wanglab/gogpt-training-data huggingface dataset:
Protein: Envelope glycoprotein H (gH) (P27599)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04033}.
Interaction partners:
Sequence:
MRRPLCAALLAAAVLALAAGAPAAARGGAGGRSREHRDARYEIEEWEMVVGAGPAVHTFTIRCLGPRGIERVAHIANLSRLLDGYIAVHVDVARTSGLRDTMFFLPRAAVDNASAADIPDTPAVQSHPGLFGAAFSWSYLQTRHLVDYDLVPSRPLQDWYFSQARAESNAARPPPAPRVTPTPAGRVAAFDINDVLASGPEHFFVPVRADRKRRERHVADFAAVWPVSYIPAGRAVLSCERAAARLAVGLGFLSVSVTSRDLLPLEFMVAPADANVRMITAFNGGGAFPPPGPAAGPQRRAYVIGYGNSRLDSHMYLTMREVASYANEPADFRAHLTAAHREAFLMLREAAAARRGPSAGPAPNAAYHAYRVAARLGLALSALTEGALADGYVLAEELVDLDYHLKLLSRVLLGAGLGCAANGRVRARTIAQLAVPRELRPDAFIPEPAGAALESVVARGRKLRAVYAFSGPDAPLAARLLAHGVVSDLYDAFLRGELTWGPPMRHALFFAVAASAFPADAQALELARDVTRKCTAMCTAGHATAAALDLEEVYAHVGGGAGGDAGFELLDAFSPCMASFRLDLLEEAHVLDVLSAVPARAALDAWLEAQPAAAAPNLSAAALGMLGRGGLFGPAHAAALAPELFAAPCGGWGAGAAVAIVPVAPNASYVITRAHPRRGLTYTLQGIDVANPLLVTFVRGTSCVSASGAVEARRLAVPGPLDACAYCGSVFVRYLPSGAVMDIVLIADKRTEVEFSRGANSSMPVFNPRLHSGRSRAMLLFPNGTVVSVLAFAGHEAPTFSPAYVWASVGGALVAGTTIYAIAKMLCSSVPLARGYSSVPVF
Protein: Meiotic driver SPOK2 (Spore killer 2) (B2AFA8)
Organism: Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system, leading to poisoning of progeny that do not inherit the allele.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24830502}. Nucleus {ECO:0000269|PubMed:24830502}.
Interaction partners:
Sequence:
MSDKDRIAQLLRELEEAKAREEEAKARAEEAKARAEEAKARAEEAKAREEEAKAREAQERCERERLQLEHRNTTFLEYLHNCHRHLYNALRLTNTSRYSTGYTKVVGKYYPKRLRPWTYFANVLHPHYFDLVQSICGQRQLFEPANTTKSLGTIISDHLAGNEKAIDRFEVDAVERPVQGILKVLATHKEAGKASICPEFRFSANLRELTQKDDGSSGADDNTSDGSLERRQQAGPNKRPTSKRKYICSNRQPDGVGIRMQPGGGQTHAFIYDYKAAHKVAIEYIRSATAKEHLFHEVVARINDDKLSRDEEVQRREQAEALIAMALTQVFDYMITYGVSYGYVAAGRCLLLLYVDRDDWQTLYCHPCLPADDVGEPTNDWTDRLSHTAVAQLISFCLSSFQSEALEGQSLETALSIAKATLKTWSESYADVAYLGLEPAELSSAPSSQNTDISEYTSKAEPTGRNVALRSQSSCKPAAVLPQSNEHDDEEDHSEPGASRLRLAANKRKRGPSSGGEDGDIAMADSGPTKQYCTQACLLGLKRGKDLDEKCPNVSLHRFDGSSRHPVNAHRFTDMVEQQLLLSPYKGCRMVDFWGKRGAMGWLFKLELLPYGYTFVGKGTLEDRLSRLEHEGRVYAQLDHLQGDVVPVYLGLVRLDRGYILPGLEFVVHMMLMSWAGQTPSASMDDAETLKRESLTAIWNEGVVHGDENRANYLWNAERGRIMIIDFDRAHLSPPPKPRAVSRLSKPKRKRGDSEADAQLFGPLEINRSKHRIRT
Protein: Meiotic expression up-regulated protein 15 (Q96WS6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MEETLPSYEAASGAANLQEVKPQVLPLEEIKKIYKISYWWLCSIALIQTWWVLLGLLPIFFALEHYEVPYKWIFIIEMLYYELYLTLYVCWCYKLRSDFWNEAAKNRPNEERLSALGGWDFLRIPKKRVLVLRDAQSEKKQNNADASNLV
