wanglab/gogpt-training-data huggingface dataset:
Protein: Tissue factor pathway inhibitor (TFPI) (Extrinsic pathway inhibitor) (EPI) (Lipoprotein-associated coagulation inhibitor) (LACI) (P10646)
Organism: Homo sapiens (Human)
Function: Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma.
Subcellular location: [Isoform Alpha]: Secreted.; SUBCELLULAR LOCATION: [Isoform Beta]: Microsome membrane {ECO:0000269|PubMed:22144186}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22144186}.
Interaction partners:
- Coagulation factor X
- Tissue factor
- Coagulation factor VII
- Thrombomodulin
- Prothrombin
- Antithrombin-III
- Heparin cofactor 2
- Endothelial protein C receptor
- Plasminogen
- Thrombospondin-1
Sequence:
MIYTMKKVHALWASVCLLLNLAPAPLNADSEEDEEHTIITDTELPPLKLMHSFCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNQNRFESLEECKKMCTRDNANRIIKTTLQQEKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQSTKVPSLFEFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGCGGNENNFTSKQECLRACKKGFIQRISKGGLIKTKRKRKKQRVKIAYEEIFVKNM
Protein: Growth/differentiation factor 10 (GDF-10) (Bone morphogenetic protein 3B) (BMP-3B) (Bone-inducing protein) (BIP) (P55107)
Organism: Homo sapiens (Human)
Function: Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P97737}.
Interaction partners:
- Activin receptor type-2A
Sequence:
MAHVPARTSPGPGPQLLLLLLPLFLLLLRDVAGSHRAPAWSALPAAADGLQGDRDLQRHPGDAAATLGPSAQDMVAVHMHRLYEKYSRQGARPGGGNTVRSFRARLEVVDQKAVYFFNLTSMQDSEMILTATFHFYSEPPRWPRALEVLCKPRAKNASGRPLPLGPPTRQHLLFRSLSQNTATQGLLRGAMALAPPPRGLWQAKDISPIVKAARRDGELLLSAQLDSEERDPGVPRPSPYAPYILVYANDLAISEPNSVAVTLQRYDPFPAGDPEPRAAPNNSADPRVRRAAQATGPLQDNELPGLDERPPRAHAQHFHKHQLWPSPFRALKPRPGRKDRRKKGQEVFMAASQVLDFDEKTMQKARRKQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCAGACEFPMPKIVRPSNHATIQSIVRAVGIIPGIPEPCCVPDKMNSLGVLFLDENRNVVLKVYPNMSVDTCACR
Protein: Murein DD-endopeptidase MepM (EC 3.4.24.-) (Murein hydrolase MepM) (ORFU) (P0AFS9)
Organism: Escherichia coli (strain K12)
Function: A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Uniform peripheral location, with partial enrichment at cell poles.
