wanglab/gogpt-training-data huggingface dataset:
Protein: Polypeptide N-acetylgalactosaminyltransferase 5 (EC 2.4.1.41) (Polypeptide GalNAc transferase 5) (GalNAc-T5) (pp-GaNTase 5) (Protein-UDP acetylgalactosaminyltransferase 5) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5) (Q7Z7M9)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- C1GALT1-specific chaperone 1-like protein
Sequence:
MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQPDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGRGKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQVVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHISRNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGTHQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA
Protein: Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division cycle 2-related protein kinase 7) (Cell division protein kinase 12) (P46551)
Organism: Caenorhabditis elegans
Function: Cyclin-dependent kinase which displays CTD kinase activity: hyperphosphorylates 'Ser-2' in the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit, thereby acting as a key regulator of transcription elongation. Required for normal reproduction.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NYV4}.
Interaction partners:
- Cyclin-like domain-containing protein
- Transcription elongation factor SPT5
- Cyclin-T1.1
- Cyclin-T1.2
- DNA-directed RNA polymerase II subunit RPB1
- RNA polymerase II subunit A C-terminal domain phosphatase
- Cell division cycle protein 73
- DNA damage-binding protein 1
- Polyadenylation and cleavage factor homolog 11
- Transcription elongation factor SPT4
Sequence:
MEISPGSSTHERDRKGSYGHRERTRSHSGSPSRFYSKDKRGSSRQGVRPRDRDSKDSISPQYKQRNWSRGGGGGGRDRGRNDFSYRKKGKDYNKRRDKRSRSRSRHRSPKRSGSSKKSKRRNSSGSSSSDLMDTSLMSELKKHGDYGSSSKSKKKSRKRRKHSSSSSSSSGEAMDLPVSSNGMNVTAIPPPPSFNINPFQPMFSQPPPPPLPPNSQFMTPPPRPPPAPFSIPPPSVDIHFAATASFSLSSIPPPPPQTDGGASSSKRQDPLPMPPDSKRIATRPVITTRRGHATNRPSDSDSWYKTNLTHYTMLDQIGEGTYGQVYKAVNNLTGEQVALKRVRLENEKEGFPITAIREIKILRQLHHKNIVRLMDIVIDDISMDELKRTRANFYLVFEYVDHDLIGLLESKELVDFNKDQICSLFKQLLEGLAYIHNTGFLHRDIKCSNILVNNKGELKIADLGLARLWEKESRLYTNRVITLWYRPPELLLGDERYGPAIDVWSTGCMLGELFTRKPLFNGNNEFGQLELISKVCGSPNVDNWPELTELVGWNTFRMKRTYQRRIREEFEHIMPREAVDLLDKMLTLNPEKRISAKEALNHPWIRSLEHTTVQPLKLPQHQDCHEMWSKKQKKSARLGRQAEGSSGSGHSIRATSHPRAPTQPSTTTTKSNGSSNHHHHHHHSHHHASSLPPSGGHAPPPPPPPTQASSTSHNNHQPVPQSQYQSVFFK
Protein: Destrin (Actin-depolymerizing factor) (ADF) (P60981)
Organism: Homo sapiens (Human)
Function: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.
Interaction partners:
- Cofilin-2
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Twinfilin-1
- WD repeat-containing protein 1
- Profilin-1
- Profilin-4
- Profilin-3
Sequence:
MASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADKKCIIVEEGKEILVGDVGVTITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFFLWAPELAPLKSKMIYASSKDAIKKKFQGIKHECQANGPEDLNRACIAEKLGGSLIVAFEGCPV
Protein: 20 kDa chaperonin, chloroplastic (Chaperonin 10) (Ch-CPN10) (Cpn10) (Chaperonin 20) (Protein Cpn21) (O65282)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seems to function only as a co-chaperone, along with CPN60, and in certain cases is essential for the discharge of biologically active proteins from CPN60. Required to activate the iron superoxide dismutases (FeSOD).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10205903}.
Interaction partners:
- Chaperonin CPN60, mitochondrial
- Chaperonin 60 subunit beta 1, chloroplastic
- Chaperonin 60 subunit alpha 1, chloroplastic
- Chaperonin 60 subunit beta 2, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
- Chaperonin 60 subunit beta 4, chloroplastic
- Chaperonin 60 subunit alpha 2, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Chaperonin 60 subunit beta 3, chloroplastic
- GrpE protein homolog
Sequence:
MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS
Protein: Inner nuclear membrane protein Man1 (LEM domain-containing 3) (Q5TZH9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004473}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004473}.
