wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane O-methyltransferase homolog (mTOMT) (EC 2.1.1.6) (Catechol O-methyltransferase 2) (A1Y9I9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Required for auditory function. Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18953341, ECO:0000269|PubMed:28504928}. Endoplasmic reticulum {ECO:0000269|PubMed:28504928}. Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia. Present but not restricted to the apical cistern, Hensen's body and the subsurface cistern. {ECO:0000269|PubMed:28504928}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Aromatic-L-amino-acid decarboxylase
- Dopamine beta-hydroxylase
- Cytochrome P450 1B1
- Phenylethanolamine N-methyltransferase
- Cytochrome P450 1A1
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member B3
- Aldehyde dehydrogenase family 3 member B2
Sequence:
MSPAIALAFLPLVVTLLVRYRHHFRLLVRTVLLRGFRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSCCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGSRLLTVERDSRTAAVAEKVIRLAGFDEQMVELIAGSSEEVIPRLRAQHQLNRADLVLLAHRPRYYLRDLQLLEAHALLPHGATVLADHVLFPGAPRFLQYTKSCGRYRCRLHHTSLPDFPAIKDGIAQLTYTGPG
Protein: Zinc finger protein 385A (Hematopoietic zinc finger protein) (Retinal zinc finger protein) (Q96PM9)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that affects the localization and the translation of a subset of mRNA. May play a role in adipogenesis through binding to the 3'-UTR of CEBPA mRNA and regulation of its translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may regulate its activity-dependent translation. With ELAVL1, binds the 3'-UTR of p53/TP53 mRNAs to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind CCNB1 mRNA. Alternatively, may also regulate p53/TP53 activity through direct protein-protein interaction. Interacts with p53/TP53 and promotes cell-cycle arrest over apoptosis enhancing preferentially the DNA binding and transactivation of p53/TP53 on cell-cycle arrest target genes over proapoptotic target genes. May also regulate the ubiquitination and stability of CDKN1A promoting DNA damage-induced cell cycle arrest. Also plays a role in megakaryocytes differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15527981}. Nucleus, nucleolus {ECO:0000269|PubMed:15527981}. Cell projection, dendrite {ECO:0000250}. Note=Detected in dendrites of Purkinje cells and hippocampal neurons. {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Endoplasmic reticulum resident protein 44
- 14-3-3 protein sigma
Sequence:
MILGSLSRAGPLPLLRQPPIMQPPLDLKQILPFPLEPAPTLGLFSNYSTMDPVQKAVLSHTFGGPLLKTKRPVISCNICQIRFNSQSQAEAHYKGNRHARRVKGIEAAKTRGREPGVREPGDPAPPGSTPTNGDGVAPRPVSMENGLGPAPGSPEKQPGSPSPPSIPETGQGVTKGEGGTPAPASLPGGSKEEEEKAKRLLYCALCKVAVNSLSQLEAHNKGTKHKTILEARSGLGPIKAYPRLGPPTPGEPEAPAQDRTFHCEICNVKVNSEVQLKQHISSRRHRDGVAGKPNPLLSRHKKSRGAGELAGTLTFSKELPKSLAGGLLPSPLAVAAVMAAAAGSPLSLRPAPAAPLLQGPPITHPLLHPAPGPIRTAHGPILFSPY
Protein: Zinc finger protein 783 (Q6ZMS7)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 398
- Zinc finger protein 212
Sequence:
MAEAAPARDPETDKHTEDQSPSTPLPQPAAEKNSYLYSTEITLWTVVAAIQALEKKVDSCLTRLLTLEGRTGTAEKKLADCEKTAVEFGNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNRNFWILRLPPGSKGEAPKVPVTFDDVAVYFSELEWGKLEDWQKELYKHVMRGNYETLVSLDYAISKPDILTRIERGEEPCLDRWGQEKGNEVEVGRPRMMGTGLPPYPEHLTSPLSPAQEELKEGQAPKQQQDSEARVAPAGPEAGGGVAIKTEAQSEDEMTPERLFLGVSRGQTECRIPRGPRNRPGGPSRHQAQGMPRVRAGEPRPPGASGETPRVLSRRRQRAFPCPDCGQSFRLKINLTIHQRTHVEEGRQEAPGRSPTSCGDSQAMLEPGEVVVPGPVIRWLPEEPEGRRSVAGGRALVGRRPAASKMYHCSECLRFFQQRKSLLLHQRLHTGNGQGWPACPYCGKAFRRPSDLFRHQRIHTGERPYQCPQCGRTFNRNHHLAVHMQTHARGQVGPHFPAAPARHGSLPLPWPSRKEEG
Protein: Leucine--tRNA ligase, mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (P11325)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of leucine to tRNA(Leu) in the mitochondrion.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:1990003}.
