wanglab/gogpt-training-data huggingface dataset:
Protein: Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain] (P9WIL3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446, ECO:0000305|PubMed:12182836}.
Interaction partners:
- Pantothenate synthetase
- Type III pantothenate kinase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Conserved hypothetical alanine and leucine rich protein
- Small ribosomal subunit protein bS1
- Nicotinamidase/pyrazinamidase
- Probable aldehyde dehydrogenase NAD dependent AldA
- Probable aldehyde dehydrogenase
- ATP-dependent Clp protease ATP-binding subunit ClpC1
- aldehyde dehydrogenase
Sequence:
MLRTMLKSKIHRATVTCADLHYVGSVTIDADLMDAADLLEGEQVTIVDIDNGARLVTYAITGERGSGVIGINGAAAHLVHPGDLVILIAYATMDDARARTYQPRIVFVDAYNKPIDMGHDPAFVPENAGELLDPRLGVG
Protein: Growth arrest and DNA damage-inducible protein GADD45 alpha (F1R8Z0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cellular tumor antigen p53
- Mitogen-activated protein kinase kinase kinase 4
- Proliferating cell nuclear antigen
- Cyclin B2
- Cyclin-dependent kinase 1
- Cyclin B1
- Cyclin B3
- Aurora kinase A
- Phosphoinositide-3-kinase, regulatory subunit 3A
- Pleckstrin homology-like domain family A member 3
Sequence:
MTFEELNGDYSIERMNSVIKALEEVLRSALPQGCITVGVYEAAKSLNVDPDNVVLCILATDDDDVKDVALQIHFTLIQAFCCENDINILRVNNTRRLANILGGAGMHGSEQMDLHCILVTVPHASTWKNPALGKVNRFCRESRCMDQWVPIINLPER
Protein: Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (Retinoic acid-induced protein 70) (SKAP55 homolog) (SKAP-55HOM) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) (O75563)
Organism: Homo sapiens (Human)
Function: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12893833}.
Interaction partners:
- FYN-binding protein 1
- Integrin beta-1
- Integrin alpha-4
- Integrin alpha-5
- Tyrosine-protein kinase Fyn
- Lymphocyte cytosolic protein 2
- PML-RARA-regulated adapter molecule 1
- Tyrosine-protein kinase Lyn
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Tyrosine-protein kinase Lck
Sequence:
MPNPSSTSSPYPLPEEIRNLLADVETFVADILKGENLSKKAKEKRESLIKKIKDVKSIYLQEFQDKGDAEDGEEYDDPFAGPPDTISLASERYDKDDEAPSDGAQFPPIAAQDLPFVLKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYSVRMNNTLRKDGKKDCCFEISAPDKRIYQFTAASPKDAEEWVQQLKFVLQDMESDIIPEDYDERGELYDDVDHPLPISNPLTSSQPIDDEIYEELPEEEEDSAPVKVEEQRKMSQDSVHHTSGDKSTDYANFYQGLWDCTGAFSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYIMEMYDI
Protein: Argonaute-binding protein 2 (Q10271)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: A member of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation, heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. Inhibits the release of the siRNA passenger strand from ago1 together with arb1.
Subcellular location: Nucleus. Cytoplasm. Note=Localizes to a large number of foci in both the nucleus and cytoplasm.
Interaction partners:
- Argonaute-binding protein 1
- Protein argonaute
- Chromo domain-containing protein 1
- RNA-induced transcriptional silencing complex protein tas3
- Protein Dicer
- Pre-mRNA-splicing factor cwf14
- Meiotic chromosome segregation protein P8B7.28c
- Helicase required for RNAi-mediated heterochromatin assembly 1
- Staphylococcal nuclease domain-containing protein 1
Sequence:
MFRKKKSRVLQRDVNFGNCLEDMNLQITNDFYLRKLNAPNELYEFQVTKDKEYNEKFYFAVLDHVYSWTLQNSLLTRISIPLESSPSEPHSWIYATRNWQTNENGIVIIIQSMSHPLIWSNRNLREGDVRRATVLDVIAKCTEKKLSVVIFSPSALLWDQSINFPRTTRYFTSQGLQITKKSIIKDVETPESYVSIGLNYVMSNSVSTKIHFVGSEYGSYLLNSYLDLNWKKFSGKAGAILLIMNMSINEELHDPDYVSYLIEHARNYLPSHEPCRHLMNSIMTESGIPNFSAGKYIDEFYDYIGDVLLEMIALDTNTSKS
Protein: EGF-like domain-containing protein (A4UVK0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNPHTRICEDLDECAFYQPCDFECINYDGGFQCNCPLGYELAEEGCRDVNECESVRCEDGKACFNQLGGYECIDDPCPANYSLVDDRYCEPECENCTSTPIQVHMLAIPSGLPISHIATLTAYDKSGRVLNDTTYAISDTGAPLARGRMTSGPFTIKAVKRGHAQVWTNRVLAAGDHHKVRVRAHSDHATNELHAPKETNFLVLINVGQYPF
Protein: Hpc2p (Q5AKU2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Protein HIR1
- Protein HIR2
- Histone chaperone ASF1
- Histone transcription regulator 3 homolog
Sequence:
MASGKNNISISSLLDSSSTPSSQPAGQAQKPTSSSSKSTVNNGRKPIAISEMVSKFQTSFNAGPVESEVIIIDDSQESTSSGEAESSSTQVPKPEPKPKLEPKSKPVSKRVSPPVAKSATSSKQYKTIKPNVQKGNTPPTRTAISTDQVKKFQTNFHLNPVTNQTSPSKTSITSIINIDDEPIPAPVSTPTSANNSPGNTNTNATKRKRANVKLFDPKKRQAVSSITTGETTATTKKKSPERQDRSASQVKLAQKSSSTTTGGLQKSPLLEKKADKTASGNSSSLKKQSSSLGAITDKNDSPVPVKLSAPSVIDLLNDDSEPETSQTDDKQSAQGNNNDKKIEGNKEPKQEETQISKKEEKPTPREKEKEKEKPEPPIIALNIPLLNPKDPQPGKAEVIVNVLKLAEEKYGWGIMHPKSKSAIDVMDDMIDDEDDDDNEDDDDIIEIVENQPPPSPLPSHQIQQSKSAQGANGNSGTSSNQQQKGKELTEEQLYRQHEVKMIRKVGKYDFEDPFIDDQELQMEEEISSTKEGFFVYWGPLVDDRNSNKKKKR
Protein: Uncharacterized protein YdjI (P77704)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized sugar kinase YdjH
- Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ
- Uncharacterized HTH-type transcriptional regulator YdjF
- Putative metabolite transport protein YdjK
- Inner membrane metabolite transport protein YdjE
- NADH-specific methylglyoxal reductase
- Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjL
- L-threonate dehydrogenase
Sequence:
MLADIRYWENDATNKHYAIAHFNVWNAEMLMGVIDAAEEAKSPVIISFGTGFVGNTSFEDFSHMMVSMAQKATVPVITHWDHGRSMEIIHNAWTHGMNSLMRDASAFDFEENIRLTKEAVDFFHPLGIPVEAELGHVGNETVYEEALAGYHYTDPDQAAEFVERTGCDSLAVAIGNQHGVYTSEPQLNFEVVKRVRDAVSVPLVLHGASGISDADIKTAISLGIAKINIHTELCQAAMVAVKENQDQPFLHLEREVRKAVKERALEKIKLFGSDGKAE
Protein: Vesicle transport protein GOT1A (Golgi transport 1 homolog A) (hGOT1b) (Q6ZVE7)
Organism: Homo sapiens (Human)
Function: May be involved in fusion of ER-derived transport vesicles with the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Uridine 5'-monophosphate synthase
- Dihydropyrimidine dehydrogenase [NADP
- Dihydroorotate dehydrogenase
- Pleckstrin homology domain-containing family A member 6
- Solute carrier family 23 member 1
- Solute carrier family 23 member 2
Sequence:
MISITEWQKIGVGITGFGIFFILFGTLLYFDSVLLAFGNLLFLTGLSLIIGLRKTFWFFFQRHKLKGTSFLLGGVVIVLLRWPLLGMFLETYGFFSLFKGFFPVAFGFLGNVCNIPFLGALFRRLQGTSSMV
Protein: Microfibrillar-associated protein 1A (Spliceosome B complex protein MFAP1A) (C0HKD8)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing as a component of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P55081}.