Protein: Protein UPS2, mitochondrial (Altered inheritance rate of mitochondrion protein 30) (Genetic interactor of prohibitins protein 1) (Unprocessed MGM1 protein 2) (P35200)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for mitochondrial cristae morphogenesis and MGM1-processing. Controls the stability of mitochondrial phosphatidylethanolamine (PE). With UPS1, controls the level of cardiolipin in mitochondria. Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Mitochondrion intermembrane space. Note=Lacks the two major intermembrane space-targeting signals, bipartite presequences and cysteine motifs, and import is mediated by another IMS protein, MDM35.
Interaction partners:
- Mitochondrial distribution and morphology protein 35
- Protein UPS1, mitochondrial
- Mitochondrial distribution and morphology protein 31
- Cardiolipin synthase
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidate cytidylyltransferase, mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Phosphatidylglycerophosphatase GEP4, mitochondrial
- Prohibitin-1
Sequence:
MKLFQNSYDFNYPWDQVTAANWKKYPNEISTHVIAVDVLRRELKDQGKVLVTERLITVKQGVPKWIMMMLGGTNMSHVREVSVVDLNKKSLTMRSCNLTMCNLLKVYETVTYSPHPDDSANKTLFQQEAQITAYGSIRKLCNKMEDWSVQRFCENAKKGKMGFDAVLQVFSENWEKHVDDLSNQLVSKVNETMEDVKISAGTLLKGTERSGRTILQQNIDLFRDAYNHEN
Protein: SUMO protease (A0A1D8PSK4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SUMO family protein
- Polynucleotide 5'-hydroxyl-kinase GRC3
- SUMO-conjugating enzyme UBC9
- Ubiquitin-activating enzyme E1-like
- SUMO ligase
- SUMO protease
- Importin subunit alpha
- TOG domain-containing protein
- SUMO ligase
- GTPase-activating protein
Sequence:
MIQSTNNPLISTQRIEINDEYEPENNSECSHKPTDSNIFRLFYNILKYLKVYILSTLFRRIEPSNRHLQSEENKEEDDEYINLSSEASSDIEIIAVNYKPTNDFHLINKTTRIQDNSILIDDTEETPFNIANNDSTTDLLRQLAKDRLKNRKTVTTQYGTDLTISKPIKYSSSRYQQWPVTQAETTTSTPEENFDHQPTLLDIEPITNKYQESILNYYVPTKPLSINSYSVIDNVISNFYIDKISSIYHKSHETLQQLITKERIDSQSKIKTLPSEQLNQVLKIWSTNSRQLIIENYSIEIYTHDLHTLKDSNWLNDNIIDYYFNLIMKANPNVFGWTTHFYTTLVQRGYQGVARWAKRKKINVFTMEKILTPINIGNMHWALAVIDNIKKTITYYDSLGGTHNSGNPQAVQTLAHYMTEEAKRLGVMGNEYKLIPHMEAPQQKNGSDCGVFTCTAARYISANKPLSYSQNDMKIIRRRMVYEILDNRLLD
Protein: Beta-lactamase inhibitory protein (BLIP) (P35804)
Organism: Streptomyces clavuligerus
Function: Inhibits a wide variety of beta lactamases.
Subcellular location: Secreted {ECO:0000269|PubMed:2203736}.