Interaction partners:
- Lysine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Probable proline--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
- Putative proline--tRNA ligase YHR020W
- Glutamate--tRNA ligase, mitochondrial
Sequence:
MLSRPSSRFLSTKRGPGPAVKKLIAIGEKWKQKTTRGLPKQDTLNSGSKYILCQFPYPSGALHIGHLRVYVISDSLNRFYKQKGYNVIHPMGWDAFGLPAENAAIERSINPAIWTRDNIAKMKQQMQSMLANFDWDREITTCDPEYYKFTQWIFLKLFENGLAYRKEAEINWDPVDMTVLANEQVDAQGRSWRSGAIVEKKQLKQWFLGITKFAPKLKKHLNQLKDWPSNVKQMQKNWIGESVGAELVFKVADPKFENLIVFTTRPETLFAVQYVALALDHPIVQKYCEEMPDLKEFIQKSDQLPNDTKEGFQLPNIKAVNPLTKEEVPIFAAPYVVSSYGSAPSAVMGCPGHDNRDFEFWQTNCPGEHIKTCIAPFFDDASKVTEQERQRIIDTVPFTSTDGVLTKECGEHSGVLTVVARKSIMGMLNSEGLSKSVVRYKIRDWLISRQRYWGTPIPIIHCDNCGPVPVPESDLPVKLPELEGLDTKGNPLSTIDEFVNVACPSCGSPAKRETDTMDTFIDSSWYYFRFLDPKNTSKPFDREIASKNMPVDIYIGGVEHAILHLLYSRFIAKFLGSINAWSDPAGIFEPFKKLVTQGMVQGKTYVDPDSGKFLKPDELTFVNDSPDGNTVIIKSNGKVPVVSYEKMSKSKYNGADPNECILRHGPDATRAHILFQSPIADALNWDESKIVGIERWLQKVLHLTKNILSLEKDLAISKDYKTPTDLNDAEVKFHNDFQRFLKSITESFEVNLSLNTVISDYMKLTNILESALKKGEVRNEMIVQNLQKLVTVIYPAVPSISEEAAEMINSQMEWNQYRWPEVERTTESKFKKFQIVVNGRVKFMYTADKNFLKLGRDAVIETLMNLPEGRMYLMNKKIKKFVMKFNVISFLFHK
Protein: Plant intracellular Ras-group-related LRR protein 4 (Intracellular Ras-group-related LRR protein 4) (OsIRL4) (Q6Z8P4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Interaction partners:
Sequence:
MGAVGVEAGVFDTVDGLVGEVMRLHRSLPARPAVEEVEAAEALAAAADREERARADAVARLRRSPAVPDELLCVAQEMHRALAGFQCREQKRDAARLLELEALHTLFDDLIQRASQCLPSTSTRAAPRIAAPAAATTTTSTAAAGSSSSSAVGNAERHASSGTNGFTASRVAGTSTSTGRVSMDDSYVRKAKAAMWDGGAAATNSHLPRGPVEANSVAVRADGNYGDDNEKLSLIKLASMIEVSAKKGARDLNLQGKLMAQIEWLPDSIGKLTGLVTLDISENRLLALPDAIGKLFSLAKLDIHANRISQLPESIGDLRSLIYLNMRGNQLSSLPSSIGRLLNLEELDVGSNGLSSLPDSIGSLTRLKKLIVETNDLDELPYTIGHCVSLVELQAGYNHLKALPEAVGKLEPLEILSVRYNNLRSLPTTMASLTKLKEVDVSFNELESIPENFCFATSLIKLNVGNNFADLQYLPRSIGNLEMLEELDMSNNQIRVLPDSFGNLKHLRVLRAEENPLQVPPRDIALKGAQAVVQYMSDASKRTTKSEPMKPKKTWVHFCFFSRPNKRKHDRIDNAT
Protein: Portal protein (Gene product 1) (Gp1) (Head-to-tail connector) (P26744)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. Procapsid assembly may initiate with a nucleation complex composed of portal and scaffolding proteins. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Switches upon genome packaging from an asymmetrical conformation in the procapsid (PC-portal) to a symmetrical ring in the mature capsid (MV-portal). This change of conformation may serve as a signal for headful packaging.