Interaction partners:
- U4/U6.U5 tri-snRNP-associated protein 1
- Pre-mRNA-splicing factor 38A
- Zinc finger matrin-type protein 2
- U4/U6 small nuclear ribonucleoprotein Prp31
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing-splicing factor 8
- WD40 repeat-containing protein SMU1
- Splicing factor 3A subunit 1
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 3
Sequence:
MSVPSALMKQPPIQSTAGAVPVRNEKGEISMEKVKVKRYVSGKRPDYAPMESSDEEDEEFQFIKKAKEQEAEPEEQEEDSSSDPRLRRLQNRISEDVEERLARHRKIVEPEVVGESDSEVEGDAWRLEREDSSEEEEEEIDDEEIERRRGMMRQRAQERKNEEMEVMEVEDEGRSGEESESESEYEEYTDSEDEMEPRLKPVFIRKKDRVTVQEREAEALKQKELEQEAKRMAEERRKYTLKIVEEETKKELEENKRSLAALDALNTDDENDEEEYEAWKVRELKRIKREREDREALEKEKAEIERMRNLTEEERRAELRANGKVITNKAVKGKYKFLQKYYHRGAFFMDEDEEVYKRDFSAPTLEDHFNKTILPKVMQVKNFGRSGRTKYTHLVDQDTTSFDSAWGQESAQNTKFFKQKAAGVRDVFERPSAKKRKTT
Protein: 1-hydroxycarotenoid 3,4-desaturase (EC 1.3.99.27) (1'-hydroxy-gamma-carotene 3,4-desaturase) (1-hydroxycarotenoid 3,4-dehydrogenase) (Q7WT72)
Organism: Flavobacterium sp. (strain P99-3)
Function: Catalyzes the introduction of a C-3,4 double bond into 1'-hydroxy-gamma-carotene and rhodopin (1-hydroxylycopene) to yield 1'-hydroxytorulene and (3E)-3,4-didehydrorhodopin, respectively. Can also 1-hydroxy-all-trans-1,2-dihydro-neurosporene, 1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene and 1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene. Probably involved in the synthesis of myxol, a gamma-carotene derivative (Probable). May use FAD as a proton acceptor (By similarity).
Interaction partners:
Sequence:
MKKAIIIGSGIAGLAAALRLKKKGYQVSVFEKNDYAGGKLHAIELGGYRFDLGPSLFTLPHLIDELHQLFPDVEIDFNYIKKKTACHYFWEDGTSFEAPADLENFAVKAAEIFDEKQNTLSKYLQNSKMKYESTKSLFLEKSLHKSNTYFSKQTLKAILKIPFLGINNTLDQENKKFSNPKLNQLFNRYATYNGSSPYLTPGIMSMIPYLELGLGTYYPQGGMHRISQSLFELAQKVGVEFRFRKNVKKINHSNNKVTGVTTEKGTHDADIVLCNMDVFPTYRQLLQDIKAPEKTLKQERSSSALIFYWGIKKSFPQLDLHNILFSENYKAEFEAIFNNKSLYEDPTVYINITSKQSPQDAPKGCENWFVMINTPGDYGQNWENLVIKAKKNILSKIKRCLNIDVEELIDVEYVLTPQGIEKNTSSYRGALYGAASNNKFAAFLRHPNFNKTIGNLYHVGGSVHPGGGIPLCLLSAKITADLIPNTNA
Protein: Uncharacterized protein ycf70 (P0C306)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MVYGYGKSNMPHPNRKRKGTDTQYDYWEELLVMVSGLYVLFCVFLVLFIFFDSFKQESNKLELSGKEEKKKLNGENRLSRDIQNLLYIK
Protein: Uncharacterized protein (H9C1B2)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MIRNFIDGDIVTHGEHFATGNEATRQGVIRRLRLFLGEYFLNAAEGTPWFQSILGKTQVDIAAASIKQRILTAPGVIGLTRFEFNIDQTTRKITIYASLVDINNKQFEMLFDEEII
Protein: Sterol regulatory element-binding protein 1 (SREBP-1) (Adipocyte determination- and differentiation-dependent factor 1) (ADD1) (Sterol regulatory element-binding transcription factor 1) [Cleaved into: Processed sterol regulatory element-binding protein 1 (Transcription factor SREBF1)] (P56720)
Organism: Rattus norvegicus (Rat)
Function: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane (By similarity). Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis and lipid homeostasis (By similarity).
Subcellular location: [Sterol regulatory element-binding protein 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36956}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum. Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed. {ECO:0000250|UniProtKB:Q9WTN3}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 1]: Nucleus {ECO:0000250|UniProtKB:P36956}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Fatty acid synthase
- Acyl-CoA desaturase 1
- Prelamin-A/C
- Sterol regulatory element-binding protein 2
- Peroxisome proliferator-activated receptor alpha
- Peroxisome proliferator-activated receptor gamma
- Acetyl-CoA carboxylase 1
- Insulin-1
Sequence:
MDELPFGEAALEQALAEVCEMDAALLTDIEDMLQLINNQDSDFPGLFDAPYAGGETGDTGPSSPGASSPESFSSPASLGSSLEAFLGGPKVTPAPLSPPPSAPTAVKMYPSVPPFSPGPGIKEEPVPLTILQPPAPQPSPGTLLPPSFPPPPVQLSPAPVLGYSSLPSGFSGTLPGNTQQTPSSLPLGSTPGISPTPLHTQVQSSAAQQPPPASAAPRMSTVASQIQQVPVVLQPHFIKADSLLLTAVKTDTGATMKTAGINTLAPGTAVQAGPLQTLVSGGTILATVPLVVDTDKLPIHRLAAGGKALGSAQSRGEKRTAHNAIEKRYRSSINDKIVELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLTLRSAHKSKSLKDLVSACGSGGGTDVSMEGMKPEVVETLTPPPSDAGSPSQSSPLSLGSRGSSSGGSDSEPDSPAFEDNQVKAQRLPSHSRGMLDRSRLALCVLVFLCLTCNPLASLFGWGILTPSDASGVHRSSGRSMLEAESRDGSNWTQWLLPPLVWLANGLLVLACLALLFVYGEPVTRPHSGPAVHFWRHRKQADLDLARGDFAQAAQQLWLALQALGRPLPTSNLDLACSLLWNLVRHLLQRLWVGRWLAGQAGGLQRDYRLRKDARASARDAAVVYHKLHQLHAMGKYTGGHLVASNLALSALNLAECAGDAISMATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGAVPLAMQWLCHPVGHRFFVDGDWAVHGAPQESLYSVAGNPVDPLAQVTRLFCEHLLERALNCIAQPSPGAADGDREFSDALGYLQLLNSCSDAVGAPACSFSVSSSMATTTGTDPVAKWWASLTAVVIHWLRRDEEAAERLYPLVEHIPQVLQETERPLPRAALYSFKAARALLDHRKVESSPASLAICEKASGYLRDSLASTSTASSIDKAMQLLLCDLLLVARTSLWRRQQSAASAQGAHGTSNGPQASALELRGFQHDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPARTHQLLDRSLRRRAGSSGKGGAAAELEPRPTWREHTEALLLASCYLPPAFLSAPGQRVSMLAEAARTVEKLGDHRLLLDCQQMLLRLGGGTTVTSS
Protein: RNA polymerase sigma factor FliA (RNA polymerase sigma factor for flagellar operon) (Sigma F) (Sigma-27) (Sigma-28) (P0AEM6)
Organism: Escherichia coli (strain K12)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00962}.