Interaction partners:
- High-affinity zinc uptake system protein ZnuA
- Murein DD-endopeptidase MepH
- Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase
- N-acetylmuramoyl-L-alanine amidase AmiB
- D-alanyl-D-alanine endopeptidase
- Signal peptidase I
- Lipoprotein NlpI
- Soluble lytic murein transglycosylase
- Lipid A biosynthesis myristoyltransferase
- Zinc import ATP-binding protein ZnuC
Sequence:
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD
Protein: Cationic amino acid transporter 3, mitochondrial (Q8GYB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Permease involved in the transport of the cationic neutral or acidic amino acids.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protease Do-like 10, mitochondrial
- Catalase-3
Sequence:
MGCLRSLVRRKQFDSSNGKAETHHHHQQLAKALTFPHLIAIGVGSTIGAGVYILVGTVAREHSGPALALSFLIAGISAALSAFCYAELSSRFPSAGSAYHYSYICIGEGVAWLIGWALILEYTIGGSTVARGISPNLAMIFGGEDCLPTILARHQIPGLDIVVDPCAAVLVFIVTGLCCLGVKESTFAQGIVTTANVFVMIFVIVAGSYLCFKTGWVGYELPTGYFPYGVDGMLTGSATVFFAYIGFDTVASMAEEVKNPRRDLPLGIGISLLLCCLLYMMVSVVIVGLVPYYAMDPDTPISSAFSSHGIQWAAYLINLGAVMALCSALMGSILPQPRILMAMARDGLLPSYFSYVNQRTQVPINGTITTGVCAAILAFFMDVSQLAGMVSVGTLVAFTMVAISLLIVRYVVPPDEVPLPSSLQENSSSHVGTSIRSKQPLLGKVDDSVVDKENAPGSWVLNKKNRRKFAGWSIMFTCIGNFLLSYAASSFLLPGLLRYSLCGVGGLFLLVGLIVLICIDQDDARHSFGHSGGFICPFVPLLPIVCILINMYLLVNLGAATWVRVSVWLFLGVVVYIFYGRRNSSLVNAVYVSTAHLQEIRRTSGHSLA
Protein: Cytosolic coat protein, putative (Q381R2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037847}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037847}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
Interaction partners:
- Cytosolic coat protein, putative
- GOLD domain-containing protein
- COP-coated vesicle membrane protein erv25, putative
Sequence:
MTMRAMPLRVSGTIARLSLPLGLLLVTLSTFITTVRADDDAISVQVPPKKELCFFEDINKAGVKVFLHYLVTSGGSQDIEATIKNPDNSMIWSSGRDTEGRVLFKSRGSGRHRFCFSNKMSTISAKVVAFSITVGDEGLEGEDGKKDKKSDLGMDPIELAVRNIQHGLREVLEVQQYIRGREHKHRAVTEVANTRVFVWAMAEILIIIAMSLGNVWYLRRIFNKRRVV
Protein: Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin) (Q9UMZ2)
Organism: Homo sapiens (Human)
Function: Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles. Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9JKC9}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9JKC9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JKC9}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Localization at clathrin-coated vesicles depends on AFTPH/aftiphilin (PubMed:15758025). Associates with membranes via the adapter protein complex AP-1 (By similarity). Colocalizes with AP1G1 (By similarity). {ECO:0000250|UniProtKB:Q9JKC9, ECO:0000269|PubMed:15758025}.
Interaction partners:
- Aftiphilin
- AP-1 complex subunit gamma-like 2
- AP-1 complex subunit gamma-1
- AP-1 complex subunit sigma-2
- AP-1 complex subunit mu-2
- ADP-ribosylation factor-binding protein GGA1
- Secretory carrier-associated membrane protein 1
- AP-1 complex subunit sigma-3
- AP-1 complex subunit sigma-1A
- Clathrin heavy chain 1
Sequence:
MALRPGAGSGGGGAAGAGAGSAGGGGFMFPVAGGIRPPQAGLMPMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAMQAGIPMGPMPAAGMPYLGQAPFLGMRPPGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSRDAKMHPTPASHPKKPGPSLEEKFLVSCDISTSGQEQIKLNTSEVGHKALGPGSSKKYPSLMASNGVAVDGCVSGTTTAEAENTSDQNLSIEESGVGVFPSQDPAQPRMPPWIYNESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRGVPAMSPDALNQFPAAPIPTLSGFSMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGPVGGAAAQASSGFIPTYPANQVVKPEEDDFQDFQDASKSGSLDDSFSDFQELPASSKTSNSQHGNSAPSLLMPLPGTKALPSMDKYAVFKGIAADKSSENTVPPGDPGDKYSAFRELEQTAENKPLGESFAEFRSAGTDDGFTDFKTADSVSPLEPPTKDKTFPPSFPSGTIQQKQQTQVKNPLNLADLDMFSSVNCSSEKPLSFSAVFSTSKSVSTPQSTGSAATMTALAATKTSSLADDFGEFSLFGEYSGLAPVGEQDDFADFMAFSNSSISSEQKPDDKYDALKEEASPVPLTSNVGSTVKGGQNSTAASTKYDVFRQLSLEGSGLGVEDLKDNTPSGKSDDDFADFHSSKFSSINSDKSLGEKAVAFRHTKEDSASVKSLDLPSIGGSSVGKEDSEDALSVQFDMKLADVGGDLKHVMSDSSLDLPTVSGQHPPAADIEDLKYAAFGSYSSNFAVSTLTSYDWSDRDDATQGRKLSPFVLSAGSGSPSATSILQKKETSFGSSENITMTSLSKVTTFVSEDALPETTFPALASFKDTIPQTSEQKEYENRDYKDFTKQDLPTAERSQEATCPSPASSGASQETPNECSDDFGEFQSEKPKISKFDFLVATSQSKMKSSEEMIKSELATFDLSVQGSHKRSLSLGDKEISRSSPSPALEQPFRDRSNTLNEKPALPVIRDKYKDLTGEVEENERYAYEWQRCLGSALNVIKKANDTLNGISSSSVCTEVIQSAQGMEYLLGVVEVYRVTKRVELGIKATAVCSEKLQQLLKDIDKVWNNLIGFMSLATLTPDENSLDFSSCMLRPGIKNAQELACGVCLLNVDSRSRKEEKPAEEHPKKAFNSETDSFKLAYGGHQYHASCANFWINCVEPKPPGLVLPDLL
Protein: Protein-serine O-palmitoleoyltransferase porcupine (mPORC) (EC 2.3.1.250) (Q9JJJ7)
Organism: Mus musculus (Mouse)
Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:24798332}; Multi-pass membrane protein {ECO:0000269|PubMed:10866835}.
Interaction partners:
- Proto-oncogene Wnt-3
- Proto-oncogene Wnt-1
- Protein Wnt-3a
- Protein Wnt-5a
- Protein Wnt-7a
- Protein Wnt-5b
- Protein Wnt-7b
- Protein Wnt-4
- Protein Wnt-2
- Protein Wnt-6
Sequence:
MATFSRQEFFQQLLQGCLLPTVQQGLDQIWLLLTICFACRLLWRLGLPSYLKHASTVAGGFFSLYHFFQLHMVWVVLLSLLCYLVLFLCRHSSHRGVFLSVTILIYLLMGEMHMVDTVTWHKMRGAQMIVAMKAVSLGFDLDRGEVGAVPSPVEFMGYLYFVGTIVFGPWISFHSYLQAVQGRPLSRRWLKKVARSLALALLCLVLSTCVGPYLFPYFIPLDGDRLLRNKKRKARGTMVRWLRAYESAVSFHFSNYFVGFLSEATATLAGAGFTEEKDHLEWDLTVSRPLNVELPRSMVEVVTSWNLPMSYWLNNYVFKNALRLGTFSAVLVTYAASALLHGFSFHLAAVLLSLAFITYVEHVLRKRLAQILSACILSKRCLPDCSHRHRLGLGVRALNLLFGALAIFHLSYLGSLFDVDVDDTTEEQGYGMAYTVHKWSELSWASHWVTFGCWIFYRLIG
Protein: Mitochondrial GTPase 1 (O74776)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial GTPase involved in assembly of the large ribosomal subunit (By similarity). Plays a role in expression of the mitochondrial translational machinery (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q03151}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03151}.
Interaction partners:
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL43
- Putative acyl carrier protein, mitochondrial
- Large ribosomal subunit protein uL15m
- tRNA modification GTPase mss1
- Pseudouridylate synthase C18B11.02c
Sequence:
MAFVARQTFEYQMPSTWYPGHMNKTLKRLKNLTSSNDIFVEVRDARIPLTSRNYVMEDFLNKKNRIIVYNKCDLADTFHTKAKVSKHRIQNLAQQFQNVECWFKETSTPEKSAFITPYVSKAPYFAKELLRLIRTLVDQASANGRVYVYFVGMPNTGKSSILNSLRNVALRKSKSAIVGNYPGVTKRISEIVRLFNDMDVYMLDTPGIMTPSITKPEDMLKLSLVGCVKEGIVHPVTVVDYLLFHLNRIDPSLYSKWSLPTNDVDEFLQNTAYKARKLTKGGFDENFVSNYVIQQYRIGRLGRFQLDTIDKNELLIRLHNEQNKKNAK
Protein: Seminal metalloprotease 1 (EC 3.4.24.-) (Q9VJN9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Seminal fluid metalloprotease which is transferred to females during mating and is required for processing of two other seminal fluid proteins Acp26Aa and Acp36DE in mated females.