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MADNENRLESILSRFDADWTASDEARREAKNDLFFSRVSQWDDWLSQYTTLQYRGQFDVVRPVVRKLVSEMRQNPIDVLYRPKDGARPDAADVLMGMYRTDMRHNTAKIAVNIAVREQIEAGVGAWRLVTDYEDQSPTSNNQVIRREPIHSACSHVIWDSNSKLMDKSDARHCTVIHSMSQNGWEDFAEKYDLDADDIPSFQNPNDWVFPWLTQDTIQIAEFYEVVEKKETAFIYQDPVTGEPVSYFKRDIKDVIDDLADSGFIKIAERQIKRRRVYKSIITCTAVLKDKQLIAGEHIPIVPVFGEWGFVEDKEVYEGVVRLTKDGQRLRNMIMSFNADIVARTPKKKPFFWPEQIAGFEHMYDGNDDYPYYLLNRTDENSGDLPTQPLAYYENPEVPQANAYMLEAATSAVKEVATLGVDTEAVNGGQVAFDTVNQLNMRADLETYVFQDNLATAMRRDGEIYQSIVNDIYDVPRNVTITLEDGSEKDVQLMAEVVDLATGEKQVLNDIRGRYECYTDVGPSFQSMKQQNRAEILELLGKTPQGTPEYQLLLLQYFTLLDGKGVEMMRDYANKQLIQMGVKKPETPEEQQWLVEAQQAKQGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAARIAEIFNNMDLSKQSEFREFLKTVASFQQDRSEDARANAELLLKGDEQTHKQRMDIANILQSQRQNQPSGSVAETPQ
Protein: Dipeptidyl-peptidase 7 (DPP7) (EC 3.4.14.-) (MER278904) (C3JAQ3)
Organism: Porphyromonas endodontalis (strain ATCC 35406 / DSM 24491 / JCM 8526 / CCUG 16442 / BCRC 14492 / NCTC 13058 / HG 370) (Bacteroides endodontalis)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most efficiently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), and slowly hydrolyzes Leu-Gln-, Lys-Ala-, Leu-Arg, and Ala-Asn-MCA. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
Interaction partners:
- Polysaccharide biosynthesis protein
- Putative TIGR00341 family protein
- Peptidase, S9A/B/C family, catalytic domain protein
Sequence:
MKLKRILLSVALLCGIGTTAMADKGMWLLNELNQQNYERMKELGFKLSPEQLYSLGQPSVASAVVIFGGGCTGITVSNEGLIFTNHHCGFGAIQSQSTVDHDYLRDGFRSNNHVEELPIPGLSVRYLREIVDVTPRIEAAVKGAKSEMERMQIIEELSQKINAEYTKGSTVVGEVTPYYAGNKYYVVVYNVFQDVRLVMAPPSSVGKFGGDTDNWMWTRHTGDFSVFRVYADANNNPALYSQNNKPYKPISYAPVSLNGYREGDYAMTIGFPGSTNRYLTSWGVEDVVNNENSPRIEVRGIKQAIWKEAMEADQATRIKYASKYAQSSNYWKNSIGMNRGLKNLDVVNRKRAEEKAFEAWIAKNNSQSTYGHILPGLKADYAKSAAISKDINYLYETLWGGTEIVRLARDVNSVGRIQAADMPKYKGRLEELYKDYLPSLDVKVLPAMLDIVRQRVSADCQPDIFKFIDKKFKGSTEKYAQYVFEKSIVPYADKVKDFLNLPADKQKKILDKDPAVALFNSVLPAIMQAQDKSEEMMLNIEKGKREYFAASRIMDPNRQMPSDANFTMRMSYGSIKGYAPKDGAWYNYYTTEQGVFEKQDPTSSEFAVQPEILSLLRSKDFGQYGVGDHLRLCFLSDNDITGGNSGSPVFNGNGELIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWAKMPHLIKELNLVKGDQRDLMPAGKGGNCSHKKAQTCAKKECSKGKKCAEKSATCISAMKDGKPCKTEKACAAGQKSAEKKANCCSTMKDGKPCTGDKDCAKSGKACCGKNKEAAAKKASKK
Protein: Protein artichoke (Q9VPF0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal morphology and function of ciliated sensory organs.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24496014}. Cytoplasm {ECO:0000269|PubMed:24496014}.
