINDVHKAYGQFEVVKGVDLRVDKGEVLSIIGGSGSGKSTLLMCINGLEPIQRGSIRVDGIDVHARGTDLNRLRRKIGIVFQQWNAFPHLTVLENVMLAPRKVLGKSRAEAEAMALKQLTHVGLGDKLKVFPQRLSGGQQQRMAIARALAMSPDYMLFDEATSALDPQLVGEVLDTMRLLAEEGMTMVLVTHEIRFARDVSDRVAFFRNGLVHEIGPPDQVIGNPQRPETVEFLRSVL
Protein: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 (PAPS synthase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK 2) (SK2) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] (O95340)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases. In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway. Plays indirectly an important role in skeletogenesis during postnatal growth.
Interaction partners:
- FAD synthase
- Sulfite oxidase, mitochondrial
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- 3'
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Dymeclin
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
- Sulfate transporter
- Elongation factor 1-alpha 2
- Elongation factor 1-alpha 1
Sequence:
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLEKN
Protein: Zona pellucida sperm-binding protein 3 receptor (Acrosomal matrix component 67) (Protein AM67) (p67) (O08569)
Organism: Cavia porcellus (Guinea pig)
Function: Probably involved in the formation of the dense core and M1 domain of the acrosome. May also regulate the release of certain secretory proteins following the acrosomal reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000269|PubMed:9139729}. Note=Sperm acrosomal matrix. Restricted to the M1 domain of the apical segment of the acrosome.
Interaction partners:
- Complement component 4 binding protein beta
- Anaphylatoxin-like domain-containing protein.
- Complement C3
- NTR domain-containing protein
- Sperm acrosome associated 1
- C4bp alpha-chain
Sequence:
MFPRLQAVSAPALLQITLMAVLLAPVLGDCGPPPILPFASPVIQSYETNFRTGTALKYNCHRGYWRVNSSHVICDINGSWIYNVFCAKKRCRNPGELANGKVEIITDLLFGSTIEFSCSKGYSLIGSTTSQCESQGKTVDWSDPLPECVIVKCDSPPDISNGKHSGTDEDLYTYGSLVTYVCDPNYSLLGNASISCLVANKTVGVWSSNPPTCEKVICRQPHIPKGIFLSGFGFYYTYKDTLVISCKKGYILRGSSIIHCEANSKWYPSIPTCEPNGCIDLPEVPYISWERNVLSLKNQEIFEIGSLLKYDCKTGYRPTPNEPRTVTCQENLKWAISKGCERVCCPTPNMEKMRIINERRDFTGVCVYAYEDYIFYMCDEGYYPISADGRSSCQADGMWNPKMPACESAVCLKPDILNGKLSVEKDHYTETENVTIHCDSGYEVVGPQNIICSENRTWTPEIPKCEWEVPEECKQVAAGRKLLECLPNPSDVKMALEVYKLSLEIEQLEKEKYVKIQEKFSKKEMKQLTSALH
Protein: Sad1 and UNC84 domain containing 1 (A0A8I6AAB7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
MWRVFVPRPGRCGRGLRRRREAAWSEPVNMDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHRLEPVFDSPRMSRRSLRLITTTAAYSSGDGQTVDTHISTSRATPAKGRETRTVKQRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAVHGPTSRVYSRDRTLRPPHLGHCGRMTAGELSRVDGESLCDDCKGKKHLETHTTTHSQLSQPHRAAGAMGRLCTYTGDLLVRALRRTRAAGWSVAEAMWSVLWLAVTAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGFSLWGQGNFFSLLPMLNWTAMQPAQRVDNPKDMHRPGPLSPSPPLKVDPMASQWPQESDMGQKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMVGQHLQEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLRSSCEQADARIQETVQLMFSEDQPGGSLEWLLQKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAMSQAGISGITEAQAHIIVNNALRLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPRDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
Protein: Cholinephosphotransferase 1 (hCPT1) (EC 2.7.8.2) (AAPT1-like protein) (Diacylglycerol cholinephosphotransferase 1) (Q8WUD6)
Organism: Homo sapiens (Human)
Function: Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}.