Subcellular location: Secreted {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868}. Note=Secreted into seminal fluid. {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868}.
Interaction partners:
- Uncharacterized protein, isoform A
- Accessory gland protein Acp36DE
- Seminase
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp62F
- AT03573p
- Lectin-46Ca
- Uncharacterized protein, isoform B
- AT20289p
- glutaminyl-peptide cyclotransferase
Sequence:
MFPQIWGVIFLFTPTVFSELFKDPELLAGFYQGDIKAHPIRTRNGIVNQIYHWPNRTVPYMIEDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMALVITSKGLGCNTVHLGYRNKTQVVNLEIYPLGEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAWHDFDEGYDYESVMHYVPRAFSRNGQPTIVPLREGAENMGQRFYMSEKDIRKLNKMYRCPDHV
Protein: Membrane spanning 4-domains A1 (E9PKH8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP
Protein: HCG2044837 (Sorting nexin-15) (E5KQS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRQAKDDFLRHYTVSDPRTHPKGYTEYKVTAQFISKKDPEDVKEVVVWKRYSDFRKLHGDLAYTHRNLFRRLEEFPAFPRAQVFGRFEASVIEERRKGAEDLLRFTVHIPALNNSPQLKEFFRGGEVTRPLEVSRDLHILPPPLIPTPPPDDPRLSQLLPAERRGLEELEVPVDPPPSSPAQEALDLLFNCESTEEASGSPARGPLTEAELALFDPFSKEEGAAPSPTHVAELATMEVESARLDQEPWEPGGQEEEEDGEGGPTPAYLSQATELITQALRDEKAGAYAAALQGYRDGVHVLLQGVPSDPLPARQEGVKKKAAEYLKRAEEILRLHLSQLPP
Protein: Trehalose 6-phosphate phosphatase (EC 3.1.3.12) (Q9VM18)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trehalase
- Trehalase
- BcDNA.GH08860
- Trehalose 6-phosphate phosphatase
- Paramyosin, long form
- Tropomyosin-2
- Myosin light chain alkali
- Troponin T, skeletal muscle
- Troponin I
- Muscle-specific protein 20
Sequence:
MAEQKKAPLLKKEEDYVKALEGFINPETDQVALLLDYDGTLAPLTEELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKFKIEMPEELLEKHNKLVSELKEKVVCSGAWVEDKKISVTYHYKGVTDKLKAKLIAEAKGLIQAHGFQLIETPYALEGKPRVNWDKGEGAKMILEKQFDADWAKNLKIVYVGDDTTDEDAIKVLHGIGKTFRVSELPTLKTYANYQIKTVEEVGYLLKAVQAYYEKKKKA
Protein: DNaJ domain (Prokaryotic heat shock protein) (O16303)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein 110
- DUF148 domain-containing protein
- Heat shock protein hsp-1
- DnaJ homolog subfamily B member 13
- Heat shock 70 kDa protein 13
- Heat shock protein 70
- Heat shock protein 70
- Endoplasmic reticulum chaperone BiP homolog
- Heat shock protein hsp-6
- Heat shock 70 kDa protein C
Sequence:
MFGGGSSGPVDTTLYTTLNVRPDASQADIKKSYFKLAKEYHPDKNPDHGDKFKEISFAYEVLSSPEKRRLYDARGLEGVQGGGAGGGGGGFPGGLFSHFFGGAGGDDDDDDDDMGGHPFGGLFGGMGGMGRGGPRRRKFQDTVHPLNVTLEELYVGKTSKLKLSKKALCKTCEGSGGKKGEKYKCDACRGRGVKTIVQQIGPGMLQQMQVHCDACKGSGGKVPAGDKCKGCHGEKYENVSKILEVHVLPGMKHNDKITFKGDGDQSDPDGEPGDVVIVIQQKDHDIFKRDGDDLHMTKKLSLNEALCGYNFLIKHLDGHPLVLSSKQGDVIKPGVIRGVLGKGMPNKKYPELKGNLFVEFEVEFPKEHFLDDEKAYAVLKSCFPTSKVVNVTPAAAEVSLMEYDEKKYSRGRGGDAYNEDSDEEQHGGHHGQGVRCQHQ
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (Q9XWS4)
Organism: Caenorhabditis elegans
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS27
- Ribosomal Protein, Small subunit
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL14
Sequence:
MAPAAKPQVKKNAENINSRLSMVMKTGQYVLGYKQTLKSLLNGKAKLVIIANNTPPLRKSEIEYYAMLAKTGVHHYNGNNIELGTACGRLFRVCTLAVTDAGDSDIILSVPSESA
Protein: Molybdenum-pterin-binding protein MopA (Q08385)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Interaction partners:
Sequence:
MNEQPLIAALSLQRAGAPRVGGDRIRLLEAIARHGTIAGAAREVGLSYKTAWDAVGTLNNLFEQPLVEAAPGGRTGGNARVTEAGQALIAGFGLLEGALTKALGVLEGGVSAPEKALNTLWSLTMRTSNRNTLRCTVTRVTLGAVNAEVELALTDGHSLTAVITERSATEMGLAPGVEVFALIKASFVMLAAGGDPGRISACNRLTGIVAARTDGPVNTEIILDLGNCKSITAVITHTSADALGLAPGVPATALFKASHVILAMP
Protein: Dihydroneopterin triphosphate 2'-epimerase (EC 5.1.99.7) (D-erythro-7,8-dihydroneopterin triphosphate epimerase) (P0AC19)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli.
Interaction partners:
- GTP cyclohydrolase 1
- Alkaline phosphatase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- Epimerase family protein YfcH
- Dihydroneopterin triphosphate diphosphatase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Dihydropteroate synthase
- Disulfide-bond oxidoreductase YfcG
- Dihydromonapterin reductase
- NAD
Sequence:
MAQPAAIIRIKNLRLRTFIGIKEEEINNRQDIVINVTIHYPADKARTSEDINDALNYRTVTKNIIQHVENNRFSLLEKLTQDVLDIAREHHWVTYAEVEIDKLHALRYADSVSMTLSWQR
Protein: Phosphotransferase (EC 2.7.1.-) (Q6FUU4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- phosphoglucomutase
- phosphoglucomutase
- phosphopentomutase
- Phosphomannomutase
- 6-phosphofructokinase
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
Sequence:
MSFENFHKATSEQLTKAVDELCKEFEVTPKMLDELTAYFIESMEKGLAAEADSENKGLPMIPSFVTGMPNGTENGVLLAADLGGTNFRVCSVTLNGDNTFKMEQMKSKIPDELLDDEGVTSEQLFGYLGRRTVAFVKKYHPEFLNKGDDIPPIRLGFTFSYPVDQTSLNSGTLIRWTKGFKIEDTVGKDVVQLYQQQLDAQGLGMIKIVAMTNDTVGTFLSHCYASGSHSSSGGEISEPVIGCIFGTGTNGCYMEEIENIKKLPEDMRHQLANEGKTHMCVNTEWGSFDNECRYLPTTKYDVDIDQKYSANPGFHLFEKRVSGMYLGEVLRNVLVDLHSRGLMLTQYRDYDQLPHRLKTPFELSSEVLSRIEIDDSTGLRETELSFLQSLRLPTTPSEREAIQKLVRAISRRSAYLASVPIAAILIKTNALNKRYHGEVEVGCDGSVIEYYPGFRSMLRHALSLSPIGADGERKIHIRIAKDGSGVGAALCALVA
Protein: cAMP-dependent protein kinase catalytic subunit (PKA C) (EC 2.7.11.11) (P21137)
Organism: Caenorhabditis elegans
Function: Essential for larval development. Controls the rhythmic contraction of enteric muscles probably by regulating G-protein coupled receptor aex-2-mediated calcium influx in GABAergic DVB neurons. Plays a role in the control of oocyte meiotic maturation by gonadal sheath cells.
