wanglab/gogpt-training-data huggingface dataset:
Protein: Antimicrobial peptide 2 (XT-2) (P84382)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Has very strong antibacterial activity against Gram-positive bacterium S.aureus and very weak activity against Gram-negative bacterium E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:11738090}.
Interaction partners:
Sequence:
GVWSTVLGGLKKFAKGGLEAIVNPK
Protein: Prostaglandin E2 receptor EP2 subtype (PGE receptor EP2 subtype) (PGE2 receptor EP2 subtype) (Prostanoid EP2 receptor) (Q9XT82)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prostaglandin E2 receptor EP1 subtype
- Prostaglandin E receptor 4
- G protein subunit alpha i1.
- Guanine nucleotide-binding protein G
- G protein subunit alpha i3.
- Proopiomelanocortin.
- Pro-glucagon
- Vasoactive intestinal peptide.
- Natriuretic peptides A
- Gastric inhibitory polypeptide.
Sequence:
MGSISNNSGSEDCESREWLPSGESPAISSAMFSAGVLGNLIALALLARRWRGDAGRRAGRGNSISLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLMALEPERRACTYFAFAMTFFSLATMLMLFAMALERYLSIGRPYFYQRHVTRRGGLAVLPTIYTVSLLFCSLPLLGYGQYVQYCPGTWCFIRHGRTAYLQLYATLLLLLIVAVLACNFSVILNLIRMHRRSGRSRCGPSLGSCRDGSGTRRRGERVSVAEETDHLILLAIMTITFAICSLPFTIFAYMNETSSRREKWDLQALRFLSINSIIDPWVFAIFRPPVLRLMRSVLCCRVSLRAQDATQTSCSIQSNASRLTFVDTS
Protein: Aminoalkylphosphonate N-acetyltransferase (EC 2.3.1.280) (KAT) (Peptidyl-lysine N-acetyltransferase) (EC 2.3.1.-) (P16691)
Organism: Escherichia coli (strain K12)
Function: Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoalkylphosphonic acids, including aminomethylphosphonate, (S)-1-aminoethylphosphonate and 2-aminoethyl- and 3-aminopropylphosphonate, using acetyl-CoA as acetyl donor. Is required for the utilization of aminomethylphosphonate and (S)-1-aminoethylphosphonate as a phosphate source via the C-P lyase pathway. Is also essential for the detoxification of (S)-1-aminoethylphosphonate, a structural analog of D-alanine that has bacteriocidal properties due to inhibition of cell wall synthesis. Also acts as a N-epsilon-lysine acetyltransferase that catalyzes acetylation of several proteins.
Interaction partners:
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Probable transcriptional regulator PhnF
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Putative phosphonates utilization ATP-binding protein PhnK
Sequence:
MPACELRPATQYDTDAVYALICELKQAEFDHHAFRVGFNANLRDPNMRYHLALLDGEVVGMIGLHLQFHLHHVNWIGEIQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGYEQSHFRFTKAL
Protein: Neuropeptide B (Preproprotein L7) (rPPL7) [Cleaved into: Neuropeptide B-29 (NPB29) (L7C)] (Q8K4P2)
Organism: Rattus norvegicus (Rat)
Function: May be involved in the regulation of feeding, neuroendocrine system, memory and learning. May be involved in the afferent pain pathway (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Neuropeptides B/W receptor type 1
- Neuropeptide W
Sequence:
MVRCRTLVAAALALLLTPALAWYKPAAGSHHYSVGRAAGLLSSFHRFPSTRRSESPALRVGTVPLRNLEMRPSVRSLALCVKDVTPNLQSCQRQLNSRGTFQCKADVFLSLHKAECQSA
Protein: Mitochondrial glutamate carrier 2 (GC-2) (Glutamate/H(+) symporter 2) (Solute carrier family 25 member 18) (Q9H1K4)
Organism: Homo sapiens (Human)
Function: Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q505J6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vitamin D-binding protein
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Guanylyl cyclase-activating protein 3
Sequence:
MTHQDLSITAKLINGGVAGLVGVTCVFPIDLAKTRLQNQHGKAMYKGMIDCLMKTARAEGFFGMYRGAAVNLTLVTPEKAIKLAANDFFRRLLMEDGMQRNLKMEMLAGCGAGMCQVVVTCPMEMLKIQLQDAGRLAVHHQGSASAPSTSRSYTTGSASTHRRPSATLIAWELLRTQGLAGLYRGLGATLLRDIPFSIIYFPLFANLNNLGFNELAGKASFAHSFVSGCVAGSIAAVAVTPLDVLKTRIQTLKKGLGEDMYSGITDCARKLWIQEGPSAFMKGAGCRALVIAPLFGIAQGVYFIGIGERILKCFD
Protein: Probable WRKY transcription factor 14 (AR411) (WRKY DNA-binding protein 14) (Q9SA80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- AT1G22750 protein
- NEFA-interacting nuclear protein
- At2g43110
- Alpha/beta-Hydrolases superfamily protein
- BTB/POZ domain-containing protein At3g19850
- Carboxyl-terminal proteinase-like protein
- Uncharacterized protein T14D3.50
- Probable LRR receptor-like serine/threonine-protein kinase At1g51810
- CDPK-related kinase 3
- CDPK-related kinase 2
Sequence:
MCSVSELLDMENFQGDLTDVVRGIGGHVLSPETPPSNIWPLPLSHPTPSPSDLNINPFGDPFVSMDDPLLQELNSITNSGYFSTVGDNNNNIHNNNGFLVPKVFEEDHIKSQCSIFPRIRISHSNIIHDSSPCNSPAMSAHVVAAAAAASPRGIINVDTNSPRNCLLVDGTTFSSQIQISSPRNLGLKRRKSQAKKVVCIPAPAAMNSRSSGEVVPSDLWAWRKYGQKPIKGSPFPRGYYRCSSSKGCSARKQVERSRTDPNMLVITYTSEHNHPWPIQRNALAGSTRSSTSSSSNPNPSKPSTANVNSSSIGSQNTIYLPSSTTPPPTLSSSAIKDERGDDMELENVDDDDDNQIAPYRPELHDHQHQPDDFFADLEELEGDSLSMLLSHGCGGDGKDKTTASDGISNFFGWSGDNNYNNYDDQDSRSL
Protein: Inter alpha-trypsin inhibitor, heavy chain 4 (ITI heavy chain H4) (ITI-HC4) (Inter-alpha-inhibitor heavy chain 4) (A6X935)
Organism: Mus musculus (Mouse)
Function: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-2-glycoprotein 1
- Hemopexin
- Haptoglobin
- Alpha-2-HS-glycoprotein
- Murinoglobulin-1
- Histidine-rich glycoprotein
- Apolipoprotein A-II
- Kininogen-1
- Vitronectin
- Plasminogen
Sequence:
MKSPAPAHMWNLVLFLPSLLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQELLQRRLGMYELLLKVRPQQLVKHLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGGSIQIEEGYFVHHFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGTNINNAVLLAVELLDRSNQAELLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMALDNGGLARRIYEDSDSALQLQDFYHEVANPLLSSVAFEYPSDAVEEVTRYKFQHHFKGSEMVVAGKLQDQGPDVLLAKVSGQMHMQNITFQTEASVAQQEKEFKSPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEGQEQFQVAEKPVEVGDGMQRLPLAAQAHPFRPPVRGSKLMTVLKGSRSQIPRLGDAVRASRQYIPPGFPGPPGPPGFPAPPGPPGFPAPPGPPLASGSDFSLQPSYERMLSLPSVAAQYPADPHLVVTEKSKESTIPEESPNPDHPQVPTITLPLPGSSVDQLCVDILHSEKPMKLFVDPSQGLEVTGKYENTGFSWLEVTIQKPHLQVHATPERLVVTRGRKNTEYKWKKTLFSVLPGLKMTMNMMGLLQLSGPDKVTIGLLSLDDPQRGLMLLLNDTQHFSNNVKGELGQFYRDIVWEPPVEPDNTKRTVKVQGVDYLATRELKLSYQEGFPGAEISCWTVEI
Protein: Stromelysin-3 (SL-3) (ST3) (EC 3.4.24.-) (Matrix metalloproteinase-11) (MMP-11) (P24347)
Organism: Homo sapiens (Human)
Function: May play an important role in the progression of epithelial malignancies.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Furin
- Syntenin-1
- Collagen alpha-1
- Stromelysin-2
- DENN domain-containing protein 2B
- Interstitial collagenase
- Beta/gamma crystallin domain-containing protein 1
- Matrilysin
- Collagen alpha-1
Sequence:
MAPAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPWHAALPSSPAPAPATQEAPRPASSLRPPRCGVPDPSDGLSARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDDQGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPLSLSPDDCRGVQHLYGQPWPTVTSRTPALGPQAGIDTNEIAPLEPDAPPDACEASFDAVSTIRGELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPSPVDAAFEDAQGHIWFFQGAQYWVYDGEKPVLGPAPLTELGLVRFPVHAALVWGPEKNKIYFFRGRDYWRFHPSTRRVDSPVPRRATDWRGVPSEIDAAFQDADGYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGCAEPANTFL
Protein: Aldo-keto reductase family 1 member C13 (EC 1.1.1.-) (Q8VC28)
Organism: Mus musculus (Mouse)
Function: Catalyzes the dehydrogenation of 17-beta-hydroxysteroids. May also exhibit significant activity with a variety of cyclic and alicyclic alcohols. Uses both NAD and NADP, but the activity is much greater with NAD than with NADP (By similarity).
Interaction partners:
- Aldo-keto reductase a
Sequence:
MSSKQHCVKLNDGHLIPALGFGTYKPKEVPKSKSLEAACLALDVGYRHVDTAYAYQVEEEIGQAIQSKIKAGVVKREDLFITTKLWCTCFRPELVKPALEKSLKKLQLDYVDLYIMHYPVPMKSGDNDFPVNEQGKSLLDTVDFCDTWERLEECKDAGLVKSIGVSNFNHRQLERILNKPGLKYKPVCNQVECHLYLNQRKLLDYCESKDIVLVAYGALGTQRYKEWVDQNSPVLLNDPVLCDVAKKNKRSPALIALRYLIQRGIVPLAQSFKENEMRENLQVFGFQLSPEDMKTLDGLNKNFRYLPAEFLVDHPEYPFVEEY
Protein: V-type proton ATPase subunit c''2 (V-ATPase subunit c''2) (Vacuolar H(+)-ATPase subunit c'' isoform 2) (Vacuolar proton pump subunit c''2) (Q9SLA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein {ECO:0000269|PubMed:18507826}. Golgi apparatus membrane {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein {ECO:0000269|PubMed:18507826}.
Interaction partners:
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit e2
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G1
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit B2
Sequence:
MSGVAIHASSWGAALVRISPYTFSAIGIAISIGVSVLGAAWGIYITGSSLIGAAIEAPRITSKNLISVIFCEAVAIYGVIVAIILQTKLESVPSSKMYDAESLRAGYAIFASGIIVGFANLVCGLCVGIIGSSCALSDAQNSTLFVKILVIEIFGSALGLFGVIVGIIMSAQATWPTK
Protein: KCNQ potassium channel, isoform G (A0A0B4KF62)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDPDNDIYAFYDIRGKCRPGRPNSERILQPRMSLLGKPLNYNRGTRRDVRYRRLQSRLYNFLERPRGLHAIFYHVMVFLMVFTCLALSVFSTIKEYEEDAVYILFRMEILVVIWFTMEFGARLWSSGCRSRYQGCLGRLKFVKRPFCIIDIVTILASIVVLGMGTSGQVFATSALRGLRFFQILRMVRMDRRGGTWKLLGSVVYAHRQELITTMYIGFLGLIFASFLVYMWEKDVNDKFSNFAQALWWGVITLCTVGYGDMVPITWQGKLIASCCALLGISFFALPAGILGSGFALKVQQQQRQKHMIRRRQPAATLIQAVWRCYAADEHSVSVATWNIHRVALPSPPASRASSSFKHNTSFVARLPTIRRHKSQTIQTPGGGDGGGVSKPPGSSRASTRYTRTIRDINASVENLDEEDEPRCTQLTNRHKTAIRFIRKLKYFVARRKFKEALKPYDVKDVMEQYAAGHVDLLGRVKMLHLRLDQILGKQGSKAKDVYASKISLASRVVKVERQVADIEEKLDILIKAYMEDRDRFLALPLPAKPKIHSISPSHKPLHHAHNLAMIDVWKRTAALSVHPEQVTTTPLLNPSAPDSSELRSLTATQTPTTTTDAIATQTPMPPHVQHTATNTKSSVLNSYQLGSEKQQHNDVFMTELENRTKKRVTLSLHRSTSEPYSKQEQRITIPDEGADSLDSSAKPTPPDSSIILIDEYEDFEEEDLNCEGEMDHFPTWEIDSDIGVEVDVDADADGDCDESTEDTALLQCATRTAIVITPISPVSSAHNLQQLNDQTTTLNKSNLLPPDSG
Protein: Clu domain-containing protein (Q54ZX7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSRKIIGLISKFENLNVNNNNNSNNNNNSNNNNSGNSINSNIGSNNLKNNVNRFNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTTTTTTTTTTTTTRTSSSNNNMNNNKSNNSNNKNDGNNSDNNVNRFNNNKMNKIMNNYIKNNSYNNNDDNNNNKKQEGEEEGEEEEEKLKLVDIKVEIRVEEDIEGEEELVTKSIVNSLSVSCLSTPSYSTNLSDSISSLQSPVLTPLSSSPSITPLSSSPSSLSSSSSPSHSRQDSLNSNCNSLTLSTPTPSHTPPISPPLQPSNPINHKYHIKNLQFDEKKSLQNILLSRKISTSFDPRKDSDDEEDDDDDEEDEVDNNNQNNNNIEEQIKNDLEEKENEIIDSFYNKNDDQLSDNSNDTVVRVNDAEEDDDDVSDDEFSQDDNKHCSNNNLKQIQINFENAICLVEQKKNSHSLNNNSNDNSSPIQQKQEQSKDAKEKIQQQPQQPQQPQQQQQQAVDLPGGYSIIVKDKGLRVSICASTRESFGDYSQSSRSSIESSIETSIGSNKSFDDTNKNEDIYDIPLLNIEKFTGQGHFKDYHWNSTFQSIVELPDNDIKRPKELSMLVEEFVYNANLIGRLLISQVKLSKESKIIPEWNIGGIGGGLKFKCNDIIFKFVEDLPIQDTTTSSTNNNNNNNNKKDNKLKWLYGGDKQSNEKAKKGASHEIKSLNHFKMASNNSIIKTPLMAVIDYLGYRVIAISNLPINNNNENNDTLVYGSRDGGNIIKSSNSTIENEMKNICNKLNLSEHSVKSSKDGLSKRIYGPVDIEIHFSDITREHYAIDFQRLFPPEDPFYFKDSLVKSNSSQLYRLLRPELVSKSPLPLSSDGFSQIQHDKDSFIQNENIRKITNILHTKVIPSFIKYIDTNSIGTIKSLKSSKSIHDSIFKVYDNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDIVDYGGDDDFNESHLINEIQIEGTPTTTTTNNTTRNNNIEWLSNINGDRYSNKDRNSRNNNSNNNNNLNNFNQKSIDIKTYIDEIHSFGINLRYLGLLSSKLKTKPLKLLLQSEMSARVWKSIISQKIRESEHPSEGYYKLILSNIFELILSNQSTQSTIEKNREFWCLNKRGNFKFIALHCFHECISDEDRLDTVDYRNIIDNRFVVYRIIQMLNIKINQEALNQFCSNSNYIITFNDIEEIGSKIKYPSIVDVAAGSFLLYEALNNINGDSTNPSNPLAAARLCEQAKIKFYSALCSMPLSIPVMLNLGHSYLLSDRINTNYKTSIENLKSALNHINSNDPKIKSLKGVFCLKLATIQLFYFNNTFEFQKTILKLKEFWKPIPQIEIIKILLFIFNIQNNNNNNNSNNNNNNINSLQYQNEGRKSINSSIIQLKSLEFNDIKIINELITLCIILDEFKLSINLKEELFNKISKINHFSIPNNLLNLFMETGKSYQPTNYFQNQTSIQEQIIISINNIIFSRVNNLQVISLSDLIINESLLDNFSNLVELKIVNCGFIFGKSNQQQQQQQQQLDPVIEILSRSKHLKSLYIDFSNNQSQNCCLRVTNQYSKLRSLALIHYLGTMKILVDQQSLSWDLEYLNLNHSLNLIGLIKSDRTISTPYLKSLSIAGFSNTINKDNNNKDNNNKDNNKDNNTINTINNKDNLNSNISSTSILDIRLLLNMEELDISYCTFTPIFIIQLISGSPGLRVLKATNNQNVQLVAIKLLKPFSNLQEIYLDAIKISKPKQFIRLKEFTNRNLLRVLHLPNLIDLKSPSTFNSKDMFDLLCDFTNLVDLKLPCGFSFHNFTNWLQKGQIPLSTIFKNLKNLDLEKNEISINSILSVLKVSPFLESLSLYGCAWKEIQPLEGSGENQFALFRGILADLTPILFNNIKELNIANCGLLKKDIPILLYKIFPSCSILKSDFLNLGKNFSKFSSSFIQFIKINNQNKYSI
Protein: Sulfotransferase 1B1 (ST1B1) (EC 2.8.2.1) (Sulfotransferase family cytosolic 1B member 1) (Q3T0Y3)
Organism: Bos taurus (Bovine)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine small phenols such as 1-naphthol and 4-nitrophenol. Catalyzes also the sulfate conjugation of dopamine and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3) (By similarity). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25539458}.
Interaction partners:
Sequence:
MTSPKDVLRKNLKLIHGCPITYAFANNWEKIEQFQSRPDDIMIVTYPKSGTTWISEIVDMVLHDGDVEKCKRDVITAKVPMLELALPGLRTSGLEQLEKNPSPRVVKTHLPIDLIPKSFWENNCKIIYLARNAKDVAVSFYHFDLMNNLQPLPGTWGEYLEKFLTGNVAYGSWFNHVKSWWKKKEGHPILFLFYEDMKENPKQEIKKVVRFLEKNLDDEILDKIIYHTSFEMMKDNPLVNYTHLPSEVMDHSKSSFMRKGIAGDWKNYFTVAQNEKFDAIYKKEMSETELQFRTEI
Protein: Imidazole glycerol phosphate synthase hisHF, chloroplastic (IGP synthase) (IGPS) (ImGP synthase) (EC 4.3.2.10) (Protein HISTIDINE BIOSYNTHESIS 4) [Includes: Glutaminase (EC 3.5.1.2); Cyclase] (Q9SZ30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Histidine biosynthesis bifunctional protein hisIE, chloroplastic
- 1-
- Imidazoleglycerol-phosphate dehydratase 1, chloroplastic
- Imidazoleglycerol-phosphate dehydratase 2, chloroplastic
- Histidinol dehydrogenase, chloroplastic
- ATP phosphoribosyltransferase 1, chloroplastic
- ATP phosphoribosyltransferase 2, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Histidinol-phosphate aminotransferase 2, chloroplastic
- Helicase protein with RING/U-box domain-containing protein
Sequence:
MEATAAPFSSIVSSRQNFSSSSSIRASSPASLFLSQKSIGNVNRKFKSPRSLSVRASSTSDSVVTLLDYGAGNVRSIRNALRHLGFSIKDVQTPGDILNADRLIFPGVGAFAPAMDVLNRTGMAEALCKYIENDRPFLGICLGLQLLFDSSEENGPVKGLGVIPGIVGRFDASAGIRVPHIGWNALQVGKDSEILDDVGNRHVYFVHSYRAIPSDENKDWISSTCNYGESFISSIRRGNVHAVQFHPEKSGEVGLSVLRRFLHPKLPATQKPMEGKASKLAKRVIACLDVRTNDKGDLVVTKGDQYDVREQSNENEVRNLGKPVDLAGQYYKDGADEISFLNITGFRDFPLGDLPMIQVLRQTSKNVFVPLTVGGGIRDFTDASGRYYSSLEVAAEYFRSGADKISIGSDAVSAAEEFIKSGVKTGKSSLEQISRVYGNQAVVVSIDPRRVYVNHPDDVPYKVIRVTNPGPNGEEYAWYQCTVSGGREGRPIGAFELAKAVEELGAGEILLNCIDCDGQGKGFDIDLVKLISDSVGIPVIASSGAGTPDHFSEVFEKTNASAALAAGIFHRKEVPIQSVKEHLQEERIEVRI
Protein: Ferric/cupric reductase transmembrane component 7 (EC 1.16.1.9) (Ferric-chelate reductase 7) (Q12333)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cell surface metalloreductase. May be involved in copper homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17553781}; Multi-pass membrane protein {ECO:0000269|PubMed:17553781}.
Interaction partners:
- Probable ferric reductase transmembrane component 8
- Metal-binding activator 1
- Iron-regulated transcriptional activator AFT1
- Copper transport protein CTR3
- Plasma membrane iron permease
Sequence:
MIEERDLVLSNGIHCIADIHSELYARLKKESQAATPWVYQKQYGKFVTYFVAVIIFLSLIKKLAFMYYDSSEEFLPEKKNSPTTPSVFLARIMTKLVAFNRYICYRKFPTLIFSYLGIPTSVGTFLVVMATTLYTLLYCFVPHPFYRPCAGFGSPPLSVRAGIMAISLVPFVFSLSGKINVIGWLVGLSYEKINIYHQWASILCLFFSWVHVIPFLRQARHEGGYERMHQRWKASDMWRSGVPPILFLNLLWLSSLPIARRHFYEIFLQLHWILAVGFYISLFYHVYPELNSHMYLVATIVVWFAQLFYRLAVKGYLRPGRSFMASTIANVSIVGEGCVELIVKDVEMAYSPGQHIFVRTIDKGIISNHPFSIFPSAKYPGGIKMLIRAQKGFSKRLYESNDDMKKILIDGPYGGIERDIRSFTNVYLICSGSGISTCLPFLQKYGPILHKTNLEVITLDWVVRHREDISWIRDEMCTLSNNLRQLFLDGKIVVRIYVCSDSTVPGIIKTFPQTIDTASDQSDLAKREKDTEFGQDDTESNSTFDKSNNEYKGLITIIPSKPDLNQVINDYQIGFRNCFICSGSDSLRYTVGNSVAGLQAKVFSNKNVEECYLHSESFGY
Protein: Sperm acrosome membrane-associated protein 1 (Q9DA48)
Organism: Mus musculus (Mouse)
Function: Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis. Important for male fertility.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:22949614}; Single-pass type I membrane protein {ECO:0000305}. Note=Primarily found in the equatorial segment of the acrosome (PubMed:22949614). The tyrosine phosphorylated protein localizes to a smaller region within the equatorial segment (By similarity). Also expressed weakly in the principal segment (By similarity). {ECO:0000250|UniProtKB:D5K8A9, ECO:0000250|UniProtKB:Q9HBV2}.
Interaction partners:
- Zona pellucida-binding protein 1
- Izumo sperm-egg fusion protein 1
- Serine-rich single-pass membrane protein 1
- Zona pellucida sperm-binding protein 3 receptor
- Spermatogenesis-associated protein 46
- Probable C-mannosyltransferase DPY19L2
- Sperm acrosome membrane-associated protein 3
- Zona pellucida-binding protein 2
- Spermatogenesis-associated protein 16
Sequence:
MRARGAGCPAGLLAVGWLILVGLQASQASNVTSSGGGVQEPAVAREGESESESESEEEAENEGEVPESETTAEADAEEEVQNRTIVKEVEFGMCTVTCGVGIREVILTNGCPGGESKCVVRVEECRGPVDCGWGKPISENLDSARLSCVHISPENRFKYVWKLLKPDQQPVILTNDSAVLEITREIRPLAFECDTLDNNEMVASVKFTVYTTNELQMRRSSRPDTDAVLVFVLTIGVIICIFVIFVLIFIIINWAAVKSFWGSKTSATEIQSELSSMRYKDSTSLDQSPTDIPVHEDDALSEWNE
Protein: Major facilitator superfamily domain-containing protein 3 (Q96ES6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Molybdate-anion transporter
Sequence:
MRGKLLPLAGLYLVQGLPYGLQSGLLPVLLRAGGLSLTRVGLAKVLYAPWLLKLAWAPLVDAQGSARAWVTRSTAGLGLVCGLLAGLPPPGAGQAGLPAAVAGLLLLLNLGAAMQDVALDALAVQLLEPAELGPGNTVQVVAYKLGAALAGGALLALLPTFSWPQLFLLLAATYWLAAALAWAAPALRRLPQQPPSEQRPHTAHLLRDVLAVPGTVWTAGFVLTYKLGEQGASSLFPLLLLDHGVSAPELGLWNGVGAVVCSIAGSSLGGTLLAKHWKLLPLLRSVLRFRLGGLACQTALVFHLDTLGASMDAGTILRGSALLSLCLQHFLGGLVTTVTFTGMMRCSQLAPRALQATHYSLLATLELLGKLLLGTLAGGLADGLGPHPCFLLLLILSAFPVLYLDLAPSTFL
Protein: von Willebrand factor A domain-containing protein 1 (Q6PCB0)
Organism: Homo sapiens (Human)
Function: Promotes matrix assembly (By similarity). Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (Probable).
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q8R2Z5}.
Interaction partners:
- Collagen alpha-1
Sequence:
MLPWTALGLALSLRLALARSGAERGPPASAPRGDLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHTGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFVDVDDLHIIVQELRGSILDAMRPQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDVALVPESNVRLLRPQILRVRTRPGEAGPGASGPESGAGPAPTQLAALPAPEEAGPERIVISHARPRSLRVSWAPALGSAAALGYHVQFGPLRGGEAQRVEVPAGRNCTTLQGLAPGTAYLVTVTAAFRSGRESALSAKACTPDGPRPRPRPVPRAPTPGTASREP
Protein: Syntaxin-19 (Q8N4C7)
Organism: Homo sapiens (Human)
Function: Plays a role in endosomal trafficking of the epidermal growth factor receptor (EGFR).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8R1Q0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8R1Q0}. Cytoplasm {ECO:0000250|UniProtKB:Q8R1Q0}.
Interaction partners:
- Synaptosomal-associated protein 23
- Syntaxin-binding protein 2
- Vesicle-associated membrane protein 8
- Syntaxin-binding protein 5-like
- Syntaxin-binding protein 1
- Syntaxin-binding protein 5
- Syntaxin-11
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 2
- Protein unc-13 homolog D
Sequence:
MKDRLQELKQRTKEIELSRDSHVSTTETEEQGVFLQQAVIYEREPVAERHLHEIQKLQESINNLADNVQKFGQQQKSLVASMRRFSLLKRESTITKEIKIQAEYINRSLNDLVKEVKKSEVENGPSSVVTRILKSQHAAMFRHFQQIMFIYNDTIAAKQEKCKTFILRQLEVAGKEMSEEDVNDMLHQGKWEVFNESLLTEINITKAQLSEIEQRHKELVNLENQIKDLRDLFIQISLLVEEQGESINNIEMTVNSTKEYVNNTKEKFGLAVKYKKRNPCRVLCCWCCPCCSSK
Protein: ABC transporter B family member 7 (ABC transporter ABCB.7) (Q55DA7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
Sequence:
MTRKSNYNYLDEDNIEDESPIGLGTSPIEFNLDKENKNKKRNSVKFNLDTPLPIINNKSSQDNNNKNNNNNNNNNNNNNNNNNNNNNNNNNNKNNKNKINNSLNSITPYLVDYKDDFDFKRSVYDFDDVDYLEEDSFDEHSFYKTSYSTRRCIYRILTYIRPQIWYFVFAFLALSITTLCQLALPYCFANGIQEAIRVNLTVNSVNSTDNNIIITPTPTPNITTTTTNPTVLESITSKYTSLFGNTEYDFKWIIIIVLVQTPFLFARYLLFTMAGFSVVTKLKRDLFKSLLTQEVSYFDSNRTGDLKAVIASDSSILQNCITVSLSTLVRCSLQLIGGLLILVFLSWKVTLLMISFLVILLISFLVFKKWIHPKYNYIQEKLVNIGLIIDDSIGNIKEIRLLNAESKELRSFETELEILHRSSRSFVLMNAFWISFGSLLVMGTIIGIYGFAMSQTLSNSILLLQFILYSLMITASMNGLIGSINEIQKLISSSKRIFSLIDRKPIVHFQGGITPSTDSNISFDNVYFNNNNNNSNNNNNNNNNNKNNNGMILSNVSFIVNKGQWLSLVGPSQSKEFIFSLIQGLYYPTRGTVFIGRIDTKVLDLYFFRSRLFTISPLQTVIFDGTVEQNIRYGLSHLSTQNIIDASKKANLHDFVIGLPHGYDSMIGKNNFFDPIQILKISIARAFLRNPSVLLLDETTLPFDSKEIEDSIELLVQNKTVIAIANKLSTLKRSNNILVFDDNRIIERGTHSELSQKSTSFYVTSVLNSINNKYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNKIEIYLFLI
Protein: Uncharacterized protein (Q38BZ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKPFPAFLTLFLVALSPLTTPSQSAGDDVQHNLFSWSSADNMTDGDVGSARVPEEEEKERTSVSNESKDAQCKGKYGLYSHYVLGHNHCSWEPPYGVAMSPLYLPPDISADADRCSFMWLLREMLFTASKEGIALVPHNVKRGDSTPLQCGRVALHPWIVVRGEPKEWGPIRGVSTHKVMVSSDPSDGTDMLWPLLLLVSLGVLAAFLLLILVFMMKTIRGGTLLEERTTSMTAASPDENDKKLHDNGSVTECRSVREGKGNEEDKEGGREGEKEEQIEKNEIGEEVVEAETASEGHTSEITALHSLSGSWHSEGSDQLLTSNDSPLPQPPIELVASPLETPKEGDVKAPHGHL
Protein: Small ribosomal subunit protein uS17x (40S ribosomal protein S11-3) (P42733)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein uS10y
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL8z
Sequence:
MAEQTEKAFLKQPKVFLSSKISGKGKRPGKGGNRFWKNIGLGFKTPREAIDGAYIDSKCPFTGTVSIRGRILAGTCHSAKMQRTIIVRRNYLHFVKKYQRYEKRHSNIPAHVSPCFRVKEGDHVIIGQCRPLSKTVRFNVLKVIPAGASAFGKKAFTGV