wanglab/gogpt-training-data huggingface dataset:
Protein: Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2) (O97921)
Organism: Equus caballus (Horse)
Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity).
Subcellular location: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
Interaction partners:
- Hematopoietic prostaglandin D synthase
- Prostaglandin E synthase
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 1
- Thromboxane-A synthase
- Prostacyclin synthase
- Prostaglandin E synthase 3
- Prostaglandin G/H synthase 2
- Uncharacterized protein
- Aldo_ket_red domain-containing protein.
Sequence:
MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLTSTFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRPEVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN
Protein: Probable GABA permease (4-amino butyrate transport carrier) (Gamma-aminobutyrate permease) (Q9I703)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the degradation of beta-alanine.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Beta-alanine--pyruvate aminotransferase
- Beta-alanine degradation protein BauB
- Malonate-semialdehyde dehydrogenase
Sequence:
MSKVVLASQLPNKRNASLAPGLKQRHVTMLSIAGVIGAGLFVGSGHAIAAAGPAALLAYLIAGTLVVLVMRMLGEMAVASPDTGSFSTYADRSIGRWAGFTIGWLYWWFWVLVIPLEAIAAAAILNAWFPAIDTWIFALAVTFLLTVTNLFSVARYGEFEFWFALLKVIAIIAFIVLGAVAIVGGLPEREVSGLSSLMASHGGFVPNGYGAVLGALLTTMFSFMGTEIVTIAAAESKDPAKQITRATNSVIWRIGLFYLVSIFIVISIVPWNDPLLIQVGSYQRALELLDIPHAKLIVDLVVLVAVASCLNSAIYTSSRMVFSLAKRGDAPSVLKLTNTAHVPRPAVLASTAVGFLTTIVNYFAPEKVFTFLLASSGAVALLVYLVIAVAQLRMRKQLQASGQPIEFRMWLYPWLTWAVILFIVAALSIMLIMPEHRHEVFATALLTIFTVCLGLLNARRKPRLGEDYAGKTARV
Protein: Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.367) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Histone H3-K9 methyltransferase 5) (H3-K9-HMTase 5) (Lysine N-methyltransferase 1D) (Q9H9B1)
Organism: Homo sapiens (Human)
Function: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity).
Subcellular location: Nucleus. Chromosome. Note=Associates with euchromatic regions.
Interaction partners:
- Histone-lysine N-methyltransferase EHMT2
- Histone H3.3
- Histone H3.1
- Histone H3.2
- Histone H3.1t
- Histone H3.3C
- Histone H3-7
- Histone-lysine N-methyltransferase PRDM16
- Histone deacetylase 1
- Cellular tumor antigen p53
Sequence:
MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL
Protein: BREAST CANCER 2 like 2A (F4JGU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSTWQLFPDSSGDGFRWEVAGRILQSVSDSTPTKALESTAPLPSMADLLLQGCSKLIAREEAMPGEIPMFRTGLGKSVVLKESSIAKAKSILAEKVTYSDLRNTNCSIPQMRQVDTAETLPMFRTASGKSVPLKESSIAKAMSILGSDKIIDSDNVLPRESGFGVSNSLFQTASNKKVNVSSAGLARAKALLGLEEDDLNGFNHVNQSSSSSQQHGWSGLKTHEEFDATVVKHHSGTPGQYEDYVSGKRSEVLNPSLKVPPTKFQTAGGKSLSVSAEALKRARNLLGDPELGSFFDDVAGGDQFFTPEKDERLSDIAINNGSANRGYIAHEEKTSNKHTPNSFVSPLWSSSKQFSSVNLENLASGGNLIKKFDAAVDETDCALNATHGLSNNRSLASDMAVNNSKVNGFIPRGRQPGRPADQPLVDITNRRDTAYAYNKQDSTQKKRLGKTVSVSPFKRPRISSFKTPSKKHALQASSGLSVVSCDTLTSKKVLSTRYPEKSPRVYIKDFFGMHPTATTRMDYVPDHVRRIKSSNADKYVFCDESSSNKVGAETFLQMLAESEKVCDRSFEACMWIVWKLACYDIYYPAKCRGNFLTITNVLEELKYRYEREVNHGHCSAIKRILSGDAPASSMMVLCISAINPKTDNDSQEAHCSDSCSNVKVELTDGWYSMNAALDVVLTKQLNAGKLFVGQKLRILGAGLSGWATPTSPLEAVISSTICLLLNINGTYRAHWADRLGFCKEIGVPLALNCIKCNGGPVPKTLAGIKRIYPILYKERLGEKKSIVRSERIESRIIQLHNQRRSALVEGIMCEYQRGINGVHSQNDTDSEEGAKIFKLLETAAEPEFLMAEMSPEQLRSFTTYKAKFEAAQQMRKEKSVAETLEDAGLGERNVTPFMRIRLVGLTSLSYEGEHNPKEGIVTIWDPTERQRTELTEGKIYMMKGLVPINSDSEILYLHARGSSSRWQPLSPKDSENFQPFFNPRKPISLSNLGEIPLSSEFDIAAYVVYVGNAYTDVLQKKQWVFVTDGSAQHSGEISNSLLAISFSTSFMDDSSVSHISHNLVGSVVGFCNLIKRAKDVTNEIWVAEAAENSVYFINAEAAYSSHLKTSSAHIQTWAKLSSSKSVRSRRLPLSIIIRVLSIIGACPSGLNSPDKCRAFNFFWSHSTLKLPHTAFQNRAMRVADKPP
Protein: Serpin B10 (Bomapin) (Peptidase inhibitor 10) (PI-10) (P48595)
Organism: Homo sapiens (Human)
Function: Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus.
Subcellular location: Nucleus. Cytoplasm. Note=Mostly found in the nucleus.
Interaction partners:
- Cathepsin G
Sequence:
MDSLATSINQFALELSKKLAESAQGKNIFFSSWSISTSLTIVYLGAKGTTAAQMAQVLQFNRDQGVKCDPESEKKRKMEFNLSNSEEIHSDFQTLISEILKPNDDYLLKTANAIYGEKTYAFHNKYLEDMKTYFGAEPQPVNFVEASDQIRKDINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKKKLHIFHIEKPKAVGLQLYYKSRDLSLLILLPEDINGLEQLEKAITYEKLNEWTSADMMELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGSGSEIDIRIRVPSIEFNANHPFLFFIRHNKTNTILFYGRLCSP
Protein: Spindle and Kinetochore-Associated protein homolog (Q9BI86)
Organism: Caenorhabditis elegans
Interaction partners:
- SKA complex subunit 1
- Outer kinetochore KNL1 complex subunit knl-1
- Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1
- EB1 C-terminal domain-containing protein
- Kinetochore protein ndc-80
- CEntrosomal Protein
- TPX2 domain-containing protein
Sequence:
MANETLEHVLIYFLEKLKDVRCNQSPELLQKLTLSQYKTLAQLDVDMRMRLTQEMESYVADHVEIMKLELQLKNKKCALAGKLKQLGTTFDKAIVETKERNEHLRIGSIDFLNPVVEKVEKIVFAKPEMPQISVEQGSVLGESARRQPELVSVMASIMKPPTFSSLVMTGRTEKKENIPETKSYSLDDSLINGHDISMVNTSNERRKLAFDELDDEELQTPARKPQRTPSRAPERNPLDLFSLQAPPVFTSSVGRAFNQTRD
Protein: Chitinase 9 (EC 3.2.1.14) (Q9W2M5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- N-acetyl-D-glucosamine kinase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
Sequence:
MGKLLALLAVLCLSQVIGAERIVNCYWGTWANYRSGNGKFDVSNIDAGLCTHLSYSFFGINDNGEIQSLDTWLDYDLGFINQAISLKNQNSNLKVLAVVGGWNEGSTKYSSMSGDWYKRQNFINSALNLLRNHGFDGLDLDWEYPNQRGGNWNDRANFVTLLREIKEAFAPYGYELGIAVGAGESLASASYEIANIAQQVDFINVMTYDFAMASDGQTGFNAPQWAVENAINFWLSQGAPANKLVLGVGTYGRSFQLSDSSQNWPGAPCRGEGSAGSYTGSTGYLGYNEICQNNWHTVFDYDNAAPYAYSGDQWVSFDNVLSVQYKMDFALSKGLAGAMIWSLETDDYRGQCGETYPLLKTINRKLRW
Protein: Elongin-C (EloC) (Elongin 15 kDa subunit) (RNA polymerase II transcription factor SIII subunit C) (SIII p15) (Stromal membrane-associated protein SMAP1B homolog) (Transcription elongation factor B polypeptide 1) (P83940)
Organism: Mus musculus (Mouse)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells.