Interaction partners:
- Coiled-coil domain-containing 13.
- Mothers against decapentaplegic homolog 2
- Cell division cycle 5-like protein
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog.
- Barrier-to-autointegration factor
- Ubiquitin thioesterase zranb1-B
- Mothers against decapentaplegic homolog
- Small nuclear ribonucleoprotein polypeptide B2
Sequence:
MASAQLTDEELVSELKRLGFTPGPVTESTRPVYLKKLKKLREEQPQLRGSRSGKGRSSSGTINNNGSGASSNSSSAARAPGFSARPPTSDVTRLSASRSEKRKAGKFVLGFSSDESDVEAPQKKGGPNHGGSRRDRGSAQQTPTIRPAGTPAAAVSLGLSADRKSVSGSPWWADRGKSGDLAETERDSRAVNGNKAFYESNSSKLARDYSDSDEEEEEVGERDRPRERRLTSRHSPPASSSPYRSAWSSDKTALGAHDTPDYNLDMVGERRDEDDKEPSEFSGSYVSRSYPKLSGTGRDDNSGGSSIPSGSFHRNHLDNGDGESACSSRFSIGLRPRFPSYTATYRANHSNHTGSNHSYSHASAHKSKQHTTVPEDELLQQFKREEVSSTGGFSAHYLSMFLLTAACLFFVLLGLMYLRMRGSGTAVGDAVIMQHPFGAEFDKQYDVKERELILNLLLSLHEHLASVAGEHDCGDFKNPLNRSVSFSDASKYLKLQNEAYENLIETSLEWVMKTKDVVGIRLIGGDPDHPIEDVSEISRLESIHPRMSFFCRFRRAFFTVIYRVLLILAGIGVVVGLVYYMKYRWRKEEEETRHMYDMVERIIDVLRSHNEACQENKDLQAYLPIPHVRDSLVQPQERKRMKKVWDRAVSFLSANESRIRTEKQRIGGADFMVWRWLQPSMSPDKMCNMPSKVWQGQAFPLDRRNSPPNSLTPCLKIRNMFDPVMEVGENWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSAEHSGKAFKALHGSWFDGKLVTVKYLRLDRYHQRFPQALGSNTPLKPSSSSMNSMSRLNQRSSTSSLKDTFS
Protein: Centromere protein H (CENP-H) (Q90ZF9)
Organism: Gallus gallus (Chicken)
Function: Component of the CENPA-HI complex, a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. Required for the localization of CENPC but not CENPA to the centromere. It however may be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11500386}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11500386}. Note=Associates with active centromere-kinetochore complexes throughout the cell cycle.
Interaction partners:
- Uncharacterized protein.
- Centromere protein S
- Centromere protein K
- Centromere protein T
- Centromere protein M
- Centromere protein L
- Centromere protein N
- Centromere protein I
- Centromere protein P
- Centromere protein O
Sequence:
MAGRLSESVGSGPGAEAETAADPDAKRDVLEHLCARTHLKQLVMEFDTACPPDEGCNSGAEVNFIESAKETLEEVGKVKSAFESKALVIKRIQLMDALRKRVKENDGCARLIVETMRDIIKLNWEIIQAHQQARVIRENLNDIRRKRYFLKQAEGEKALRIFTTVRKKKEVVRMKIAEKLKFIHRNVQYERKVTTLVQNILQNIIVGCQINWAKDPSLRAIILQLEKDISIQNLL
Protein: Peripheral-type benzodiazepine receptor-associated protein 1 (PRAX-1) (Peripheral benzodiazepine receptor-interacting protein) (PBR-IP) (RIMS-binding protein 1) (RIM-BP1) (TSPO-associated protein 1) (O95153)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9915832}. Mitochondrion {ECO:0000269|PubMed:9915832}. Note=Preferentially expressed in the mitochondria in the presence of TSPO.