Interaction partners:
- Choline-phosphate cytidylyltransferase B
- Choline-phosphate cytidylyltransferase A
- Phosphatidylethanolamine N-methyltransferase
- Lysophosphatidylcholine acyltransferase 2
- Lysophospholipid acyltransferase 5
- Lysophosphatidylcholine acyltransferase 1
- Phospholipid phosphatase 2
- Phosphatidylserine synthase 1
- Phospholipid phosphatase 3
- Phospholipase D2
Sequence:
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLWMAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARRTNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYVSGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSCSNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILMFGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSFDMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
Protein: Proteasome regulatory non-ATPase subunit 11 (Q38BU2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome regulatory non-ATP-ase subunit 7
- 26S proteasome regulatory subunit 4 homolog
- Probable 26S proteasome regulatory subunit rpn-6.2
- Proteasome regulatory non-ATP-ase subunit 5
- Proteasome regulatory non-ATPase subunit 8
- 26S proteasome regulatory subunit RPN3
- Proteasome regulatory non-ATP-ase subunit 9
- Proteasome regulatory ATPase subunit 6
- Proteasome regulatory ATPase subunit 5
- Protease regulatory ATPase subunit 4
Sequence:
MFHPQLVAGGANRAAPAEELRDTAETVQISSLALLKMLMHGRAGVPLEVMGLMIGELIDDYTVRVSDVFSMPQTATGQSVEAVDPEYQVHMLDKLSVVGRPEKVVGWYHSHPGFGCWLSGEDVMTASSYEQLTPRSVSVVIDPIQSVRGKVVIDAFRTTKDPHTGPRIMFQEPRQTTSNIGWLTRPSPIALTRGLDRDYYSLPITFRKKNHELALLLNVYKKGWQEGFRLENMTRFDRNTVREKMRALASLAVQSERFIVQGLDEDDVGNVGRANPIAHLQSESEGLINASLNQSIGAMINGVVF
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (Q9VVQ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MLNVVRAAAVLILVQSIHSTDPNDFLNRKYYSSSVLGLVKLLKMEQEFMVNFSIYANILQEKVDNLNIFLDALKRPNHKTHNEREKFVSNPLNAFGLIRRLNQDWPKLQNYTQKPLGLEQLTAMQDIVSAAPESFDMNEKLKAMHRIETTYDLQPKDIAKGLLQRTEFNYRLLFRDCLALAYHKFEIGEFKRSLLWFQEALKLSTDGSLEIMNRLKEIELKGFATAVAKRSIYLSNQGLTNETIDDMANSQLQDAKLMDLEQLISSELKQWINDDSTTPPTDHNLGCRGLFPKKSNLVCRYNSSTNAFLKLAPLKMEEISRDPYIVMFHEVISDKDIEEMKGEITEMENGWTSLGDPKEIVSRVYWIRKESSFSKRINQRISDMTGFKLEEFPAIQLANFGVGGYFKPHYDFYTDRLKEVDVNNTLGDRIGSIIFYAGEVSQGGQTVFPDLKVAVEPKKGNALFWFNAFDDSTPDPRSLHSVCPVLVGSRWTITKWLHYAPQLFVKPCSPRVHLE
Protein: Peroxisomal targeting signal 2 receptor (PTS2 receptor) (Peroxin-7) (P78798)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase. Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol. Cargo protein-binding triggers interaction with PEX21 and formation of a ternary complex composed of PEX21 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. Peroxisome matrix {ECO:0000250|UniProtKB:P39108}.
Interaction partners:
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein pex13
- Peroxisomal membrane protein pex14
- Acetyl-CoA acetyltransferase
- Probable proteasome subunit beta type-5
- Peroxisomal ATPase pex6
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 11
Sequence:
MLSLRTPGFQGESVQFSPLVENKIAVAAVTHYGLGGSGRLYIHDVTPKGIQVCQHYDVEDSLFGVRWSQNCENQVYACCGDGSLRLFDLTMPSKPIHKWKEHKAEIVAIDTNTVDRRIVVTGSWDGTIKLWLGNLPNSVQTLNNGSNSRILTVATHYSSPNLLGYTSSDGLCKFWDFRSSDKFMSIEIPNQITCMNWSKSNHRMVYTADNNNLVYCYDIANLKTPLSVLSGHQLAVRSIKSSNSAHDLLATASYDMTSRIFDPEQHSCIRKVDLHSEFVRDVDWSDFGDGSWIASVGWDESLYIWNAF
Protein: ER degradation-enhancing alpha-mannosidase-like protein 2 (Q9BV94)
Organism: Homo sapiens (Human)
Function: Involved in the endoplasmic reticulum-associated degradation (ERAD) pathway that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. May initiate ERAD by promoting the first mannose trimming step of ERAD substrates, from Man9GlcNAc2 to Man8GlcNAc2. Seems to recognize and bind to exposed hydrophobic regions in target proteins (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15537790}.
Interaction partners:
- Thioredoxin domain-containing protein 11
- ER degradation-enhancing alpha-mannosidase-like protein 3
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Calnexin
- Alpha-mannosidase 2
- Short transient receptor potential channel 4-associated protein
- Protein OS-9
- X-box-binding protein 1
- Calreticulin
- Protein sel-1 homolog 1
Sequence:
MPFRLLIPLGLLCALLPQHHGAPGPDGSAPDPAHYRERVKAMFYHAYDSYLENAFPFDELRPLTCDGHDTWGSFSLTLIDALDTLLILGNVSEFQRVVEVLQDSVDFDIDVNASVFETNIRVVGGLLSAHLLSKKAGVEVEAGWPCSGPLLRMAEEAARKLLPAFQTPTGMPYGTVNLLHGVNPGETPVTCTAGIGTFIVEFATLSSLTGDPVFEDVARVALMRLWESRSDIGLVGNHIDVLTGKWVAQDAGIGAGVDSYFEYLVKGAILLQDKKLMAMFLEYNKAIRNYTRFDDWYLWVQMYKGTVSMPVFQSLEAYWPGLQSLIGDIDNAMRTFLNYYTVWKQFGGLPEFYNIPQGYTVEKREGYPLRPELIESAMYLYRATGDPTLLELGRDAVESIEKISKVECGFATIKDLRDHKLDNRMESFFLAETVKYLYLLFDPTNFIHNNGSTFDAVITPYGECILGAGGYIFNTEAHPIDPAALHCCQRLKEEQWEVEDLMREFYSLKRSRSKFQKNTVSSGPWEPPARPGTLFSPENHDQARERKPAKQKVPLLSCPSQPFTSKLALLGQVFLDSS
Protein: Armadillidin (Q64HC7)
Organism: Armadillidium vulgare (Pillbug) (Pill woodlouse)
Function: Has antibacterial activity against the Gram-positive bacterium B.megaterium LM101.
Interaction partners:
Sequence:
MKFFALFSFFVLCVALATAGHLGRPYIGGGGGFNRGGGFHRGGGFHRGGGFHSGGGFHRGGGFHSGGSFGYRG