Interaction partners:
- FI02011p
Sequence:
MMLLPIFLLLCIGINLIRAESCPPSQAILPCRCSLRGKEIQIWCSHSNLPQIMDGLKAVERNIKGRIDELVLENNQLPALPGRFFGSLQIVRLMLRHNSIERVSNGWLNELENGLVEIFVVEPQLRSIPAESLNGMINMLAITIQSEELKHLPDFSGLLSLTYLSVQTGALQELPSHLFRHLPKLQHIHITGGSGLTRLEAGLFDGLISLKNLDLSHNGLNWIHLRALSRLPNLVSLKLSHNQISDVGMVGRIVKDLEHLKKLRLDNNLITVIEDGSFVDLPNLSELHLNDNRITELQYGAFLRTPQLKTIYLQNNLIRRIHPESLLQASGSGVEAVHMYNNEIGHVEALRALLDALPRLRYLDMSGNLLSELPYGALRGHGTLEQLHLNHNHLRLIERDALMAMPALRELRMRNNSLSSDLPLPFWNLPGLKGLDLAQNQFARVDSQLLAGLPSLRRLDLSENGLIELAPNSFRHNPLLETLNISSNELTKIHSSTLIHLERLFEVDASYNQLKSVIAGLPRIVERISLKGNQITSLPAAASKDLQLPNLRMLDLSQNRIEQLPRHGFQGAMELRVLSLAQNELRQLKDTSFIGIQRLELLHLQENQLGEADERALLPLAELRNLNLQSNKLEAITDNFFSNNSRLEQLDLSRNLIRSISPTAFDTQRSLEYLDLSGNALLDISVGLGNLNNLRDIDLSYNQISRIQSDVIGGWRNVVEIRLSNNLIVELQQGTFRNLPKLQYLDLSSNEIRNVEPGALKGLDELQEFVLADNKLVELKDHVFEELPSLLASHFQYNKLRYISPESFHNANSLVFLNLSNNHFRNMENIGLRSMRNLEVLDLSTNGVKLVSTMPLKALNWLVELKMDNNQICRIQGSPFETMPRLRVLSMRNNQLRSIKERTFRNVRGNIAILDVDGNPIDCNCEMQWLSVWLQETNFPYPGPKCQDGRLLRSARMERSLCVGADIYGNERTDGNQLPLLNEHGDVFQRDLPDDFNDECEAGEGTRLPGDRPLVGESEYFYDQYVDATEAPDTTHSAISTSQRPKPTPTINSNIDLNNTILHTKYFNRKPQPGSGSPFTFFGYPLPSVSLGRFFGFGDRGRKQRTDSNDDMPATHRMAHISLPSGRGKTRMYQPNSAEFEKYLKDQQKQEKLNIARNRYVDTDSTTSSMEDALSNESGSAATTVGVFRTTFREPSSIERGGFRPIVPAHVGGFMPVHDPQQRRGLVEVVNITGNPSEIVQGIGQRKFIPISTQARPKPTKSSGESSETATYEVTETTPDITTTTPLMQRIATSTTKASTTTTRSTTTTSTTQVTPAENNASSSTELDSQYDDEDLEAQSVTLLRPPPLVQTTTAETILLIPPAEEHVAQIKSRSWVTTTTPQSPSDNQVTLAGPTSTVPPPPPASPPLRGGGRSTITKVYTPYQQQVAQPTAEEYQRTTPSGDNEGVASEHQLTANAQKRTELELLQVDRVDRKDGMDWYYESFKKKRDFNGGAAVRKTAHKEVFYDGVAASSSWNRLHKEILFISLLLLWRAC
Protein: Transmembrane 9 superfamily member 4 (Tumor cannibalism associated protein 1) (Q92544)
Organism: Homo sapiens (Human)
Function: Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface. Regulates the assembly and activity of V-ATPase in colon cancer cells via its interaction with V-type proton ATPase subunit H (ATP6V1H) and contributes to V-ATPase-mediated pH alterations in cancer cells which play an important role in drug resistance and invasiveness of colon cancer cells. Plays an important role in an atypical phagocytic activity of metastatic melanoma cells called cannibalism and is involved in the pH regulation of the intracellular vesicles in tumor cells.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000269|PubMed:25999474}. Early endosome {ECO:0000269|PubMed:19893578}.