Subcellular location: Nucleus {ECO:0000305|PubMed:33590678}.
Interaction partners:
- Cullin-5
- von Hippel-Lindau disease tumor suppressor
- Elongin-B
- RING-box protein 2
- Cullin-2
- E3 ubiquitin-protein ligase RBX1
- Core-binding factor subunit beta
- Hypoxia-inducible factor 1-alpha
- Elongin-A
- Suppressor of cytokine signaling 2
Sequence:
MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Protein: Uncharacterized protein C4.02c (Q9USS8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSLNVDIGLGTYDFSKWGYIDVHKIKEVHIYDFDNTLFQTPLPNANIWSNQAIRILMAFNILANGGWFFDPHVLAATGDGVEVEEKRAWEGWWNEKIVSQARESIRRPDVLAVLLTGRNEGFRGIVEKIIASKGLDFQGVVFKLQAPDGFWPQTLNFKLWFFNEVYRHFLYINSTRIYEDRPSHIEAFSAWLTERKKKNKNADFEIIAVAEPPKYLKFKVEIALVRGMLTAHNLKAPSLKLPLYKFVKNVIATVVTVPVAELHHIRNAFFNIPIAEIMESVSANSSRRNSHDSNSTIICEPEYPPDTSFNSSPGRLWIVTAIGRYRDEYWTVRAEAAEGYDCEKIHEIDVADIPSLYGTILYVSMSTGIVKSEIGDIGAQQWKTLAPSERWILRTNIRKECTYDIRYKRPYVSSLKYSDDDLTAGRASPMTGPTKRK
Protein: Ganglioside-induced differentiation-associated protein 2 (Q9NXN4)
Organism: Homo sapiens (Human)
Interaction partners:
- Core histone macro-H2A.2
- Protein mono-ADP-ribosyltransferase PARP15
- Protein mono-ADP-ribosyltransferase PARP9
Sequence:
MDPLGAPSQFVDVDTLPSWGDSCQDELNSSDTTAEIFQEDTVRSPFLYNKDVNGKVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYKSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGETIEKVVFAVSDLEEGTYQKLLPLYFPRSLKEENRSLPYLPADIGNAEGEPVVPERQIRISEKPGAPEDNQEEEDEGLGVDLSFIGSHAFARMEGDIDKQRKLILQGQLSEAALQKQHQRNYNRWLCQARSEDLSDIASLKALYQTGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAVKEYVLVYFHTLTSEYNHLDSDFLKKLYDVVDVKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDSLHQLFSAISPEQIDFPPFVLEYDARENGPYYTSYPPSPDL
Protein: Probable NAD(P)H dehydrogenase subunit CRR3, chloroplastic (Probable NDH subunit CRR3) (Protein CHLORORESPIRATORY REDUCTION 3) (Q9ZVE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable subunit of the chloroplast NAD(P)H dehydrogenase (NDH) complex of the photosynthetic electron transport chain. Required for both formation and activity of NDH. May function in assembly or stabilization of the NDH complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:17041026}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- NAD
- NAD
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- NAD
- NAD
- At2g01870
- NAD
Sequence:
MAVLSTIYSITRASTPTMASLTNDSPSPLPSSSPSKLPSPTSPSKKPLKLRQVSKQMGSQNQQRRGNKPSIAQIERAFGSGSYRDSEGEMDMNTVFDELLLGHANKFESKIEKKLREIGEIFVARTEPKLRSSGKPVLMFTIQWILPIWIMSLLVACGVIKLPFSIPFLDDLIM