Interaction partners:
- Regulator of sigma S factor FliZ
- Negative regulator of flagellin synthesis
- Flagellar basal body rod protein FlgB
- Flagellin
- Flagellar basal-body rod protein FlgC
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 2
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Basal-body rod modification protein FlgD
Sequence:
MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL
Protein: Long-chain acyl-protein thioester reductase (EC 1.2.1.50) (Acyl-CoA reductase) (P12748)
Organism: Aliivibrio fischeri (Vibrio fischeri)
Function: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
Interaction partners:
Sequence:
MNKCIPMIINGMIQDFDNYAYKEVKLNNDNRVKLSVITESSVSKTLNIKDRINLNLNQIVNFLYTVGQRWKSEEYNRRRTYIRELKTYLGYSDEMARLEANWIAMLLCSKSALYDIVNYDLGSIHVLDEWLPRGDCYVKAQPKGVSVHLLAGNVPLSGVTSILRAILTKNECIIKTSSSDPFTANALVSSFIDVNADHPITKSMSVMYWPHDEDMTLSQRIMNHADVVIAWGGDEAIKWAVKYSPPHVDILKFGPKKSLSIIEAPKDIEAAAMGVAHDICFYDQQACFSTQDVYYIGDNLPLFLNELEKQLDRYAKILPKGSNSFDEKAAFTLTEKESLFAGYEVRKGDKQAWLIVVSPTNSFGNQPLSRSVYVHQVSDIKEIIPFVNKNRTQTVSIYPWEASLKYRDKLARSGVERIVESGMNNIFRVGGAHDSLSPLQYLVRFVSHERPFNYTTKDVAVEIEQTRYLEEDKFLVFVP
Protein: Bifunctional epoxide hydrolase 2 (EC 3.3.2.9) (Ephx2 protein) (Epoxide hydrolase 2, cytoplasmic) (Q5PRC6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKKAVLFSLWGGVVTPQIGQAFQKFEETTGISKGFIKNVETKLGSDNALHRAEKGKTTLAQMIPEFDAECQKVAADQGLSLPAQFSTQKLFDDMGKVEFNMTFLDAAAVLRRNGIATGILANIWVDDTAQRGSIARVLSVLESRFDLVLRSCHAGVRIPEPDFFKHALEKLAVKPQEALWLDVDEESVKAAEGLGIMAVQVKDVTEALTEIQKLTGIEVTSDLQPPSCDPEKVSHGYVNIKPGVKIHYVEMGDGPPVLLCHGFPESWFSWRYQIPALADAGFRVLAPDMKGYGGSTAPPDIEEYSQEQIMLDLVTFLDKMAIAQVTLVGHDWGGVLVWNMAQFHPERVRAVASLNTPLFPVDPNTNPMEKLMAIPIFDYQIYFQKPGVAEAELEKNLKRTFKLMFISSSDTGGFPKLSPAGVCQRGGLFVGSPDDPPRSSMLSVSALQFYTEQYSKSGFRGPLNWYRNYERNWRWMVSRPRAKILMPALMVTAGKDPVLLPAFATGMENLIPNLSRGHIEECGHWTQMERPAELNKILISWLKETHQKASISVHPKL
Protein: Appendage-associated protein (Q5SF94)
Organism: Anaplasma marginale (strain Illinois)
Function: Associates with actin filament appendages that are formed in the inclusion appendages of the parasitophorous vacuole during infection of the host erythrocyte.
Subcellular location: Secreted {ECO:0000269|PubMed:15557651}.
Interaction partners:
Sequence:
MGCPVSRGGSPGCGRRIAEELRFFVVDREASMCGDSCNGGGDRQQRQELAAAARASLLCLGGVMQQHITAAKARAELRKELDAIDAEWRPVIARESLRKELKAIDAQWQHAITFLRISRAIVVSIELSKELKAIDAGWEPVIIHEAQKKKREREERVAQVRRELRAELRAIDAEWRLVIARESLRKELDAIDAECRHTIKLRSALRAIEGRMELSKELKAIDAEWRPAIRLESAYRAIIGSIELSKELKAIDAETQHAVELRRALRTIEGRIELSRELKAIDAEWAPRIAQAELAAAADALKRAADKLQALGKMDTTSTPGTDLIGVVTTAIATLAAAGMQPAPSTALTGVAAEVATPSTALGV
Protein: Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl leukotrienase) (GGL) (Gamma-glutamyl transpeptidase-related enzyme) (GGT-rel) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain] (Q9QWE9)
Organism: Rattus norvegicus (Rat)
Function: Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione-S-conjugate. Converts leukotriene C4 (LTC4), a glutathione-S-conjugate, to leukotriene D4 (LTD4). Does not cleave gamma-glutamyl compounds such as gamma-glutamyl leucine. May also catalyze a transpeptidation reaction in addition to the hydrolysis reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Acts as a negative regulator of geranylgeranyl glutathione bioactivity by cleaving off its gamma-glutamyl group, playing a role in adaptive immune responses.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9Z2A9}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Z2A9}.
Interaction partners:
- Glutathione synthetase
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- 5-oxoprolinase
- Leukotriene C4 synthase
- Gamma-glutamylcyclotransferase
- Cytosol aminopeptidase
- Aminopeptidase N
- Glutathione reductase
- Glutamate--cysteine ligase catalytic subunit
Sequence:
MAWGHRTTVCLVLLGVSLGLAIIVLAVVLPHHQASCRPDAFTRAAVAADSKICSDIGRVILQQQGSPVDAAIAALICTGVVNPQSMGLGGGVVFTIYNASTGKVEVINARETVPASHDQRLLDQCTNALPLCTGAQWIGVPGELRGYAEAHRRYGRLPWAQLFQPTIALLREGFRVPPILSQFLNTSFLQPCLNSSTLRQLFFNGTETLRSQDPLPWPALANTLETVAKEGAEVLYTGKLGQTLVEDIAWQGSQLTVQDLAAFRPKVVEPLEMALGNYTLYSPPPPAGGAILSFILNVLKGFNFSAETVAGPEGKVNMYHHLVEALKFAVGQRWRLWDPYSHPGIQNISQDLLRETLAQHIRQQIDGRGDHQLSHYNLSGVRGNSMGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGILLNNELLDLCWRHKPGSTVTPPPVPGEQPPSSMVPSILINEVQGSKLVIGGAGGELIISAVTQAIVNKLWLGFSLTDAIAAPILHVNSKGHVEYEPKFNQEVRKGLQDRGQSQSQSQRPVFLNSVQAVFQEGPCVYAASDLRKAGKASGY
Protein: Sulfhydryl oxidase 1 (mSOx) (EC 1.8.3.2) (Quiescin Q6) (Skin sulfhydryl oxidase) (Q8BND5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.
Subcellular location: [Isoform 1]: Golgi apparatus membrane {ECO:0000250|UniProtKB:O00391}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00391}. Secreted {ECO:0000269|PubMed:26819240}. Note=A small proportion is secreted, probably via a proteolytic cleavage that removes the membrane anchor. {ECO:0000250|UniProtKB:O00391}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:12354420}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
Interaction partners:
- Immunoglobulin kappa chain variable 4-54.
- Sex-determining region Y protein
- Catenin beta-1
- POU domain, class 5, transcription factor 1
- Transcription factor SOX-9
- Transcription factor SOX-5
- Transcription factor SOX-4
- Transcription factor SOX-2
- Transcription factor SOX-11
- Transcription factor SOX-3
Sequence:
MRRCGRLSGPPSLLLLLLLLSPLLFSGPGAYAARLSVLYSSSDPLTLLDADSVRPTVLGSSSAWAVEFFASWCGHCIAFAPTWKELANDVKDWRPALNLAVLDCAEETNSAVCREFNIAGFPTVRFFQAFTKNGSGATLPGAGANVQTLRMRLIDALESHRDTWPPACPPLEPAKLNDIDGFFTRNKADYLALVFEREDSYLGREVTLDLSQYHAVAVRRVLNTESDLVNKFGVTDFPSCYLLLRNGSVSRVPVLVESRSFYTSYLRGLPGLTRDAPPTTATPVTADKIAPTVWKFADRSKIYMADLESALHYILRVEVGKFSVLEGQRLVALKKFVAVLAKYFPGQPLVQNFLHSINDWLQKQQKKRIPYSFFKAALDSRKEDAVLTEKVNWVGCQGSEPHFRGFPCSLWVLFHFLTVQANRYSEAHPQEPADGQEVLQAMRSYVQFFFGCRDCADHFEQMAAASMHQVRSPSNAILWLWTSHNRVNARLSGALSEDPHFPKVQWPPRELCSACHNELNGQVPLWDLGATLNFLKAHFSPANIVIDSSASRHTGRRGSPEATPELVMDTLKLESRNSVLGHEQAASAESPGATALDVPAEKPEASGPQELYTGLRMGGASPGQGPPERMEDHQRDMQENAPGQQHLSKRDTEALFLPEVNHLQGPLELRRGGRSPKQLAPILEEEPEALAIQGQGQWLQVLGGGISHLDISLCVGLYSVSFMGLLAMYTYFRARLRTPKGHASYPTA
Protein: Glycogen [starch] synthase, muscle (EC 2.4.1.11) (Glycogen synthase 1) (P13834)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Protein phosphatase 1 regulatory subunit 3C
- UTP--glucose-1-phosphate uridylyltransferase
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1 regulatory subunit
- Glycogenin-1
- Protein phosphatase 1 regulatory subunit 3A
- Glycogen synthase kinase-3 beta
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MPLSRTLSVSSLPGLEDWEDEFDLENSVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEPPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQNEEKPHVVAHFHEWLAGIGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALAKAFPDHFTYEPHEADATQGYRYPRPASVPPSPSLSRHSSPHQSEDEEEPRDGLPEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSSGGSKRSNSVDTSSLSTPSEPLSPASSLGEERN
Protein: Cdc42-interacting protein 4, isoform K (M9PE52)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLALLASGSSRSSSNNKLAESENSAQNSNNMSWGTELWDQNENLAIHTNRGIDALDKFANFLRDRVAIETEYAGKLRRLVKNYQPKKKEEEDNEFTSVQAFRNLLKEVGDLAGQREVVSESLQLQIIAGVTLLSKTLREERKKCLSDGATLQQNLTTQLSSLDRAKRNYEKAYRDSEKAVDSYKRADMDLNLSRAEVERYKNVMTSKIQQSDDAKNEYANQLQKTNNLQQQHYSMLLPSVLNRLQELDEKRTRGFREFIVGAADVESSVAPIIARCMEGIVKAGESINEKEDTFKVIERYQSGFTPPRDIPFEDLSKCDPDSVQDSHYSNSTSNHLTIRGTMSANKLKKRVGIFNIFGSNKNSLTADGQKEDFSDLPPNQRRKKLQAKIAELTQNIAQETKARDGLMKMKIVYEANSSLGNPMTVEGQLNESEHKLEKLKVDLKKYQGFLEKASQVPTATSSPQASRNQLQNGHRTSRHSNGSADDHHDDGDDQPDDAGSLSSSASPESGLGTSHTSLPGSGQGSANENAIGEDTYYETEVETLNPVGKCRALYPFEASSEGSIPMSEGEELQVIEIDQGDGWTRVRRENNSNGWDEGFVPTSYIEITLYA