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- adenylate cyclase
- Glycogen synthase kinase-3
- Probable 3',5'-cyclic-AMP phosphodiesterase pde-4
- Forkhead box protein O
- Presenilin sel-12
- Presenilin hop-1
- Presenilin spe-4
- Protein lgg-1
- Protein kinase domain-containing protein
Sequence:
MPTRLDIVGNLQFSSSTDNGDEDQEADVTACFVLPSPSSFSKLSILDDPVEDFKEFLDKAREDFKQRWENPAQNTACLDDFDRIKTLGTGSFGRVMLVKHKQSGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAIDFPFLVNMTFSFKDNSNLYMVLEFISGGEMFSHLRRIGRFSEPHSRFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDSTGYLKITDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVKFPSHFSNELKDLLKNLLQVDLTKRYGNLKNGVADIKNHKWFGSTDWIAIYQKKITPPSFSKGESNGRLFEALYPRVDGPADTRHFVEEVQEPTEFVIAATPQLEELFVEF
Protein: Eukaryotic translation initiation factor 4E (Q32Q75)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATVEPEATPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Protein: Putative aryl-alcohol dehydrogenase C977.14c (EC 1.1.1.-) (Q9P7U2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Carbohydrate-binding domain-containing protein C2E1P3.05c
Sequence:
MSSLSPELYGCLGNSGLKVSKLILGCMSYGKKEYWEDWVLEDEEEVFKIMKAAYDAGIRTFDTANCYSAGVSEELVGKFIRKYEIPRSSIVILSKCFFPVRKDLIKIFGDLSSRGVHFLDSPELANQCGLSRKHIFDAVEDSVKRLGTYIDVLQIHRYDPHVSAEEVMRALNDVVESGKVRYIGASTMRCYQFIELQNTAEKHGWHKFISMQNYHNLLYREEEREMIPYCQKTGVGLIPWSPLARGLLTRSIDANEETIRSKTDLYTRALEFGAGYKAILSRVEELAKKYNVSMATLATAWSLHKGDYPIVGISKVERLKDALAAVELKLSEEDIKYLEEPYCPVPIQGEI
Protein: MKIAA1222 protein (Q80TH3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KLQAAENEKVRWELEKNQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEVERKKREEVEKAHLLEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHTQSQNRAVHEWSVQQVSHWLMSLSLDQYVPEFSAQSISGEQLLQLDGNKLKALGMTSSQDRALVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKSEKMTSTADQP
Protein: Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (E1BYE9)
Organism: Gallus gallus (Chicken)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03202}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cytochrome b5 heme-binding domain-containing protein.
- Very-long-chain
- Hydroxysteroid 17-beta dehydrogenase 12
- Cytochrome b5 heme-binding domain-containing protein.
- FA_desaturase domain-containing protein.
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Elongation of very long chain fatty acids protein 5
- Delta-6 fatty acid desaturase
Sequence:
MEHLKAFDQEVNAFVDYMFGPRDARVRGWLLLDSYLPTFFLTVAYLLCIWLGNKFMKNRQPFSLKAHLIVYNLGITLLSLYMLIELILATWEGGYNLQCQNLHSAGEADIRVAKVLWWYYFSKVIEFADTIFFVLRKKSSQITFLHVYHHATMFNIWWCVLNWIPCGQSFFGPTLNSFIHVLMYSYYGLSVIPSMRKYLWWKKYLTQAQLIQFLLTIVHTLSAAVKPCGFPFGCLMFQSSYMATLVILFVNFYIKTYQKAPSRTAAKETPVTTEVKNGYHKNYFAASNGFLSNKKAQ
Protein: Cysteine-rich venom protein 25-A (CRVP-25h-A) (P84807)
Organism: Naja haje haje (Egyptian cobra)
Subcellular location: Secreted {ECO:0000269|PubMed:15670767}.