Interaction partners:
- Translocator protein
- Regulating synaptic membrane exocytosis protein 1
- Regulating synaptic membrane exocytosis protein 2
- Protein unc-13 homolog B
- Ras-related protein Rab-3A
- Ras-related protein Rab-3C
- Golgi resident protein GCP60
Sequence:
MEQLTTLPRPGDPGAMEPWALPTWHSWTPGRGGEPSSAAPSIADTPPAALQLQELRSEESSKPKGDGSSRPVGGTDPEGAEACLPSLGQQASSSGPACQRPEDEEVEAFLKAKLNMSFGDRPNLELLRALGELRQRCAILKEENQMLRKSSFPETEEKVRRLKRKNAELAVIAKRLEERARKLQETNLRVVSAPLPRPGTSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLTLVGKEGPQWLHVRDFDRLLRESQREVLRLQRQIALRNQRETLPLPPSWPPGPALQARAGAPAPGAPGEATPQEDADNLPVILGEPEKEQRVQQLESELSKKRKKCESLEQEARKKQRRCEELELQLRQAQNENARLVEENSRLSGRATEKEQVEWENAELRGQLLGVTQERDSALRKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQARLSLREKQEEVRRLQQAQAEAQREHEGAVQLLESTLDSMQARVRELEEQCRSQTEQFSLLAQELQAFRLHPGPLDLLTSALDCGSLGDCPPPPCCCSIPQPCRGSGPKDLDLPPGSPGRCTPKSSEPAPATLTGVPRRTAKKAESLSNSSHSESIHNSPKSCPTPEVDTASEVEELEADSVSLLPAAPEGSRGGARIQVFLARYSYNPFEGPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVERVSDDDLLTSLPPELADLSHSSGPELSFLSVGGGGSSSGGQSSVGRSQPRPEEEDAGDELSLSPSPEGLGEPPAVPYPRRLVVLKQLAHSVVLAWEPPPEQVELHGFHICVNGELRQALGPGAPPKAVLENLDLWAGPLHISVQALTSRGSSDPLRCCLAVGARAGVVPSQLRVHRLTATSAEITWVPGNSNLAHAIYLNGEECPPASPSTYWATFCHLRPGTPYQAQVEAQLPPQGPWEPGWERLEQRAATLQFTTLPAGPPDAPLDVQIEPGPSPGILIISWLPVTIDAAGTSNGVRVTGYAIYADGQKIMEVASPTAGSVLVELSQLQLLQVCREVVVRTMSPHGESADSIPAPITPALAPASLPARVSCPSPHPSPEARAPLASASPGPGDPSSPLQHPAPLGTQEPPGAPPASPSREMAKGSHEDPPAPCSQEEAGAAVLGTSEERTASTSTLGEKDPGPAAPSLAKQEAEWTAGEACPASSSTQGARAQQAPNTEMCQGGDPGSGLRPRAEKEDTAELGVHLVNSLVDHGRNSDLSDIQEEEEEEEEEEEEELGSRTCSFQKQVAGNSIRENGAKSQPDPFCETDSDEEILEQILELPLQQFCSKKLFSIPEEEEEEEEDEEEEKSGAGCSSRDPGPPEPALLGLGCDSGQPRRPGQCPLSPESSRAGDCLEDMPGLVGGSSRRRGGGSPEKPPSRRRPPDPREHCSRLLSNNGPQASGRLGPTRERGGLPVIEGPRTGLEASGRGRLGPSRRCSRGRALEPGLASCLSPKCLEISIEYDSEDEQEAGSGGISITSSCYPGDGEAWGTATVGRPRGPPKANSGPKPYPRLPAWEKGEPERRGRSATGRAKEPLSRATETGEARGQDGSGRRGPQKRGVRVLRPSTAELVPARSPSETLAYQHLPVRIFVALFDYDPVSMSPNPDAGEEELPFREGQILKVFGDKDADGFYQGEGGGRTGYIPCNMVAEVAVDSPAGRQQLLQRGYLSPDILLEGSGNGPFVYSTAHTTGPPPKPRRSKKAESEGPAQPCPGPPKLVPSADLKAPHSMVAAFDYNPQESSPNMDVEAELPFRAGDVITVFGGMDDDGFYYGELNGQRGLVPSNFLEGPGPEAGGLDREPRTPQAESQRTRRRRVQC
Protein: Renin (EC 3.4.23.15) (Angiotensinogenase) (Renin-like aspartic protease EOC123) (SVAP EOC123) (Snake venom aspartic protease EOC123) (Q18DC8)
Organism: Echis ocellatus (Ocellated saw-scaled viper)
Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney (Probable). This protein is also found in snake venom and shown to specifically cleave human and porcine angiotensinogen into angiotensin I. It does not have general protease activity, no cleavage of alpha or beta casein. May be directly responsible for elevation of blood pressure in the victims of envenomation.