Interaction partners:
Sequence:
MRTVGIGAGVRRLGRAVVMAAAVGGLVLGSAGASNAAGVMTGAKFTQIQFGMTRQQVLDIAGAENCETGGSFGDSIHCRGHAAGDYYAYATFGFTSAAADAKVDSKSQEKLLAPSAPTLTLAKFNQVTVGMTRAQVLATVGQGSCTTWSEYYPAYPSTAGVTLSLSCFDVDGYSSTGFYRGSAHLWFTDGVLQGKRQWDLV
Protein: Chitin deacetylase 1 (EC 3.5.1.41) (J9VPD7)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate. Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis. Plays a major role in synthesizing cell wall chitosan during host infection; chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:30459196}. Cell membrane {ECO:0000269|PubMed:30459196}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
Sequence:
MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAPKLDTGFITLEHDIYQQSVDLAVGYILPQVLANGTYQLKSIINCLGKDTSEAYIETSSNQTTTQITAATGSQSTFFQPIVGTATGAEVSAPSEATGSTAAGSAASTTSGSGASASTGAASNTSSSGSGRSATMGGALIALAAVAVGMVYVA
Protein: Pseudouridylate synthase RPUSD4, mitochondrial (EC 5.4.99.-) (RNA pseudouridylate synthase domain-containing protein 4) (Q96CM3)
Organism: Homo sapiens (Human)
Function: Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of different mitochondrial RNA substrates. Acts on position 1397 in 16S mitochondrial ribosomal RNA (16S mt-rRNA). This modification is required for the assembly of 16S mt-rRNA into a functional mitochondrial ribosome. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA, controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation. Acts on position 39 in mitochondrial tRNA(Phe). Also catalyzes pseudouridylation of mRNAs in nucleus: acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions. Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:23435261, ECO:0000269|PubMed:27974379, ECO:0000269|PubMed:28082677}. Nucleus {ECO:0000269|PubMed:23435261}. Cytoplasm {ECO:0000269|PubMed:23435261}. Note=Mainly localizes to mitochondrion (PubMed:23435261, PubMed:27974379, PubMed:28082677). Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly (PubMed:27974379, PubMed:28082677). Also found in nucleus and cytoplasm (PubMed:23435261). {ECO:0000269|PubMed:23435261, ECO:0000269|PubMed:27974379, ECO:0000269|PubMed:28082677}.
Interaction partners:
- Neugrin
- FAST kinase domain-containing protein 2
- Pseudouridylate synthase TRUB2, mitochondrial
- rRNA methyltransferase 3, mitochondrial
- Probable ATP-dependent RNA helicase DDX28
- Mitochondrial assembly of ribosomal large subunit protein 1
- RCC1-like G exchanging factor-like protein
- Pseudouridylate synthase PUS7L
- Pseudouridylate synthase 7 homolog
- Pentatricopeptide repeat-containing protein 1
Sequence:
MAAPRWSASGPWIRGNGQGCGSLFTLVSKPFCAAAAASTAINAQRLAEKLRAQKREQDTKKEPVSTNAVQRRVQEIVRFTRQLQRVHPNVLAKALTRGILHQDKNLVVINKPYGLPVHGGPGVQLCITDVLPILAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKYWAITVHVPMPSAGVVDIPIVEKEAQGQQQHHKMTLSPSYRMDDGKMVKVRRSRNAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLSFGLDCPILGDHKYSDWNRLAPQKLSVGTLKKLGLEQSKARYIPLHLHARQLILPALGSGKEELNLVCKLPRFFVHSLHRLRLEMPNEDQNENNEAKCLGAQ
Protein: Large ribosomal subunit protein bL32c (50S ribosomal protein L32, chloroplastic) (P0C453)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS11c
- Large ribosomal subunit protein bL20c
- Large ribosomal subunit protein uL22c
- Large ribosomal subunit protein uL22c
- Large ribosomal subunit protein bL33c