Interaction partners:
Sequence:
DVDFNSESTRRKNKQKEIVDLHNSLKKTV
Protein: RutC family protein YjgH (P39332)
Organism: Escherichia coli (strain K12)
Interaction partners:
- HTH-type transcriptional repressor BdcR
- Cyclic-di-GMP-binding biofilm dispersal mediator protein
- 2-iminobutanoate/2-iminopropanoate deaminase
Sequence:
MVERTAVFPAGRHSLYAEHRYSAAIRSGDLLFVSGQVGSREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPENQFEDIMTVKNEIFSAPPYPNWTAVGVTWLAGFDFEIKVIARIPEQ
Protein: COMM domain-containing protein 10 (Q9Y6G5)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 2
- COMM domain-containing protein 1
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 5
- COMM domain-containing protein 6
- COMM domain-containing protein 9
- COMM domain-containing protein 7
- COMM domain-containing protein 3
- Coiled-coil domain-containing protein 93
- COMM domain-containing protein 8
Sequence:
MAVPAALILRESPSMKKAVSLINAIDTGRFPRLLTRILQKLHLKAESSFSEEEEEKLQAAFSLEKQDLHLVLETISFILEQAVYHNVKPAALQQQLENIHLRQDKAEAFVNTWSSMGQETVEKFRQRILAPCKLETVGWQLNLQMAHSAQAKLKSPQAVLQLGVNNEDSKSLEKVLVEFSHKELFDFYNKLETIQAQLDSLT
Protein: Ethanolamine kinase (EK) (EC 2.7.1.82) (Q03764)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the committed step of phosphatidylethanolamine synthesis via the CDP-ethanolamine branch of the Kennedy pathway. Also exhibits choline kinase activity, thus contributing to phosphatidylcholine synthesis via the CDP-choline pathway, but its preferred substrate is ethanolamine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline kinase
- Choline/ethanolaminephosphotransferase 1
- Choline-phosphate cytidylyltransferase
- Target of rapamycin complex 1 subunit KOG1
- Glycerophosphocholine phosphodiesterase GDE1
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Cholinephosphotransferase 1
- Phosphatidylserine decarboxylase proenzyme 2
- Phosphatidyl-N-methylethanolamine N-methyltransferase
Sequence:
MYTNYSLTSSDAMPRTYLVGTASPEMSKKKRQSANCDKPTRRVIHIIDTNEHSEVDLKNELPITCTNEDGEMTSSSWTSQTANDFLKLAYVNAKLDPSLPSQYFKQDIINVLQSLEIPGWSVPGSKESSLNKNLLTLTQIKGALTNVIYKIHYPNLPPLLMRIFGDSIDSVIDREYELKVIARLSFYDLGPKLEGFFENGRFEKYIEGSRTSTQADFIDRDTSIKIAKKLKELHCTVPLTHKEITDQPSCWTTFDQWIKLIDSHKEWVSNNVNISENLRCSSWNFFLKSFKNYKRWLYNDSAFTSKLLREDDKDSMINSGLKMVFCHNDLQHGNLLFKSKGKDDISVGDLTIIDFEYAGPNPVVFDLSNHLNEWMQDYNDVQSFKSHIDKYPKEEDILVFAQSYINHMNENHVKIASQEVRILYNLIIEWRPCTQLFWCLWALLQSGRLPQRPLIEGEKLMSEKAGLGDETHLMEHKNKENGKYDCSEDDSFNYLGFCKEKMSVFWGDLITLGVIDKDCPDIGKTDYLDTKLIF