Subcellular location: Secreted {ECO:0000269|PubMed:28734982}.
Interaction partners:
Sequence:
MLQSWEFVLLISCFLCFSSDALQRISLKKMPSIRETLQEMGMKVADVLPSLKHRFSYLDEGLHNKTASTILTNFRDTQYYGEISIGTPAQIFKVVFDTGSSNLWVPSHQCSPLYSACVSHNRYDSSESSTYKPKGTKITLTYGQGYIEGFLSQDIVRVADIPITQFFTEAIALPSIPFMYAHFDGVLGMGYPKQAIGGVIPVFDNIMSEKVLSENVFSVYYSRHSESNTGGEIILGGSDPSHYTGDFHYVSTSREGYWHVDLKGVSIENKIALCHDGCTATIDTGTSFISGPASSISVLMETIGATLSRGDYVIDCNQINLLPDISFHLGDMTYSLSSSTYVLKYSDETECTVAFSAIDIPPPRGPLWLLGATFIKQYYIEFDRQNNRIGFATSF
Protein: Mycocerosic acid synthase (P96291)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MESRVTPVAVIGMGCRLPGGINSPDKLWESLLRGDDLVTEIPPDRWDADDYYDPEPGVPGRSVSRWGGFLDDVAGFDAEFFGISEREATSIDPQQRLLLETSWEAIEHAGLDPASLAGSSTAVFTGLTHEDYLVLTTTAGGLASPYVVTGLNNSVASGRIAHTLGLHGPAMTFDTACSSGLMAVHLACRSLHDGEADLALAGGCAVLLEPHASVAASAQGMLSSTGRCHSFDADADGFVRSEGCAMVLLKRLPDALRDGNRIFAVVRGTATNQDGRTETLTMPSEDAQVAVYRAALAAAGVQPETVGVVEAHGTGTPIGDPIEYRSLARVYGAGTPCALGSAKSNMGHSTASAGTVGLIKAILSLRHGVVPPLLHFNRLPDELSDVETGLFVPQAVTPWPNGNDHTPKRVAVSSFGMSGTNVHAIVEEAPAEASAPESSPGDAEVGPRLFMLSSTSSDALRQTARQLATWVEEHQDCVAASDLAYTLARGRAHRPVRTAVVAANLPELVEGLREVADGDALYDAAVGHGDRGPVWVFSGQGSQWAAMGTQLLASEPVFAATIAKLEPVIAAESGFSVTEAITAQQTVTGIDKVQPAVFAVQVALAATMEQTYGVRPGAVVGHSMGESAAAVVAGALSLEDAARVICRRSKLMTRIAGAGAMGSVELPAKQVNSELMARGIDDVVVSVVASPQSTVIGGTSDTVRDLIARWEQRDVMAREVAVDVASHSPQVDPILDDLAAALADIAPMTPKVPYYSATLFDPREQPVCDGAYWVDNLRNTVQFAAAVQAAMEDGYRVFAELSPHPLLTHAVEQTGRSLDMSVAALAGMRREQPLPHGLRGLLTELHRAGAALDYSALYPAGRLVDAPLPAWTHARLFIDDDGQEQRAQGACTITVHPLLGSHVRLTEEPERHVWQGDVGTSVLSWLSDHQVHNVAALPGAAYCEMALAAAAEVFGEAAEVRDITFEQMLLLDEQTPIDAVASIDAPGVVNFTVETNRDGETTRHATAALRAAEDDCPPPGYDITALLQAHPHAVNGTAMRESFAERGVTLGAAFGGLTTAHTAEAGAATVLAEVALPASIRFQQGAYRIHPALLDACFQSVGAGVQAGTATGGLLLPLGVRSLRAYGPTRNARYCYTRLTKAFNDGTRGGEADLDVLDEHGTVLLAVRGLRMGTGTSERDERDRLVSERLLTLGWQQRALPEVGDGEAGSWLLIDTSNAVDTPDMLASTLTDALKSHGPQGTECASLSWSVQDTPPNDQAGLEKLGSQLRGRDGVVIVYGPRVGDPDEHSLLAGREQVRHLVRITRELAEFEGELPRLFVVTRQAQIVKPHDSGERANLEQAGLRGLLRVISSEHPMLRTTLIDVDEHTDVERVAQQLLSGSEEDETAWRNGDWYVARLTPSPLGHEERRTAVLDPDHDGMRVQVRRPGDLQTLEFVASDRVPPGPGQIEVAVSMSSINFADVLIAFGRFPIIDDREPQLGMDFVGVVTAVGEGVTGHQVGDRVGGFSEGGCWRTFLTCDANLAVTLPPGLTDEQAITAATAHATAWYGLNDLAQIKAGDKVLIHSATGGVGQAAISIARAKGAEIFATAGNPAKRAMLRDMGVEHVYDSRSVEFAEQIRRDTDGYGVDIVLNSLTGAAQRAGLELLAFGGRFVEIGKADVYGNTRLGLFPFRRGLTFYYLDLALMSVTQPDRVRELLATVFKLTADGVLTAPQCTHYPLAEAADAIRAMSNAEHTGKLVLDVPRSGRRSVAVTPEQAPLYRRDGSYIITGGLGGLGLFFASKLAAAGCGRIVLTARSQPNPKARQTIEGLRAAGADIVVECGNIAEPDTADRLVSAATATGLPLRGVLHSAAVVEDATLTNITDELIDRDWSPKVFGSWNLHRATLGQPLDWFCLFSSGAALLGSPGQGAYAAANSWVDVFAHWRRAQGLPVSAIAWGAWGEVGRATFLAEGGEIMITPEEGAYAFETLVRHDRAYSGYIPILGAPWLADLVRRSPWGEMFASTGQRSRGPSKFRMELLSLPQDEWAGRLRRLLVEQASVILRRTIDADRSFIEYGLDSLGMLEMRTHVETETGIRLTPKVIATNNTARALAQYLADTLAEEQAAAPAAS