- Large ribosomal subunit protein uL22c
- Small ribosomal subunit protein bS16c
- Small ribosomal subunit protein uS8c
- Uncharacterized protein
- DNA-directed RNA polymerase subunit alpha
Sequence:
MAVPKKRTSMSKKRIRKNLWKKKTYFSIVQSYSLAKSRSFSGVSEHPKPKGFSRQQTNK
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q54RL3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNFKLIIILLILLVGFLSVEAKIEFSNINDNDNDDDGSIVETNNGYVQGLINEQYKSFFGIPFAKPPTVENGLRWKSPMVAESWSPKILNASFNQMVGCIQKCELPPMNCPNIISEDCLYLNVYTPLQVSQTQLKPVMAYIPGGRFEQGTASSILYTPELMINSSDIVVVTLNYRLGVSGFLVGDEITGNFGFQDQRLALTWIQENIKFFGGDPNKVTLCGQSAGASSIATHMTAKNSYSLFQGAIIQSNPFTLGLKTLETAKKYSDNFAKAVNCSLKDEDCLNALTIDQIVQGQIKSQAKLDVFEPLQSFLPWTPTIGIDDITDQPLNLILKGDFYDVPTIVGTVSEEALLFIYQASPKNVSETDYKLAIDLIFLDKENVIEINYPPFTNGSDNRPVLSTLGTNFIFACSTRLAIESMLKFKQSPIYLYQFSHVMSFNPWGPNYPYCNHHCCHGSELVFEFDAARYGGYNFTQDEQQLSYEMNNYWTNFINNADPNQGLSVPIEWPKYDITNLESLQLDIPVSITTDLLGSQCNILDNVGYSPR
Protein: Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Choriogonadotropin alpha chain) (Chorionic gonadotrophin subunit alpha) (CG-alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha chain) (Q9BEH3)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:10612425}.
Interaction partners:
- Follitropin subunit beta
Sequence:
MDYYRKYAAVILVTLSVFLHILHSFPDGEFTMQDCPECKPRENKFFSKPGAPIYQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSLTRVMVMGNVRVENHTQCHCSTCYYHKF
Protein: Protein transport protein SEC13 homolog B (SEC13-like protein B) (O64740)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for protein transport from the endoplasmic reticulum to the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000305|PubMed:24280388}. Endoplasmic reticulum {ECO:0000269|PubMed:21189294, ECO:0000305|PubMed:24280388}. Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP107
- Protein transport protein SEC31 homolog A
- Protein SEH1
- Protein transport protein SEC31 homolog B
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP85
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP96
- Nuclear pore complex protein NUP155
- Protein transport protein SEC23 D
Sequence:
MPGQKIETGHEDIVHDVQMDYYGKRIATASSDCTIKITGVSNNGGSQQLATLTGHRGPVWEVAWAHPKYGSILASCSYDGQVILWKEGNQNQWTQDHVFTDHKSSVNSIAWAPHDIGLSLACGSSDGNISVFTARADGGWDTSRIDQAHPVGVTSVSWAPATAPGALVSSGLLDPVYKLASGGCDNTVKVWKLANGSWKMDCFPALQKHTDWVRDVAWAPNLGLPKSTIASGSQDGKVIIWTVGKEGEQWEGKVLKDFMTPVWRVSWSLTGNLLAVSDGNNNVTVWKEAVDGEWEQVTAVEP
Protein: Cathelicidin-derived antimicrobial peptide 2 isoform B (Q08G23)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MKMKALVRSLLLLAVANLLVRGQTQTETRYEDIITAASNQLLPVEEQAFHPLLNQLEVETLNTEDVDQSEVSVRLSFPLQETLCSKAQGQQGQPCPLKKNGKRMMCSMEVRHPILEIGNTLNTDRSDISCEYMEAEVQKIRTRRGKDSGGPKMGRKYSKGGWRGRPGSGSRPGFGSSIAGASGVNHVGTLTA
Protein: Deneddylase 1, isoform A (RE42624p) (Q7JUX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSNSKADPISLTFHDSCLRMSDVQLLHGPHWLNDQILSFYYEYLAHMKYKTNADLHFIAPEITQCMKYMGDQELKQLLDQSNTTGKPFIFFALNDNETTDAGGSHWSLLVFSRPEKTFYHFDSYGNNNTGNSLELMNKIKDLLGVRMAKFRPMRCLQQANGYDCGIHVICMTDHIADYLNRYEVIDGLPSLHIDTVKAKRTELLKLILSLGGKG
Protein: Neuroserpin (Peptidase inhibitor 12) (PI-12) (Serine protease inhibitor 17) (Serpin I1) (Q9JLD2)
Organism: Rattus norvegicus (Rat)
Function: Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator.
Subcellular location: Secreted {ECO:0000269|PubMed:10642518}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q99574}. Perikaryon {ECO:0000250|UniProtKB:Q99574}.
Interaction partners:
- Tissue-type plasminogen activator
- Plasminogen
Sequence:
MAYLGLLSLVALQSLVTGAAFPDETIAEWSVNVYNHLRATGEDENILFSPLSIALAMGVMELGAQGSTLKEIRHSMGYESLKSGEEFSFLRDFSSMVSAEEGQYVMKIANSLFVQNGFHINEEFLQMMKMYFNAEVNHVDFSENVAVANYINKWVENYTNSLLKDLVSPGDFDAVTHLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLATLEPLLKPQLIEEWANSVKKQKVEVYLPRFTVEQEIDLKDILKALGVTEIFIKDANLTAMSDKKELFLSKAVHKSFIEVNEEGSEAAVASGMIAISRMAVLFPQVIVDHPFLFLIKNRKTGTILFMGRVMHPETMNTSGHDFEEL
Protein: AT4g28240/F26K10_120 (Putative wound-induced protein) (Wound-responsive family protein) (Q94A22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Sec14p-like phosphatidylinositol transfer family protein
- Decapping 5-like protein
- UTP:RNA uridylyltransferase 1
- Proline-rich protein 4
Sequence:
MSYLNKVWMAASFVAVQGNADHGVKLKSGLTSAHRLQRRLSSDLRPLAAADLTGDSLPSEERRRTSSSTPDESLRQVMYLNCWAQG
Protein: Trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) (Trans-3-hydroxy-L-proline dehydratase) (Q9CXA2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline to delta-1-pyrroline-2-carboxylate (Pyr2C).
Interaction partners:
- D-amino-acid oxidase
- Ketimine reductase mu-crystallin
Sequence:
MEAALAVTRLPPNDPRTPALSVVDMHTGGEPLRIVHAGCPEVAGPTLLAKRRYMRQHLDYIRRRLVFEPRGHRDMYGAILVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPKGAREAQVNIHCPCGLVTAFVECEGGRSCGPVRFHSVPAFVLASDLTVDVPGHGKVLVDIAYGGAFYAFVSAEKLGLDVCSAKTRDLVDAASALTGAVKAQFKINHPESEDLGFLYGSILTDGKDAYSEEATTNICVFADEQVDRSPTGSGVTARIALQYHKGLLQLNQTRAFKSSATGSVFTGCAVREAKCGDFKAVIVEVAGQAHYTGTANLTVEDGDPLRDGFLLK
Protein: dTMP kinase (EC 2.7.4.9) (Q57YW2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Ribonucleoside-diphosphate reductase
- thymidine kinase
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
Sequence:
MVAVNRKIVVFTDVEDKQVLEVIREVAGDAETIQLEKSFAYEFMWRGKHTPYRVGTPMCFITEKTVEDADVVFAVYSKRVPVLSLTTGGETTNLLQTISSLGIECKQNTSETWADAVRAFLPNNDSESAVIVFGGGDGAGKATQTEYMRKRLDKEGKAHASLDFPSDKHRYGKLIRKVLSGERGALHGLDPKLFSLLFSLNRFDTLPELRYWLTHGKKILLDRYYTSNFGHQASKLEESERSDFIRHLEQLELEWLKLPPPDVALYLDLPPAAALVAMQRDEKRESLDIHETAGLSYKENVRQTYVWCCQNQRNWVQIECCNDEGERYSREKVHEMIYNAVAKHI
Protein: phenylalanine--tRNA ligase (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (C6KSN5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- phenylalanine--tRNA ligase
- Phenylalanine--tRNA ligase
Sequence:
MLLPKTILSNEGRILCNTINHPLRTVKNKIENFFKFENIDNLKSEICIKQNFDDLNVPLTHPVRNIRDTFYLNENYIKNYNSILSTYYIPFDILNTFYKYYLSNKLLSHDKIILKRTHMTSHLNDLLKGSYTNVIYTGQVYRKDEIDKYHYPIFHQTDGFLIKPEMFNVEIELKQKLEQLIYYLFNKNNIEIKWESDTSFPFTHPSYELYIKRKQDNKWIEILGCGKIKNEVLAMSLYHNHINKIIENEITIYNKTLLNSFQQKFLSNEKETIRQSHLINHLCNKQLNHNIQIKINELLKSINYQGWAFGIGLERLCMLLYDINDIRLFWSNDKRFINQFKENQITTFRPFSNFPCIQKDISFYIKQYFNETSFFQICRDIANDNIEQIQKIDKYYDPKNNQTSLCYRITYRSHNKNLTHNEVNGIQNKIVQILMDQFEVSIR
Protein: RNA polymerase II transcriptional coactivator KIWI (O65154)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. Binds single-stranded DNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RNA polymerase II transcriptional coactivator KELP
- Transcription factor IND
- Regulatory protein NPR6
- Zinc finger protein JAGGED
- Symplekin
- Phosphatidylinositol 3-and 4-kinase family protein
- HEAT repeat-containing protein
Sequence:
MSSRGKRKDEDVRASDDESETHAPAKKVAKPADDSDQSDDIVVCNISKNRRVSVRNWNGKIWIDIREFYVKDGKTLPGKKGISLSVDQWNTLRNHAEDIEKALSDLS
Protein: Protocadherin 7 (A0A0A6YY83)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Gap junction alpha-1 protein
Sequence:
MLRMRTTGWARGWCLGCCLLLPLCFSLAAAKQLLRYRLAEEGPADVRIGNVASDLGIVTGSGEVTFSLESGSEYLKIDNLTGELSTSERRIDREKLPQCQMIFDENECFLDFEVSVIGPSQSWVDLFEGRVIVLDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELLQEPGGGGGSGEGRRLGPADSAPYPGGGGNSASGGGSGGSKRRLDAPEGGGGTSPSGRSSVFELQVADTPDGEKQPQLIVKGALDREQRDSYELTLRVRDGGDPPRSSQAILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRATDLDVGVNGQIEYVFGAATESVRRLLRLDETSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPSIEIRKIGRIPLKDGVANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDTEGDQNKKKYFLHTSAPLDYETTREFNVVIVAVDSGSPSLSSNNSLVVKVGDTNDNPPVFGQSVVEVYFPENNIPGERVATVLATDADSGKNAEIAYSLDSSVMGTFAIDPDSGDILVNTVLDREQTDRYEFKVNAKDKGIPVLQGSTTVIVQVADKNDNDPKFMQDVFTFYVKENLQPNSPVGMVTVMDADKGRNAEMSLYIEENSNIFSIENDTGTIYSTMSFDREHQTTYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPTVTLPRNISYTLLPPSSNVRTVVATVLATDSDDGINADLNYSIVGGNPFKLFEIDSTSGVVSLVGKLTQKHYGLHRLVVQVNDSGQPSQSTTTLVHVFVNESVSNATVIDSQIVRSLHTPLTQDIAGDPSYEISKQRLSIVIGVVAGIMTVILIILIVMMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQPFRRVTFSVVSQPQDPHQGSLQSCYDSGLEESETPSSKSSSGPRLGALPLPEDNYERTTPDGSVGEAEHMENDSRPLPDVALTGKCTRECDEYGHSDSCWMPVRTSPERKKSQPKLSTFMPVDERGSQEKLANGEAAIMGDRNRNLLNKKLTSSYETFSAASFSKNEEANPEDIPLTKTGEYKPSPVNTLTRREVYL