Interaction partners:
- Protein transport protein Sec24C
- Zinc finger protein PLAGL2
Sequence:
MATAMDWLPWSLLLFSLMCETSAFYVPGVAPINFHQNDPVEIKAVKLTSSRTQLPYEYYSLPFCQPSKITYKAENLGEVLRGDRIVNTPFQVLMNSEKKCEVLCSQSNKPVTLTVEQSRLVAERITEDYYVHLIADNLPVATRLELYSNRDSDDKKKEKDVQFEHGYRLGFTDVNKIYLHNHLSFILYYHREDMEEDQEHTYRVVRFEVIPQSIRLEDLKADEKSSCTLPEGTNSSPQEIDPTKENQLYFTYSVHWEESDIKWASRWDTYLTMSDVQIHWFSIINSVVVVFFLSGILSMIIIRTLRKDIANYNKEDDIEDTMEESGWKLVHGDVFRPPQYPMILSSLLGSGIQLFCMILIVIFVAMLGMLSPSSRGALMTTACFLFMFMGVFGGFSAGRLYRTLKGHRWKKGAFCTATLYPGVVFGICFVLNCFIWGKHSSGAVPFPTMVALLCMWFGISLPLVYLGYYFGFRKQPYDNPVRTNQIPRQIPEQRWYMNRFVGILMAGILPFGAMFIELFFIFSAIWENQFYYLFGFLFLVFIILVVSCSQISIVMVYFQLCAEDYRWWWRNFLVSGGSAFYVLVYAIFYFVNKLDIVEFIPSLLYFGYTALMVLSFWLLTGTIGFYAAYMFVRKIYAAVKID
Protein: Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg) (P04418)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Participates in the repair of UV-damaged DNA by excising pyrimidine dimers that are the major UV-lesions. DNA glycosylase activity hydrolyzes the glycosylic bond of the 5' pyrimidine of the dimer. This leaves apurinic/apyrimidic (AP) sites in the DNA. These AP sites are removed by the AP lyase activity which cleaves the intrapyrimidine phosphodiester bond. Catalysis proceeds via a protonated imine covalent intermediate between the alpha-amino group of the N-terminal threonine residue and the C1' of the deoxyribose sugar of the 5' pyrimidine at the dimer site.
Interaction partners:
Sequence:
MTRINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLKRGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
Protein: NADPH-dependent reductase BacG (EC 1.3.1.-) (Bacilysin biosynthesis oxidoreductase YwfH) (H2HPP reductase) (P39644)
Organism: Bacillus subtilis (strain 168)
Function: Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the 3Z,7R-ex-H2HPP isomer is kinetically disfavored by BacB and produced in a smaller quantity than 3E,7R-ex-H2HPP, it is the preferred substrate for the conjugate reduction reaction of BacG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Transaminase BacF
- H2HPP isomerase
- Prephenate decarboxylase
- Uncharacterized MFS-type transporter YwfA
- Coproheme decarboxylase
- Alanine--anticapsin ligase
- Short-chain dehydrogenase/reductase homolog YusS
- Short-chain dehydrogenase/reductase homolog YusR
- Uncharacterized oxidoreductase DltE
- Putative bacilysin exporter BacE
Sequence:
MSKRTAFVMGASQGIGKAIALKLADQHFSLVINSRNLDNIESVKEDILAKHPEASVIVLAGDMSDQHTRAGIFQKIESQCGRLDVLINNIPGGAPDTFDNCNIEDMTATFTQKTVAYIDAIKRASSLMKQNEFGRIINIVGNLWKEPGANMFTNSMMNAALINASKNISIQLAPHNITVNCLNPGFIATDRYHQFVENVMKKNSISKQKAEEQIASGIPMKRVGSAEETAALAAFLASEEASYITGQQISADGGSMKSI
Protein: Probable lipoprotein LppE (O07750)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Found in membrane and whole cell lysates. {ECO:0000269|PubMed:21920479}.
Interaction partners:
- Putative cytochrome P450 140
- Coenzyme Q-binding protein COQ10 START domain-containing protein
- Probable short-chain type dehydrogenase/reductase
Sequence:
MCNRLVTVTGVAMVVAAGLSACGQAQTVPRKAARLTIDGVTHTTRPATCSQEHSYRTIDIRNHDSTVQAVVLLSGDRVIPQWVKIRNVDGFNGSFWHGGVGNARADRARNTYTVAGSAYGISSKKPNTVVSTDFNILAEC
Protein: Calnexin (D6RGY2)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Melanosome membrane {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004573}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004583}.