Protein: Molybdopterin biosynthesis protein CNX1 (Molybdenum cofactor biosynthesis enzyme CNX1) [Includes: Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E); Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G)] (Q39054)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Interaction partners:
- Molybdopterin synthase catalytic subunit
- GTP 3',8-cyclase, mitochondrial
- Cyclic pyranopterin monophosphate synthase, mitochondrial
- Molybdenum cofactor sulfurase
- Molybdopterin synthase sulfur carrier subunit
- Adenylyltransferase and sulfurtransferase MOCS3
- ABC transporter B family member 25, mitochondrial
- Molybdate transporter 1
- Vacuolar protein sorting-associated protein 54, chloroplastic
- Molybdate transporter 2
Sequence:
MEGQGCCGGGGGKTEMIPTEEALRIVFGVSKRLPPVIVSLYEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGVTVTPGTVAYVTTGGPIPDGADAVVQVEDTKVIGDVSTESKRVKILIQTKKGTDIRRVGCDIEKDATVLTTGERIGASEIGLLATAGVTMVKVYPMPIVAILSTGDELVEPTAGTLGRGQIRDSNRAMLVAAVMQQQCKVVDLGIVRDDRKELEKVLDEAVSSGVDIILTSGGVSMGDRDFVKPLLEEKGKVYFSKVLMKPGKPLTFAEIRAKPTESMLGKTVLAFGLPGNPVSCLVCFNIFVVPTIRQLAGWTSPHPLRVRLRLQEPIKSDPIRPEFHRAIIKWKDNDGSGTPGFVAESTGHQMSSRLLSMRSANALLELPATGNVLSAGSSVSAIIVSDISAFSIDKKASLSEPGSIRKEKKYDEVPGPEYKVAILTVSDTVSAGAGPDRSGPRAVSVVDSSSEKLGGAKVVATAVVPDEVERIKDILQKWSDVDEMDLILTLGGTGFTPRDVTPEATKKVIERETPGLLFVMMQESLKITPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKGDKREKHPKHIPHAEATLPTDTWDQSYKSAYETGEKKEEAGCSCTH
Protein: Stromal-processing peptidase, putative (EC 3.4.24.55, EC 3.4.24.56) (Q8IL67)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLKSDVVLLLYILIINLICCLNGNSKKRAYILNTPKSSNCKRSSFRRWNNPVNNNINELKEDEDLIKYELQNGLSNIIYKKRKSVNKKKYILNNENHVILPTYKISDEYKCYINPIDYNYEELHVYMEVNTGSVNEKKNQQGISHLCEHVSYMGSKNRKNIVDKNIRTNAYTDFHHIVFYISVSLNNEIYKENFYSDFKCDQFIKNIREEDIEDYDIYTVDEFNYKHAILSQCIDTMVEVLKGETQFNKERITKEKKAIFSEYSIINNIEYKMNSDIIKVLHKENRLSHRLPIGKLELLKRYGEKDVKEYFNLFFRPENVNFFVYGDVNVDIAQKLISSKLENIKGKDLKEQDKIYLNILNDRCTLRSRNKNLPAVFHMFGNNSDIKVKEEEEEEVKKNIQLEKNEKNIETKDEKFHINNNENITFKDTDENFQEDDYNNKKENDCNTYDDDNIIDLEKYKEFKRNENDIVCELKFRNYLKNKYGVNMEEEKLLNKNEMKNINTSFEIIKYSLNNVNINILLKEEIKSVRTLEDLKISVIKEVIFYCLSFRFNIHRNNLFNSIDINEYTNINEGATIRTIEIKTTIKAFEKTIECFYNFIKSLLKYGFSEDELLNYKMNEIDYEDDLKDVEEKKSGQIIDHQNISHDVSEAYTNSNKHSSKNMKLIHPHDDDYDDNHNDAEKDMNNKMNEQDEEYILDSTKINETYTDEIQKIIDYNTCQHIYLNEKREKKIKREIFEKLKLQEINNFAKQYFQYLFNIFNPYSNMKPHCVVIHVPSKNENLFHKNKIRKLFFNNIYSMNDVQNYSINIQNKLLSPHYVYENITKKLSQARYIIPQKRENKYSEDIFNFIVNKMEDHKNENIFDVNNMCLSLPFYGLSTNPDLNMFKKCYCIKENKDDHINNVNDHMNETKILPQITESSVQPSLPTSSKKSNNNLCVDMKEKPKTMEINNKYNNMHDDVVCDNRRNNLSEKGVTFLNLKNYVLSLKNQKEIENYELLNGIKVNLYKTKVDKKNIYMRLIIPHNDIIKKKKENVHLLLFSIICLFEGGEIENVTREHVEIHCSNKSINIYIDINDEYFFIDIYTHNKYENISSAFSILNNIILETKIENTALPRVVDKLKKDFFEYKNSLQSLLLGQTISYVTGGKIGYQNFEVSDTENITMDDVQRMLKHIFSDLSLFELTIVGDFSDFIHYYILHYLGTLQGKIIEQEGEKKRSDVCLKNNKDNIIIEKHRTNNLSNESYPINEKKKKNEDNGCKSNSEILLNDYYSMLCPFADFEEKSKNTTYVYIKEKEEHGIFLLVGKGANMYGFLSNGIHISFYLMEYLKRIINGEEKNKNCENIYKDEYICNELDKIKSQVLEDFHFEDKHNINEYLKKKKKLYTSPLFFNAVSYIIQYILNSKLFHYLREKKELTYDSSFEFISYEKYFAGFFTILVQTNPRDLELIKKEVLSCIELFTTNYNNFSDYLIENSKLSYLNKKNKDLKYFVDKISGMQLTHFPLKYKNKHILKDNILLNKIQKIDVLLVLFILFNQTKNYHISYGISAPHDIWKETYKNINKLY
Protein: Transcription factor Sox-21-A (SRY-box containing gene 21a) (Q7SZS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May function as a switch in neuronal development (By similarity). Acts as a negative regulator of transcription. Plays a role in dorsoventral patterning of the embryo.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- POU domain, class 5, transcription factor 1
Sequence:
MAKPMDHVKRPMNAFMVWSRAQRRKMALDNPKMHNSEISKRLGGEWKLLSDSEKRPFIDEAKRLRAVHMKEHPDYKYRPRRKPKNLIKKDRYHFNVTYNLGEGDPLKSARLSGDALSDSLSAEKTSVAAAATRMFFSHHLSANPYPFLDLNSKISELPPAPFPHYSVLGYPSGLPAFPGMGVLAGAPHAHPSAGSPGHMLPYNCLGWPGSGPAVPSSYVLLPGMTKAQHEPYLAYAATI
Protein: Penicillin-binding protein 4 (PBP 4) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P40750)
Organism: Bacillus subtilis (strain 168)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth.
Subcellular location: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Penicillin-binding protein 3
- Penicillin-binding protein 2B
- Peptidoglycan glycosyltransferase RodA
- Probable peptidoglycan glycosyltransferase FtsW
- D-alanyl-D-alanine carboxypeptidase DacA
- Penicillin-binding protein H
- Uncharacterized protein YuxK
- Sporulation-specific N-acetylmuramoyl-L-alanine amidase
- Probable undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase
- D-alanyl-D-alanine carboxypeptidase DacC
Sequence:
MTMLRKIIGWILLLCIIPLFAFTVIASGKEVKQMKSLDQVLDKNIDLKDISLVQNSYMYDRDGSLVSEIVSDHENRVLVPFNKIPEEVKQIFLTSEDRHFYEHKGFDFMGMVRATASNVKDKKIDQGASTITQQLSRNLYLSHERSFSRKLTELAYSYQLEKKYTKNEILEAYLNTIYFNNGVYGVGSAAQFYFSKPLKSLTVGEMAFICAIPNNPTLYDPLKHFDYTKSRQERLLKGLKDAGVITDKELKKAVKQKIKLDVEKREDKYPDYVSYVNDEFTQLVSESEGFDKRLQKASGKQKEKIENELSARVSTLMKDGVKIYTALDPYMQNQVVAQMNSKLPYADVQGGAAVINHQTHQIIALSGGKNYQKYDFNRAYQAYRQPGSSIKPLLDYGPYIEQTGATTSSTIDASKFCSKDYCPQNYNNRTYGTVTLDTAFKNSYNTPAIRMLDRVGIQKAFSYIEPYHFAKLVDSDYLLPAALGGFTNGMTPLEMTKAYTTFGNSGSYTPSHAITKVTDLKGKTLYKWNDKATQIFSVRTNMQLKKLMSSVVKSGTGKKAYFNAPYIGGKTGTSNDYHDMWFVGLTDTYTMGVWVGKDTPTSVEYLHSISPQLSIWKGTLQAAY
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (EC 2.4.99.-) (GalNAc alpha-2,6-sialyltransferase VI) (ST6GalNAc VI) (ST6GalNAcVI) (hST6GalNAc VI) (Sialyltransferase 7F) (SIAT7-F) (Q969X2)
Organism: Homo sapiens (Human)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen. Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
Sequence:
MACSRPPSQCEPTSLPPGPPAGRRHLPLSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRSRRPVNLKKWSITDGYVPILGNKTLPSRCHQCVIVSSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTYRVVAHSSVFRVLRRPQEFVNRTPETVFIFWGPPSKMQKPQGSLVRVIQRAGLVFPNMEAYAVSPGRMRQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPNYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT
Protein: NPR1-like3 protein (L7TUW7)
Organism: Theobroma cacao (Cacao) (Cocoa)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAYLSEPSSSLSFSSSSHLSNGSITHNIPSFTVPETGASLEVISLTKLSTSLEQLVNDNGPDFSDADIVVEDVPVGVHRCILAVRSKFFNELFKKGNGSCEKEGKPSYNMSELLPYGKIGLEAFRILLHYLYTGKLRPSPMEVSTCVDNVCAHDACRPAINFAVELMYASSIFQIPELVSLFQRRLLNFVEKALVEDIITILVVAFHCQCSQLVSQCVDRVARSDLDSISIEKELPYEVAESIRLLRRKSPPDGEDNEAVVDPLREKRIRRIHKALDSDDVELVKLLLTESDITLDDAAALHYAAAYCDPKVVSEVLGLRLADVNLRNSRGYTVLHIAAMRKEPSVIMSLLAKGASASELTVDGRSAVNICQRLTRPKDYHAKTEQGKETNKDRICIDVLEREMRRNPMAGDVSVTSHTLADDLHMRLLYLENRVAFARLLFPSEAKLAMDIAHAETTSEFAGLCASKGSNGNLRQVDLNETPIMQKKRLLARMEALMKTVEMGRRYFPHCSEVLDKFMEDDLPDLFYLEKGSSEEQKIKRSRFRELKDDVQKAFSKDKAEFNRTGLSSSSSSSSLKDGGPYKLRKL
Protein: Mitochondrial glycoprotein (Q386E5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Mitochondrial SSU ribosomal protein
- Uncharacterized protein
- Uncharacterized protein
- Mitochondrial glycoprotein-like protein
- Uncharacterized protein
- Kinteoplast poly
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MLVCCRSSLSLLARATMPLCCSRRFLTHQNNIDDISGLVDTNSNSVSDGRLHCSTGEGGKASTCERVSLRTIAESLGAAAAAELRAEVERDTRDGVAAIPPLPPLGWRVRHPSGSNYFVMTRTLKNGVQSAELNNRRYRSVHDIFLQSLQKGGHKYAQKGKGSEGRQKHAKEEEEPPSQEDGKSSPKVTVGYDREGRGHRATLQRMDELHDSPKLSRADVHLTVFAPFRVYDPSLHDPTVDICEWSSFDLVVQKTVPDNRVANKLLQPLSCTPQDGALSMYVCLASVNSEMRIRSIQLLSMKEAQALVEHACFGNGEPLFLELLRRRGRRRPLVERRFDDPRLRYEEVAQPQQVADEAAVACSSSCYGPYYPAFEMLMDSCGSAGEYSRALCYGGPYVSELSRELCDALLDYIKGDLGVSDQLCEYVCQMQFFLEQEEYMTWLGQVQHVANAVSRTA
Protein: 6-pyruvoyl tetrahydrobiopterin synthase (PTP synthase) (PTPS) (EC 4.2.3.12) (P27213)
Organism: Rattus norvegicus (Rat)
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Interaction partners:
- GTP cyclohydrolase 1
- Sepiapterin reductase
- Carbonyl reductase
- Carbonyl reductase 1])
- Aldo-keto reductase family 1 member B1
- aldose reductase
- Aldo-keto reductase family 1 member B7
- Alkaline phosphatase
- Intestinal-type alkaline phosphatase 2
- Intestinal-type alkaline phosphatase 1
Sequence:
MNAAVGLRRRARLSRLVSFSASHRLHSPSLSAEENLKVFGKCNNPNGHGHNYKVVVTIHGEIDPVTGMVMNLTDLKEYMEEAIMKPLDHKNLDLDVPYFADVVSTTENVAVYIWENLQRLLPVGALYKVKVYETDNNIVVYKGE