Protein: Glycosyl transferase 48 domain-containing protein (Q8HCN4)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MHILSCSCLNVVQMVVIIVYVFLYGRLYLALSGLEFAIMKQARMRGNRALQAAMGSQSIVQLGLLMALPMFMGIGLERGFRSALGDFIIMQLQLCSVFFTFYLGTKSHYFGRTILHGGAKYRATGRGFVVRHVRFAENYRMYSRSHFVKGLELMLLLVVYQLYGDVATDSTAYILLTSSMWFLVITWLFAPFLFNPSGFEWQKIVDDWTKWISSRGGIGVPANKAWESRWEEEQQAAPLPL
Protein: Desmocollin-1 (Cadherin family member 1) (Desmosomal glycoprotein 2/3) (DG2/DG3) (Q08554)
Organism: Homo sapiens (Human)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1713860}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, desmosome {ECO:0000250|UniProtKB:P55849}.
Interaction partners:
- Desmoglein-1
- Corneodesmosin
- Desmoplakin
- Junction plakoglobin
- Plakophilin-1
- Loricrin
- Periplakin
- Filaggrin
- Desmoglein-3
- Plakophilin-3
Sequence:
MALASAAPGSIFCKQLLFSLLVLTLLCDACQKVYLRVPSHLQAETLVGKVNLEECLKSASLIRSSDPAFRILEDGSIYTTHDLILSSERKSFSIFLSDGQRREQQEIKVVLSARENKSPKKRHTKDTALKRSKRRWAPIPASLMENSLGPFPQHVQQIQSDAAQNYTIFYSISGPGVDKEPFNLFYIEKDTGDIFCTRSIDREKYEQFALYGYATTADGYAPEYPLPLIIKIEDDNDNAPYFEHRVTIFTVPENCRSGTSVGKVTATDLDEPDTLHTRLKYKILQQIPDHPKHFSIHPDTGVITTTTPFLDREKCDTYQLIMEVRDMGGQPFGLFNTGTITISLEDENDNPPSFTETSYVTEVEENRIDVEILRMKVQDQDLPNTPHSKAVYKILQGNENGNFIISTDPNTNEGVLCVVKPLNYEVNRQVILQVGVINEAQFSKAASSQTPTMCTTTVTVKIIDSDEGPECHPPVKVIQSQDGFPAGQELLGYKALDPEISSGEGLRYQKLGDEDNWFEINQHTGDLRTLKVLDRESKFVKNNQYNISVVAVDAVGRSCTGTLVVHLDDYNDHAPQIDKEVTICQNNEDFAVLKPVDPDGPENGPPFQFFLDNSASKNWNIEEKDGKTAILRQRQNLDYNYYSVPIQIKDRHGLVATHMLTVRVCDCSTPSECRMKDKSTRDVRPNVILGRWAILAMVLGSVLLLCILFTCFCVTAKRTVKKCFPEDIAQQNLIVSNTEGPGEEVTEANIRLPMQTSNICDTSMSVGTVGGQGIKTQQSFEMVKGGYTLDSNKGGGHQTLESVKGVGQGDTGRYAYTDWQSFTQPRLGEKVYLCGQDEEHKHCEDYVCSYNYEGKGSLAGSVGCCSDRQEEEGLEFLDHLEPKFRTLAKTCIKK
Protein: Probable serine/threonine-protein kinase PBL7 (EC 2.7.11.1) (CDG1-like protein 1) (PBS1-like protein 7) (Q0WRY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase involved in the positive regulation of brassinosteroid (BR) signaling and plant growth. Phosphorylates both BSU1 and BSL1 in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21855796}; Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
Interaction partners:
- Subtilisin-like protease SBT4.9
- Subtilisin-like protease SBT4.4
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Putative defensin-like protein 3
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Glutathione S-transferase T3
- Glutathione S-transferase T2
- NDR1/HIN1-like protein 13
- Subtilisin-like protease SBT4.12
- Oligopeptide transporter 4
Sequence:
MGWIPCSGKSSGRNKTRRNGDHKLDRKSSDCSVSTSEKSRAKSSLSESKSKGSDHIVAQTFTFSELATATRNFRKECLIGEGGFGRVYKGYLASTSQTAAIKQLDHNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDISPGKQPLDWNTRMKIAAGAAKGLEYLHDKTMPPVIYRDLKCSNILLDDDYFPKLSDFGLAKLGPVGDKSHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVLLEIITGRKAIDSSRSTGEQNLVAWARPLFKDRRKFSQMADPMLQGQYPPRGLYQALAVAAMCVQEQPNLRPLIADVVTALSYLASQKFDPLAQPVQGSLFAPGTPPRSKRV
Protein: ISG12a protein (Interferon, alpha-inducible protein 27) (Q70LN0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAFSGTGTLVASIVSKMTSSAAMVKAGGAVSGTILAGSKGLILLTQSALGSATSALGALKVGTILSGFSASTLAASPIGAMTVAAVPPALSAVGFTASGIAASSLAAKMMSLSAIANGGGVPAGGLVAILQSAGAAGLSVPSTVIVGSAGSAVVASVMNICESFYPFLMGSEVADMATEVADMAIEVADISTEEALPNLSNTEKD
Protein: Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC 1.5.3.13) (Polyamine oxidase) (Q8C0L6)
Organism: Mus musculus (Mouse)
Function: Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.
Subcellular location: Peroxisome {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Diamine acetyltransferase 1
- Spermine synthase
- S-adenosylmethionine decarboxylase proenzyme 1
- Spermidine synthase
- S-adenosylmethionine decarboxylase proenzyme 2
- Ornithine decarboxylase
- Gene model 853
Sequence:
MAFPGPRVLVVGSGIAGLGAAQKLCSHRAAPHLRVLEATASAGGRIRSERCFGGVVELGAHWIHGPSQDNPVFQLAAEFGLLGEKELSEENQLVDTGGHVALPSMIWSSSGTSVSLELMTEMARLFYGLIERTREFLNESETPMASVGEFLKKEISQQVASWTEDDEDTRKRKLAILNTFFNIECCVSGTHSMDLVALAPFGEYTVLPGLDCILAGGYQGLTDRILASLPKDTVAFDKPVKTIHWNGSFQEAAFPGETFPVLVECEDGARLPAHHVIVTVPLGFLKEHQDTFFEPPLPAKKAEAIKKLGFGTNNKIFLEFEEPFWEPDCQFIQVVWEDTSPLQDTALSLQDTWFKKLIGFLVQPSFESSHVLCGFIAGLESEFMETLSDEEVLLSLTQVLRRVTGNPQLPAAKSVRRSQWHSAPYTRGSYSYVAVGSTGDDLDLMAQPLPEDGTGTQLQVLFAGEATHRTFYSTTHGALLSGWREADRLVSLWDSQVEQSRPRL
Protein: Transmembrane protein 106A (Q8VC04)
Organism: Mus musculus (Mouse)
Function: Activates macrophages and polarizes them into M1-like macrophages through the activation of the MAPK and NF-kappaB signaling pathway. Upon activation, up-regulates the expression of CD80, CD86, CD69 and MHC II on macrophages, and induces the release of pro-inflammatory cytokines such as TNF, IL1B, IL6, CCL2 and nitric oxide. May play a role in inhibition of proliferation and migration (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26215746}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKAVSQLTSRKDEDKPILPDNPAMASQAANYFSTGSSKPAHSCMPYEKAASSSFVTCPTCQGNGEIPQEQEKQLVALIPYGDQRLKPRRTKLFVFLSVAICLLIFSLTIFFLYPRPIAVRPVGLNSSTVTFEDAHVQLNTTNVLNIFNSNFYPITVTQLTAEVLHQASVVGQVTSSLRLHIGPLASEQMPYEVASRILDENTYKICTWPKIRVHHILLNIQGSLTCSFLSHPQQLPFESFEYVDCRENMSLPHLELPRPA
Protein: Probable export or membrane protein (P71810)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Carbamoyl phosphate synthase large chain