Interaction partners:
Sequence:
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
Protein: Panurgine R (PNG-R) (C0HL86)
Organism: Panurgus calcaratus (Solitary bee)
Function: Antimicrobial peptide active against Gram-positive bacteria M.luteus (MIC=0.8 uM) and B.subtilis (MIC=1.5 uM). Less active against Gram-negative bacteria E.coli (MIC=32.5 uM) and yeast C.albicans (MIC=18.7 uM). Not active against S.aureus and P.aeruginosa. Has no hemolytic activity against human erythrocytes. Probably acts by disrupting membranes of target cells.
Subcellular location: Target cell membrane {ECO:0000305|PubMed:23483218}. Secreted {ECO:0000269|PubMed:23483218}.
Interaction partners:
Sequence:
LDVKKIICVACKIRPNPACKKICPK
Protein: Scavenger receptor cysteine-rich type 1 protein CD163c-alpha (Scavenger receptor family member expressed on T cells 1) (Q8CGY7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRTTLWPLSLGSLLTLGAALTGTSSEGDQGNLRLAHRQSTCDGVVLVRHQGEWGHLCNLEWTLAEASVVCRQLGCGPAVGAPKYVPLPGEMVRPWLHNVSCWGNESSLWECSLGAWSQRACPHEWVVVALCANGTFREIRLVKGHSPCAGLPEIMNVNGVDRLCGLHVEEATVFCRELQCGHALQAPRQDVGVSKYMTCKGTESTIRNCRLNNKLRGGCNLLLDAEVICSGHVEARLVGGEHSCAGRLEVLRGLTWGTICHADLDLPTAHVVCRELGCGIAVSTLGGAQFGQGSGPVWLEAFRCVGNESLLFHCPREPGHHCGHEQDAALTCSEFRLVNGSSDCEGRVELQVQGTWAPVCAANWDLADAMVLCHQLNCGNAVSVPPGGHFGDGDDLIWPDIFHCVGTEPHLLHCAASTLGAHGCVLGNTASTICSGLQDILRLRDGQSYCDGRVEISLDGSWGRVLDDAWDLHGASVVCRQLGCGEAQRAYDAPAPIFRRVPVGLSQVRCLGSETRLVHCNVSTSLLVPAGTLRDAGVVCSGSLRVRLAAGPGRCAGRVELFYQGSWGTVCDDAWDLQDAQVVCRQLDCGHALSAPRNAHFGAGTGHIWMDELHCLGNESSLWKCQSGSWGQHDCRHKEDAGVFCSESVALRLRGGTSGCVGWLDVLYNGSWGAVCSNALRDISLSIICRQLGCGDQGWLENRPSSGAGLGISWVDNIKCRNLHNATLWQCPSAPWNPHSCTQEEEVWINCEGTPQIALQDPAQTPNCSSPFGCLENSVLRVLGGEDGCSGRVELWHAGSWGTVCDDSWDLVDAEVVCRQLGCGQALAALGEASFGPGVGPVWLDEVECLGSEVTLEACQAEPWGHGDCTHKEDAGVRCAGVSTTTALSPSLTPPSVAEVWKLSEIACLVLGCLLGIVFLVMIAQWCHIRDASMGAGMLGHLQSEGIYEDIEVDPVPKKEENTVSRLLMLEEGYDDAEEPEDQPTENDE
Protein: CSD domain-containing protein (G5EDV3)
Organism: Caenorhabditis elegans
Interaction partners:
- ATP-dependent RNA helicase cgh-1
- Protein LSM14 homolog car-1
- Polyadenylate-binding protein
- K Homology domain-containing protein
Sequence:
MSTEQANGTTIEEKKDKVAEVTEKLDNLAVDTTNEANDAKQPARRGGFRGRGRGRGRGGHFYQPRPPYEDQMKKLEEDLASKKVIETGVKGHVKWFSVRGRYGFVARDKPTDENEDFFVHQTAITKSSTIKFYLRTLDDDEPVVFDIVEGLKGPEAANVTGPDGENVRGSRFARTLLTHWRTRGRGGARGRGGRGRGAPRQTRDQDGDEKDEKEKSDTIENSGDGETRGKRRTRRHGKLQPDAPSGEKGDGDAAAATTDAAPAAEKKKKRQRKGNKEPTTTTEQKEETAAPAKA
Protein: NADH-dependent L-xylulose reductase (EC 1.1.1.15) (EC 1.1.1.250) (Q70FD1)
Organism: Ambrosiozyma monospora (Yeast) (Endomycopsis monosporus)
Function: NADH-dependent L-xylulose reductase; part of the yeast pathway for L-arabinose catabolism. Reversibly converts L-xylulose to xylitol and D-ribulose to D-arabinitol. It has a much lower activity with D-xylulose. Sugar alcohols can serve as a substrate when the hydroxyl group of C-2 is in the L- and the hydroxyl group of the C-3 is in the D-configuration. Seems also to be specific for sugar alcohols that have not more than 5 carbons since no activity is observed with dulcitol (galactitol), which has the hydroxyl group of C-2 in L- and of C-3 in D-configuration, but is a six-carbon sugar alcohol.
Interaction partners:
Sequence:
MTDYIPTFRFDGHLTIVTGACGGLAEALIKGLLAYGSDIALLDIDQEKTAAKQAEYHKYATEELKLKEVPKMGSYACDISDSDTVHKVFAQVAKDFGKLPLHLVNTAGYCENFPCEDYPAKNAEKMVKVNLLGSLYVSQAFAKPLIKEGIKGASVVLIGSMSGAIVNDPQNQVVYNMSKAGVIHLAKTLACEWAKYNIRVNSLNPGYIYGPLTKNVINGNEELYNRWISGIPQQRMSEPKEYIGAVLYLLSESAASYTTGASLLVDGGFTSW
Protein: Transmembrane protein 88 (Q6PEY1)
Organism: Homo sapiens (Human)
Function: Inhibits the Wnt/beta-catenin signaling pathway. Crucial for heart development and acts downstream of GATA factors in the pre-cardiac mesoderm to specify lineage commitment of cardiomyocyte development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21044957}; Multi-pass membrane protein {ECO:0000269|PubMed:21044957}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MADVPGAQRAVPGDGPEPRDPLDCWACAVLVTAQNLLVAAFNLLLLVLVLGTILLPAVTMLGFGFLCHSQFLRSQAPPCTAHLRDPGFTALLVTGFLLLVPLLVLALASYRRLCLRLRLADCLVPYSRALYRRRRAPQPRQIRASPGSQAVPTSGKVWV
Protein: Glutathione S-transferase domain-containing protein (Q86JB5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Mitofilin
- Translocase of outer mitochondrial membrane
- Uncharacterized protein
- Translocase of outer mitochondrial membrane
- Probable mitochondrial Rho GTPase gemA
- Bacterial surface antigen
- Uncharacterized transmembrane protein DDB_G0283573
- SMP-LTD domain-containing protein
Sequence:
MEKVIEVVKNNKLLVAATVTVSAGILYKTISLNTNKPIFEKDVVYVADFPGINKDLPSYSPFVLKVISILEYCNIRYEINTTGDLGPNPRKTFPYIRYNDEFVYDSYFILEWISQQFKHVTPKMQQSIGSGGGSGEMDQAIDHITKRFIDQAFTYLSAYIRWVVPEYNEKIIPRLLSSIQNPIFRSFAHKAINQVSIQKYKTQVGNFSLDEVVSVFKSDLNSLSNLLGSKTFIFGDHLSMADISLFSTLAQIYYVPVDTPIRSILFENQNLLNYIQNVRSLIFSDAKWELLKQ
Protein: Translation initiation factor IF-3, putative (Q8IJ64)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNTCIDFHKKKKKLLIHPIHLLNYVYNYNRLFCCHLVNLPLYKKRSHLKNEKDNLKRYKNYETHLKCLNYDFLTHTNTFYNIRKKFTTFININERQNHIANIKNNIQSNHKKENNILTNNIINNNNIYMNNSHKIHGLLNKQIAQIKNSTHTHPRSYNFDPCTKTKKIQVYYNCEMNDVIRKINYIKKFLSTGSPVDIFLIYNTHDHIKTRNIKMKKQTKISKNKISNIEDEQQEEPHNHYDRQIFKNYESNKITKFLHTQKLNETKYSLHLYIKINFILNHIRNISIVDEIFRHIQNKNHIILIKAYPK