Protein: Phospholipase D1 (PLD 1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1) (Q09706)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for meiosis and spore formation. Seems to be involved in the coordinate induction of late meiotic events.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative phosphatidate cytidylyltransferase
- Phosphatidylserine decarboxylase proenzyme 3
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
- Phosphatidylserine decarboxylase proenzyme 2, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Probable diacylglycerol pyrophosphate phosphatase 1
- Nuclear elongation and deformation protein 1
- Uncharacterized acyltransferase C1851.02
- Lysophospholipid acyltransferase
- CTP-dependent diacylglycerol kinase 1
Sequence:
MTIHQGGNSVIDNVPYSLNTNVNDSIYSEKGTGRKDAEDHTPSKITDLEKNVDHSIPSFPENDPKNYSEFVNLNPPKRPDLEHTRGSSWHTASENVNDLAANDSTRVQTPEFITQTMEDENVEVPPLERDERDAAAAHTSKANRNSARQMWAQLMASVRKFKREDEKPILKENLPAINLFEAGIPASLPIAKHFIRDKSGQPVLPIITDLIKVSVLDVEPKHNRIHSTFTIQVEYGTGPHAIRWLIYRQLRDFINLHSHFLFFEFQHRFSGRRMKLPKFPKEVLPYLVKLRGYQKILYSNPSDQLIDETHSISDISWESHSQDGDRTTGQPRHANNGRKKHGNFWTIQGNTLGVYLQEMIHNLQFFPEVNVLYSFLEFSSLGLYLAGAGTFHGKEGFATLKRNYSPTQYMLCCNTTMMKTRSQPFWIIVSESCIILCDNMLSMQPADVFIWDVDFEITRKNFRKAHSKDTNEKIRLSHHSFKIKNRQKVMKLSVRSGRWLQQFINSVQVAQGLTAWCEIHRFDSFAPVRTNVAVQWMVDARDHMWNVSRAIKNAKRCIMIHGWWLSPELQMRRPYSMAHKWRIDRILNEKAHEGVMVYIMIYRNIDATIPIDSFHTKEHLQSLHPNIYVIRSPSHFRQNALFWAHHEKLVVVDDAITFIGGIDLCFGRYDTPQHILYDDKPVADKTGLCEQTWRGKDYSNARVHDFFDLTEPYKDMYDRLAVPRMGWHDVSMCIIGQPARDAARHFVQRWNYLIQCKKPARKTPLLIPPPDFTTDQLTDSQLTGTCEVQVLRSAGLWSLGLVDTVEQSIQNAYVTCIEKSEHFIYIENQFFVTSTTCEGTTIENRVGDALVERIIRAHKNNEKWRGVIMIPLLPGFEGQIDLQEGGSLRLIVECQYRSICHGEHSIFGRLNAKGIDGSKYLRFYGLRGWAHLGENHELVTEMIYVHAKILIADDRVAVIGSANINERSLLGNRDSEIAAVIRDTLTIDSKMDGKPYKVGKFAHTLRKRLMREHLGLETDVLEQREYNMDGLDRDTEWKRVEVWTPDEGNAINGSAYTAEELKMKYRSQSQFTTTPDILRKAEKSMKKLDQRVSLIPSSIEFNIKTQKDKVEFEKNYEKSKKGPDVIANALVGGIPLSLKTKEDSLYELSKFSQCGEDQRPMVLKDPDHLVPEPSRPHCGNGLVFYDDIPLLEVNPISGETIPKFDASSFEDPVCDEFFEDIWSKVASNNTTIYRHIFRCVPDDEMLTWESYNEWKKYGKRFKEEQARWRQEELSNLHETHEKSENDPKNPKAGSQGSGNTSASEDSKTEKPKTRTNNGLQVPDKRVVYDLLRGIRGQLVELPLKWMSTESNARNWLSSIDKIPPLEIYD