- Dihydroorotase
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase small chain
- Orotidine 5'-phosphate decarboxylase
- Bifunctional protein PyrR
- Uncharacterized protein Rv2265
- Uncharacterized protein Rv2325c
- Uncharacterized protein
- UPF0102 protein Rv2898c
Sequence:
MNSGTLAGSLIFAAVLVMLIAVLARLMMRGWRRRSERQAELLGDLPDVPEHVSSATVTTRGLYVGATLSPAWNERVTVGDLGYRSKAVLTRYPSGIMVERARAQPIWIPTESIAAIRMERGVAGKVVAGIGILAIRWRLPSGTEIDVGFRADNRDEYQEWLEEPV
Protein: Putative F-box/LRR-repeat protein At3g59160 (Q9LX55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVDSKRMDSGSKDMINDLPDALLCHVLSYLTTKEAASTSLLSRRWRYLLAFVPNLEFDDSAYLHRDKRVKNPLHEKGLVGFVLTVDDKRKKLSTSFPDFVDRILDLQGNSPLDKFSLKMVDDHDPVDPDCVAPWIHKVLVRGVSDLHLVIDMNEWTSLPAKIFLTETLVKLTLKIRDGPPIDVKHVHLPKLKTLHLESVMFDEEDIGFSKLLSGCPELEELVLHHIWSCVWTSCSVSVATLKRLTFCCNNMKFCGMHEENPNNVSFDTPNLVYLEYAEVIANNYPKVNFDSLVEAKIDIWMTNDQLDEVRIRDIYEKNVMVGNATDLIVGIRNVRVLCLSADTLEVLTYCCKQIPIFNNLTHVTIQSTPKVGWKSLLKLLKNSPKLQTLVFQGLLHRDTKEEGVAIIKIEKQIEKVKHFLETMPHLEQLVLHYDSSIDGDMKQLLMLSSLASPKCKVQLIPLVT
Protein: Golgi SNAP receptor complex member 1 (28 kDa Golgi SNARE protein) (28 kDa cis-Golgi SNARE p28) (GOS-28) (GOS28) (Q62931)
Organism: Rattus norvegicus (Rat)
Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10585748, ECO:0000269|PubMed:10747018, ECO:0000269|PubMed:11323436, ECO:0000269|PubMed:11748249, ECO:0000269|PubMed:11927603, ECO:0000269|PubMed:12388752, ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:18648846, ECO:0000269|PubMed:20450495, ECO:0000269|PubMed:9382863, ECO:0000269|PubMed:9647643}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10585748, ECO:0000269|PubMed:10747018, ECO:0000269|PubMed:11323436, ECO:0000269|PubMed:11748249, ECO:0000269|PubMed:11927603, ECO:0000269|PubMed:12388752, ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:18648846, ECO:0000269|PubMed:20450495, ECO:0000269|PubMed:9382863, ECO:0000269|PubMed:9647643}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network. Enriched on vesicular components at the terminal rims of the Golgi apparatus.
Interaction partners:
- Golgi SNAP receptor complex member 2
- BET1 homolog
- BET1-like protein
- Syntaxin-5
- Synaptobrevin homolog YKT6
- Golgin subfamily A member 2
- General vesicular transport factor p115
- Golgin B1
- Sec1 family domain-containing protein 1
- Vesicle-trafficking protein SEC22b
Sequence:
MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSARDGGRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTHSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFMAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH