wanglab/gogpt-training-data huggingface dataset:
Protein: Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (Solute carrier family 1 member 4) (P43007)
Organism: Homo sapiens (Human)
Function: Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine.
Subcellular location: Membrane {ECO:0000269|PubMed:17081065}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Syncytin-1
- High affinity cationic amino acid transporter 1
- Amino acid transporter heavy chain SLC3A2
Sequence:
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGAALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAYFGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFPSNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKLGSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFASILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENNGVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGAAGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQKATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
Protein: Proton-coupled zinc antiporter SLC30A5 (Solute carrier family 30 member 5) (Zinc transporter 5) (ZnT-5) (Q5ZLF4)
Organism: Gallus gallus (Chicken)
Function: Together with SLC30A6 forms a functional proton-coupled zinc ion antiporter mediating zinc entry into the lumen of organelles along the secretory pathway. By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15525635}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in early compartments of the secretory pathway including COPII-coated vesicles and the Golgi cis cisterna. {ECO:0000250|UniProtKB:Q8TAD4}.
Interaction partners:
- Zinc transporter ZIP9
- Zinc transporter ZIP13
- Zinc transporter 6
- Solute carrier family 30 member 10.
Sequence:
MEEKYSSQALAGGGVLGPVDVPSARLTRYIVLLCFAKFLKAVGLFESYDLLKAVHLVQFIFIVKLGSAFFMVLFQKPFSSGKVVTKHQWIKIFKHAVVGCIISLLWFFGLTLCGPLRTLLLFEHSDVVVLSLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKIAEHPEGHHDSALTHVLYTVIAFLGVADHKGGVLLLVLALCCKVGFHMASRKLSVDVGGAKRLQALSHLVSVLLLCPWVIVLSLTTESKVESWSSLIMPFITVIFFVVILDFYVESICSVKMESSKCARYGSFLIFISALLFGNFWTHPITDQLRAMNKPAHHESTEHVLSGGVVVSAVFFILSANILSSPSRKGQKGTLIGYSPEGTPLYNFMGDAIQQSSQSLPRFIKESLKQILEEYDSRQIFYFLCLNLAFTFVELFYGVWTNSLGLISDGFHMLFDCSALVMGLFAALMTRWKATRIFSYGYGRVEILSGFINGLFLMVIAFFVFMESVARLVDPPDIDTNMLTPVSVGGLIVNLVGICAFSHAHSHGASRGGCHSHEHSHSYHGHSHSHGHGHSHNDHGHSHGHSHVSSGGGMNTNMRGVFLHVLADTLGSVGVIVSTTFIQQFGWLIADPLCSLFIATLIFLSVIPLLKDACQVLLLRIPPEQEKDLHAALEKIQKIDGVISYRDPHFWCHSASVVAGTIHVQVVSDVMEQRIVQQVTAILKDAGVNNLTVQVEKEAYFQHMSGLSTGFQDVLAMTQHLESMKYYKDGTYIM
Protein: Ribosomal RNA processing protein 6 (Q581R8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Ribosomal RNA processing protein 45
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 4
- Exosome component CSL4
- Exosome complex exonuclease RRP40
- ATP-dependent DEAD/H RNA helicase, putative
- U3 small nucleolar RNA-associated protein 14
- Exosome-associated protein 4
- Sas10 C-terminal domain-containing protein
Sequence:
MLLMLVSIHLFQTRGHARAEIFLPLTLSKGVGYMSGSLPQTKDLVNGAFTLVKEYTKLTADLAEEDYDYHMAFPAFRHQITRHSEAVVSLMDKFCQLLPAKRRVTLSSTGGKLTDPQRAAVMEAADSLLENVDGLLDELKGRRLSAKDQLSVKFGSELQGVVPSSSYSVFNAAGVSVLRPQLTFEHPVDNSPTPFRPVYYDEKGVRHVGEPGVHPFAERIKAVSVPSEQLLLKTETPYLSLVTCPLTFVDTVEDLEALVAVLLNETEIAVDLEHHDFYSYQGFTCLMQISTRTQDFIVDCLKVRANMYLMAPVFLQPNIVKVFHGAREDVRWLQKDFGLYIVNLFDTSIALQNLHMPHSLAFAVDHFCQVKLNKKYQTADWRVRPIPAEMVSYAQQDTHFLLYVYDRLKQLLLNCEARASVGNMLLHVFQESRLLSLERYEKPHLDPDVTYKQALGRSLGGLSSSQLQVAREIFNWRDMAAREADDSPSAVMHISCVLSIATKLPTSANEVLKCCSPVSVAVRTNVMKLLQIVKDAIGSADSLKDGANGDVKPKPLPNVGVALRYMGVHRSMTGTLPSIEQRADPAFTVEDAHVVVRTEPSAWFETMRNVAAILRRKPYYPIALPGHDVVTRMSAVKRAREVEEMKVKGEGEEEEKRVHVDAEEPTVERENSSERGEGMAGPCLHEGLEVKDEVEEIDVPTQKPLELKEGAISLRQQYGTGSANRKKARLGKKNKS
Protein: Nickel transport system permease protein NikC (P0AFA9)
Organism: Escherichia coli (strain K12)
Function: Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Nickel-binding periplasmic protein
- Nickel transport system permease protein NikB
- Nickel import ATP-binding protein NikE
- Nickel import ATP-binding protein NikD
- Dipeptide transport ATP-binding protein DppD
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Oligopeptide transport ATP-binding protein OppD
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Oligopeptide transport ATP-binding protein OppF
- Dipeptide transport ATP-binding protein DppF
Sequence:
MNFFLSSRWSVRLALIIIALLALIALTSQWWLPYDPQAIDLPSRLLSPDAQHWLGTDHLGRDIFSRLMAATRVSLGSVMACLLLVLTLGLVIGGSAGLIGGRVDQATMRVADMFMTFPTSILSFFMVGVLGTGLTNVIIAIALSHWAWYARMVRSLVISLRQREFVLASRLSGAGHVRVFVDHLAGAVIPSLLVLATLDIGHMMLHVAGMSFLGLGVTAPTAEWGVMINDARQYIWTQPLQMFWPGLALFISVMAFNLVGDALRDHLDPHLVTEHAH
Protein: Thyrotropin-releasing hormone receptor (Thyroliberin receptor) (Q9ERT2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Pro-thyrotropin-releasing hormone
- Thyrotropin-releasing hormone receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MDGPSNVSLVHGDTTLGLPEYKVVSVLLVLLVCTVGIVGNAMVVLVVLTSRDMHTPTNCYLVSLALADLIVLLAAGLPNVSDSLVGHWIYGHAGCLGITYFQYLGINVSSCSILAFTVERYIAICHPMRAQTVCTVARARRIIAGIWGVTSLYCLLWFFLVDLNVRDNQRLECGYKVSRGLYLPIYLLDFAVFFIAPLLGTLVLYGFIGRILFQSPLSQEAWQKERQSHGQSEGTPGNCSRSKSSMSSRKQATRMLAVIVLLFAVLWTPYRTLVLLNSFLARPFLDPWVLLFCRTCVYTNSAINPVIYSLMSQKFRAAFLKLCWCRAAGSQRRAACAPTSNYSAAQETSLGTEKMQLGSREVSGPAAAASLRCQHEPHFSVL
Protein: Trafficking protein particle complex subunit (A0A087WWM0)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, cis-Golgi network {ECO:0000256|ARBA:ARBA00004222, ECO:0000256|PIRNR:PIRNR018293}.
Interaction partners:
Sequence:
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDKILFSNFLPRGFNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSSLIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
Protein: S-adenosylmethionine synthase (EC 2.5.1.6) (Q7K6A4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- DNA
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, apicoplast
- Spermidine synthase
- Homocysteine S-methyltransferase, putative
- Ribosomal protein L16, mitochondrial, putative
- Adenosylhomocysteinase
- GDP-L-fucose synthase
- Aspartate aminotransferase
- Phosphoglycerate kinase
- Ornithine aminotransferase
Sequence:
MSQLKIKRGNFLFTSESVNEGHPDKICDQISDAILDSCLREDPYSKVACEVCAKKNYIFIFGEITTKAKVNYDKVTRDVLKHIGYDDESKGLDYKTAEIKVSIDEQSPDIAQCVHENRSPELIGAGDQGIMFGYATDETENYMPLTHHYATLLGKRLTEVRKLGILPYLGPDGKTQITIEYKNKGSCGGHLEPLRVHTVLISTQHAEDIKYEQLKTDLMENVIKYVIPEKLLDNETLYYLNPSGKFVLGGPAADAGLTGRKIICDTYGGWGAHGGGAFSGKDASKVDRSAAYYLRFIAKSLVANKFCRRVLVQASYSIGIANPISLNVNSYGTVSTGYTDYDLEQIILRNFDLRPGFIIQELKLTEPVFSKTSAYGHFGREGDTFTWEKIKDLSHEKNALKN
Protein: Nuclear hormone receptor family member nhr-153 (O01929)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MTPPQKSKPKRNRRKIYKILPQNQCPSVCQICRNPAIGYHYEVPSCNGCKTFFRRTIITGRKFKCFKVSNCLDGNDVIDTSKRVCRACRFEKCVQAGMNPMAIQAEAKTDEGEELKKLIAKKFENGEKLNDGTVFFNVHDRLNQILGKLIKIETKLEKVHDNGMPMGFLDQRDLSTALSSKVIYNNMEIPSMSYTPVKISKNTGLPKRRSRNFVHSSCLASIEYSKTFDFSSAIDISSKIILLKNTALSCANLTNAYTTFRKLKSDTLLYPDGSIYGPPRRKNGPLIEKQRSFLQNTLISFMTNNVDKTEYILLKAIVLCNPAIIDLPYADSKHIQREREVYAQCLFRYCLLQHGTLHGPARFSALLSIFNVLENQQKEQKDYYLYIKLIHSQKHKDPEVLKKKCISVIYDQIMD
Protein: Gliolectin (Q9VD73)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has a role in intercellular carbohydrate-mediated cell adhesion.
Subcellular location: Membrane {ECO:0000269|PubMed:8631270}; Single-pass type II membrane protein {ECO:0000269|PubMed:8631270}.
Interaction partners:
- IP10051p
- Uncharacterized protein
Sequence:
MLCPPMALGPFLAAPVPRPPPSASEKKRICRNLFNNAPGDSNIDQLLAQEQHTQRLYVKERYGYDIQLESNRDADANTDADADTDAHCQVLRGMRYPTSRTISSTDADECNPKAVSQAPRGMALTPAQISASAKLILQKCPESDRKKSNGSADLANCTRHGQKPYARQPQGLKGMYNVRKTVNGISKPNVKNGYNNNNNSSSSNNNSNMNINNKIVDNGTSELADQKQ
Protein: Protein yippee-like (H0YKL4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XRAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKP
Protein: Histone H2A deubiquitinase MYSM1 (2A-DUB) (EC 3.4.19.-) (Myb-like, SWIRM and MPN domain-containing protein 1) (Q5RGA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- Histone acetyltransferase KAT2B
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome 26S subunit, non-ATPase 6.
- Proteasome 26S subunit, ATPase 3
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasome subunit beta
- Proteasome subunit alpha type
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome non-ATPase regulatory subunit 3
- Proteasome subunit alpha type
Sequence:
MADELDVVDIEGDECDEIVGDLSSAEILQDQYLQSAWRTNSSVLPWTLDSSISDENRQVIESMLLEEQYYFASKKAPKVAWTNEKTKVKKPLVKSSAAQTRWAEEEKELFEKGLAQFGRRWTKIAKLIGTRTVLQVKSYAKQYFKNKPKAEPAAEVTSANVTSVSSIQPHVSALTNAVRIERLSDDEDVDITDDFSDSELQSKKQPERSVSPDCNHHGELRPSLSDALLHLPSESTAADGQADPDFSEDTEIHHSEIDSEAVEESGNPFINLDSPSKHSLTGEEETELADKCESAECLEEEVEDQEEDEEEELRAPEQEVELDLNTITEEEKQAISEFFEGRPSKTPERYLKIRNYILDQWRRSKPKYLNKTSVRPGLKNCGDVNCIGRIHTYLELIGAINFNCDQAIYNRPRLVDRSRLKESKDSLEAYHLAQRLQSMRTRKRRIRDVWGNWCDAKDLEGQTYEHLSAEELAIRREEMKKKGPRPSKLPKQRGSFDPFQLIPCKTFGEERQEPYSVIVCAEALIVMDIHAHVSMGEVIGLLGGTYEEEDKVLKICSAEPCNSLSTGLQCEMDPVSQTQASEVLGVKGLSVVGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAPFIGMIVSPYNPSNSSPQSQSTCLLVQEEPGPSGSHKFPYQFNMQCSAEPPDWSEVMRRAEWVVFKYRLCHGSVPMDRLFRRDSSLTCLEKMLLSIRTVLERLSEVDIETFLVQLESLFNTHFLSETGSSSTHLYETATQPQLLSFLSSEPISSSATEETSDGHDEPNTTGPDKLEQSCVEEEHDETVMQSTSAETV
Protein: Dynein (Q9TW74)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PALVARHLTKLYDSMGKLNLISGSKNAAGMVAKELEEYVPFLENCDCSGKVEVWLNRITDKMRDTLRDQLKRSLTFYDHKPRHVWIFEWPAHAALVGTQIMWTTETNDAFAKVQQRYENALKDYNKKQITQLNNLIILLLGDLTAAERQKIMTICTIDVHSRDVVGTIIAKKVEVQTAFQWQSQLRHRWDPKIDDCFANICDAQFRYDYEYLGNTPRLVITPLTDRCYITLTQSLHLVMGGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYKSIGDIHKGLAQTGAWGCFDEFNRISVEVLSVVAVQVKCIQDAIKSKKQTFSFLGEHIALRTTVGVFITMNPGYAGRAELPENLKALYRPCAMVVPDFALISEIMLVAEGFQEARLLARKFITLYTLCKELLSKQDHYDWGLRAIKTVLVVAGALRRDDRQRPEDQVLMRALRDFNIPKIVTDDVPVFMGLIGDLFPALDVPRKRNPEFEAVIKRSALDLKLQPEDGFILKIVQLEELFAVRHSVFIIGFAGTGKSEVWKTLNKTYQNQKRKPHYNDLNPKAVTNDELFGIVNPSTREWKDG
Protein: Mating-type switching protein swi1 (Replication fork protection complex subunit swi1) (Q9UUM2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Forms a fork protection complex (FPC) with swi3. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. It is required for programmed fork-pausing which is necessary for mating-type switching. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors. It is involved in termination at the mat1-proximal polar-terminator of replication (RTS1) and also required for activation of the Rad53-like checkpoint kinase cds1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14560029, ECO:0000269|PubMed:15367656}. Note=Associated with chromatin during S phase. Nuclear accumulation requires swi3.
Interaction partners:
- Swi1-interacting protein swi3
- Mediator of replication checkpoint protein 1
- DNA replication licensing factor mcm2
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm7
- Minichromosome loss protein 1
- DNA replication licensing factor mcm5
- Replication factor A protein 1
- DNA replication licensing factor mcm3
Sequence:
MELDEVIQGIVSAIGGFDYSDDEKVYVLGDEALACLKDLKRYLQVVDEKYKVWQIRSLLSSLQLVTNDICPILSDWDKDITNYRNWRIALACVELLVPLTWPLETEHETFRENVDVLYNLRQAQSNYKNSILSYKKGSVLSAILAVLLKPLSTPAESRTLRDKGIIRIVLLLFRNILQIDELKTKNETIISFAKAHILDLIVTLVSNLDEFEHFDVYILEIVYNLIRGCKPSALFSDASLTNSQTELNSLLLKESTQNRYLKRNAHTRHNRFGTMLSVQTEDRRFTIASQNIKTDGLDELDSHKRFRKRGTRRKHFDDINKSFFINTEAGTALRNFAVEFLEAGFNPLFQSLLKDLEREDPRVLPIHKMQLLYVQSFFLEFMRFSSKPKKTEEIYSNDYSFGLAASVFDQRALIMHNRLMVESFEMKQWSTFQASMLSMTQLLFTLRSMTLCSSEIYQRIADNLLSNIFYQEEILLLVYSALKHFKTQSFGYLDAITELTIVLLKELEKFSSAKQYLYVKKRRRNQKSVDSNVLESDEDEESSLINANAAVEDRLFDFGRYESRYCDNGCIDSFVLFLQCYQDLDSKQIHRAISFFYRIFVKQKCHVYLYRLDFLRVLDKMFNDHVYFSTTNSARQDFEQFFVYYMRKLSDALKDVPALFIELPFPKLTDTFYYLEYGKSPLFSIHGSRKGPLYETVPGLSHLEKVAAVVACLINENKSDLLDELKVQLNCLISERKLITLADENKYINEGGNDGERMGKNLKGDTDSFNTALLKDGKFRLLLELCGFEESDNNIDVQALWKLPNSVIIDELVEHAMLLRRFTDDPPTFEGTKPEDLLVRKQRGNVRLPSSSEGETSDEEIEFEADDPITFANRREALNKITDRKRKKMKTNETIIDHTTRKKKENHLRSAKYIVDSDDDSETDIAFFQSEAALREKNAQKASALFKRIDDLEMEGKLQEIEQLSENSSSD
Protein: Polyamine aminopropyltransferase (Diamine/triamine aminopropyltransferase) (Norspermidine aminopropyltransferase) (EC 2.5.1.126) (Norspermine synthase) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Thermospermine synthase) (Q8ZXM4)
Organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine and 1,3-diaminopropane to yield norspermine, and to spermidine to yield thermospermine. It can also synthesize thermospermine from putrescine (1,4-diaminobutane) and caldopentamine from norspermine with a very low activity. The biosynthesis of caldohexamine and caldoheptamine from caldopentamine has been also observed.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Arginine decarboxylase proenzyme
- Agmatinase
- S-methyl-5'-thioadenosine phosphorylase
- Purine nucleoside phosphorylase
- Coenzyme A biosynthesis bifunctional protein CoaBC
Sequence:
MSKVPGPIVLMEPLSGKTSLIIKINAIHVSKRSKYQGILIVDTDDYGRTLVLDDYIQSSYYDEIYYHESLVHPAVTTHPRPSDVLILGGGEGATLREVLKHNTVKRAVMVDIDGDVVELSKKYLPQMHQGAFDDPRSEVRIEDGFVYVENALKRGEKFDVVIMDLTDPYSSDIAKQLYTPEFFGKVKRLLREDGIVVTQAGNSFYFPEAYDYVLQGVKGNFPIIAEYSVWIPSFGYAVNFVLGSLKHDPHSLSAEEVDKRLSERGVRAEFYSGKTHIALMNMPVIKKILRV
Protein: Claudin (Q7T2E7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|RuleBase:RU060637}. Cell membrane {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU060637}.
Interaction partners:
- Claudin 12 isoform fc43a12
- WD repeat and FYVE domain-containing 2
- Tight junction protein 3
- Tight junction protein 1a
- Claudin
- Claudin 18
- Claudin
- Claudin-7-B
- Translation initiation factor eIF2 assembly protein
- Claudin-3
Sequence:
MDPIIEAVALFLGFVSWTMVGITIPNRYWKVSSLDGTVITTSTLYENLWMSCATDSTGVHQCREFPSLLALSGYIQASRALMIAAVVSGTFGVVATLIGMQCSKAGGENYVLKGRIAGTGGVFFLLQGLCTMISVSWYAANITQEFFNPLYPGQKYEIGEALYIGWASAVLAICGGVCLMFSCKLGTEKKTAYSYHPTRETVYSASASRRETQSTYGKNAYV
Protein: Protein kinase C eta type (EC 2.7.11.13) (PKC-L) (nPKC-eta) (Q64617)
Organism: Rattus norvegicus (Rat)
Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase A-Raf
- RAF proto-oncogene serine/threonine-protein kinase
- Transient receptor potential cation channel subfamily V member 4
Sequence:
MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCTNVSDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGTSDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQVNGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDAKIAEQRFGINIPHKFNVHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLISRSTLRRQGKEGSKEGNGIGVNSSSRFGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHEILRHPFFKEIDWVQLNHRQLEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP
Protein: Heat shock 70 kDa protein 12B (Heat shock protein family A member 12B) (Q96MM6)
Organism: Homo sapiens (Human)
Interaction partners:
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 12A
- Heat shock 70 kDa protein 13
- Heat shock 70 kDa protein 14
- Stress-70 protein, mitochondrial
- Heat shock 70 kDa protein 4L
- A-kinase anchor protein 12
- Endoplasmic reticulum chaperone BiP
- Heat shock 70 kDa protein 6
Sequence:
MLAVPEMGLQGLYIGSSPERSPVPSPPGSPRTQESCGIAPLTPSQSPKPEVRAPQQASFSVVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYFEKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQELREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMREAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQLLDLSGRAPGGGRLGERRSIDSSFRQAREQLRRSRHSRTFLVESGVGELWAEMQAGDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQRPAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPTVSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDVGLTILKGAVLFGQAPGVVRVRRSPLTYGVGVLNRFVPGRHPPEKLLVRDGRRWCTDVFERFVAAEQSVALGEEVRRSYCPARPGQRRVLINLYCCAAEDARFITDPGVRKCGALSLELEPADCGQDTAGAPPGRREIRAAMQFGDTEIKVTAVDVSTNRSVRASIDFLSN
Protein: ATPase 10, plasma membrane-type (EC 7.1.2.1) (Proton pump 10) (Q43128)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Protein DETOXIFICATION 41
- Glutathione S-transferase F12
- Transcription factor TT8
- Transcription factor TT2
- Dihydroflavonol 4-reductase
- Anthocyanidin reductase
- Protein TRANSPARENT TESTA 1
- Soluble inorganic pyrophosphatase 5
- Soluble inorganic pyrophosphatase 4
- Leucoanthocyanidin dioxygenase
Sequence:
MAEDLDKPLLDPDTFNRKGIDLGILPLEEVFEYLRTSPQGLLSGDAEERLKIFGPNRLEEKQENRFVKFLGFMWNPLSWVMEAAALMAIALANSQSLGPDWEDFTGIVCLLLINATISFFEENNAGNAAAALMARLALKTRVLRDGQWQEQDASILVPGDIISIKLGDIIPADARLLEGDPLKIDQSVLTGESLPVTKKKGEQVFSGSTCKQGEIEAVVIATGSTTFFGKTARLVDSTDVTGHFQQVLTSIGNFCICSIAVGMVLEIIIMFPVQHRSYRIGINNLLVLLIGGIPIAMPTVLSVTLAIGSHRLSQQGAITKRMTAIEEMAGMDVLCCDKTGTLTLNSLTVDKNLIEVFVDYMDKDTILLLAGRASRLENQDAIDAAIVSMLADPREARANIREIHFLPFNPVDKRTAITYIDSDGKWYRATKGAPEQVLNLCQQKNEIAQRVYAIIDRFAEKGLRSLAVAYQEIPEKSNNSPGGPWRFCGLLPLFDPPRHDSGETILRALSLGVCVKMITGDQLAIAKETGRRLGMGTNMYPSSSLLGHNNDEHEAIPVDELIEMADGFAGVFPEHKYEIVKILQEMKHVVGMTGDGVNDAPALKKADIGIAVADATDAARSSADIVLTDPGLSVIISAVLTSRAIFQRMRNYTVYAVSITIRIVLGFTLLALIWEYDFPPFMVLIIAILNDGTIMTISKDRVRPSPTPESWKLNQIFATGIVIGTYLALVTVLFYWIIVSTTFFEKHFHVKSIANNSEQVSSAMYLQVSIISQALIFVTRSRGWSFFERPGTLLIFAFILAQLAATLIAVYANISFAKITGIGWRWAGVIWLYSLIFYIPLDVIKFVFHYALSGEAWNLVLDRKTAFTYKKDYGKDDGSPNVTISQRSRSAEELRGSRSRASWIAEQTRRRAEIARLLEVHSVSRHLESVIKLKQIDQRMIRAAHTV
Protein: Aquaporin NIP2-1 (NOD26-like intrinsic protein 2-1) (ZmNIP2-1) (ZmNIP2;1) (Q19KC1)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Silicon transporter
- Aquaporin SIP1-1
- Aquaporin SIP2-1
Sequence:
MSTNSRSNSRANFNNEIHDIGTAQNSSMPPTYYDRSLADIFPPHLLKKVVSEVVSTFLLVFVTCGAAGIYGSDKDRISQLGQSVAGGLIVTVMIYAVGHISGAHMNPAVTLAFAVFRHFPWIQVPFYWAAQFTGSICASFVLKAVLHPIAVLGTTTPTGPHWHSLVIEIIVTFNMMFVTLAVATDTRAVGELAGLAVGSAVCITSIFAGAVSGGSMNPARTLGPALASNLYTGLWIYFLGPVLGTLSGAWTYTYIRFEEAPSHKDMSQKLSSFKLRRLQSQSVAVDDDELDHIQV