wanglab/gogpt-training-data huggingface dataset:
Protein: 4'-phosphopantetheinyl transferase AcpT (EC 2.7.8.7) (P37623)
Organism: Escherichia coli (strain K12)
Function: May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis in E.coli. The native apo-protein substrate is unknown. Is able to functionally replace AcpS in vivo but only when expressed at high levels.
Interaction partners:
- Acyl carrier protein phosphodiesterase
- Dephospho-CoA kinase
- Enoyl-[acyl-carrier-protein] reductase FabI
- Enterobactin synthase component F
Sequence:
MYRIVLGKVSTLSAAPLPPGLREQAPQGPRRERWLAGRALLSHTLSPLPEIIYGEQGKPAFAPEMPLWFNLSHSGDDIALLLSDEGEVGCDIEVIRPRANWRWLANAVFSLGEHAEMDAVHPDQQLEMFWRIWTRKEAIVKQRGGSAWQIVSVDSTYHSSLSVSHCQLENLSLAICTPTPFTLTADSVQWIDSVN
Protein: Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (BmPNPO) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase) (Q1PCB0)
Organism: Bombyx mori (Silk moth)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Interaction partners:
- Pyridoxal kinase
- Uncharacterized protein.
- NAD
- Uncharacterized protein.
- Phosphoserine aminotransferase.
Sequence:
MLNNCVVLIRKSVLLSPNLKYIRNMSIDIGGMRIKYKEKDETFLEKHLVSKEPFGQFKSWFEEACARKEILEPNAMCLATVSQEGFPSARFVLCKGYGKEGFKFYTNYGSKKAKDIEGNPNVAATFYWEILNRSVRIEGRVEKLSEDDSTKYFHTRPVVSQIAACASYQSTPIESRDVLCEREKLLEQQYMIPGKEVPKPSYWGGYLLIPRSVEFWQGQRDRLHDRIKFRRPNKGEVSDERLLHEGEDGWVFERLSP
Protein: Secreted frizzled-related protein 4 (sFRP-4) (Frizzled protein, human endometrium) (FrpHE) (Q6FHJ7)
Organism: Homo sapiens (Human)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types (By similarity). SFRP4 plays a role in bone morphogenesis. May also act as a regulator of adult uterine morphology and function. May also increase apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling (By similarity). Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake.
Subcellular location: Secreted {ECO:0000269|PubMed:19480240}. Note=Cytoplasmic in ovarian tumor cells.
Interaction partners:
- Protein Wnt-3a
- Protein Wnt-4
- Protein Wnt-2
- Protein Wnt-7a
- Proto-oncogene Wnt-1
- Proto-oncogene Wnt-3
- Protein Wnt-5b
- Protein Wnt-6
- Protein Wnt-16
- Protein Wnt-5a
Sequence:
MFLSILVALCLWLHLALGVRGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSAVLRFFLCAMYAPICTLEFLHDPIKPCKSVCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDLPEDVKWIDITPDMMVQERPLDVDCKRLSPDRCKCKKVKPTLATYLSKNYSYVIHAKIKAVQRSGCNEVTTVVDVKEIFKSSSPIPRTQVPLITNSSCQCPHILPHQDVLIMCYEWRSRMMLLENCLVEKWRDQLSKRSIQWEERLQEQRRTVQDKKKTAGRTSRSNPPKPKGKPPAPKPASPKKNIKTRSAQKRTNPKRV
Protein: LD06557p (Myb-interacting protein 40) (Q7K159)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Lin-52, isoform A
- LD07342p
- Protein lin-54 homolog
- Chromatin assembly factor 1 p55 subunit
- Transcription factor E2F2
- Myb protein
- RE32990p
- Retinoblastoma family protein
- Transcription factor Dp
- LD05287p
Sequence:
MKTVPKKKETALRLRESRREEQKPETTNLPPDDDAESDLPIRGRPSKKLLIQQQQQRQYQVKLDPKVKTVTSGSSEKPSTSSSAAAAGAGGRIKARRVLYKKSVGAAAVAQKAPGETYVMRLFERSLDLSKYQDKTPLYPICRAWMANQPKNPAVGAFQTDASLTATKREDNGEEILSQIKSGEIKVINQLPQAKSTDLPIIPPRLEFSQEDKKREKALQGASTSDLLSSNMNRWKKVRGHWIKHIKKYEKERYEVIDKIMSLVCKN
Protein: MIP18 family protein YHR122W (P38829)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in chromosome segregation through establishment of sister chromatid cohesion.
Interaction partners:
- DNA repair/transcription protein MET18/MMS19
- Cytosolic iron-sulfur protein assembly protein 1
- Cytosolic Fe-S cluster assembly factor NAR1
- Cytosolic Fe-S cluster assembly factor NBP35
- NADPH-dependent diflavin oxidoreductase 1
- General transcription and DNA repair factor IIH helicase subunit XPD/RAD3
- Cytosolic Fe-S cluster assembly factor CFD1
- Fe-S cluster assembly protein DRE2
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA polymerase delta catalytic subunit
Sequence:
MSEFLNENPDILEENQLPTRKEDSTKDLLLGGFSNEATLERRSLLLKIDHSLKSQVLQDIEVLDKLLSIRIPPELTSDEDSLPAESEDESVAGGGKEEEEPDLIDAQEIYDLIAHISDPEHPLSLGQLSVVNLEDIDVHDSGNQNEMAEVVIKITPTITHCSLATLIGLGIRVRLERSLPPRFRITILLKKGTHDSENQVNKQLNDKERVAAACENEQLLGVVSKMLVTCK
Protein: Zinc chaperone YjiA (EC 3.6.5.-) (GTP-binding protein YjiA) (P24203)
Organism: Escherichia coli (strain K12)
Function: Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them (By similarity). Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis (By similarity).
Interaction partners:
- Uncharacterized protein YjiX
- Pyruvate/proton symporter BtsT
- Hydrogenase maturation factor HypB
- Uncharacterized protein YjiS
- GTPase ArgK
- UPF0259 membrane protein YciC
Sequence:
MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSNELEDALLDLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQFTIAQSQVGYADRILLTKTDVAGEAEKLHERLARINARAPVYTVTHGDIDLGLLFNTNGFMLEENVVSTKPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENLLLESADKLLRYKGMLWIDGEPNRLLFQGVQRLYSADWDRPWGDEKPHSTMVFIGIQLPEEEIRAAFAGLRK
Protein: Pectinesterase inhibitor 11 (Pectin methylesterase inhibitor 11) (AtPMEI11) (Q9STY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pectin methylesterase (PME) inhibitor involved in the maintenance of cell wall integrity in response to necrotrophic pathogens. Modulates PME activity and pectin methylesterification during infection by Botrytis cinerea and contributes to resistance against the pathogen.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:28082716}.
Interaction partners:
- Pectinesterase inhibitor 12
- Pectinesterase inhibitor 5
- Pectinesterase inhibitor 1
- Pectinesterase inhibitor 2
- Probable pectinesterase/pectinesterase inhibitor 17
- Berberine bridge enzyme-like 11
- Plant intracellular Ras-group-related LRR protein 8
- At4g31150
- At2g41380
- Berberine bridge enzyme-like 10
Sequence:
MAKQIFYTLFLFLLSTAILTASSSAPRAAITSKRAINFIQASCKATTYPTVCVNSLTGYANSIQTSPRRLAETALNVTVTQAQSTKVFVWRLGRFTSLKKREIQAVKDCIEEIHDAVDRLTMSIHEVKMCGSAKGRDQFWFHMSNAQTWTSAALTNANTCSDGFAGRVMDGRVKNSVRARILNLGRGTSNALALINAFAKKY
Protein: Neurotensin/neuromedin N [Cleaved into: Large neuromedin N (NmN-125); Neuromedin N (NN) (NmN); Neurotensin (NT); Tail peptide] (P30990)
Organism: Homo sapiens (Human)
Function: Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.
Subcellular location: Secreted. Cytoplasmic vesicle, secretory vesicle. Note=Packaged within secretory vesicles.
Interaction partners:
- Neurotensin receptor type 2
- Neurotensin receptor type 1
- Sortilin
- Neurolysin, mitochondrial
- Protachykinin-1
- Gastrin-releasing peptide
- Kininogen-1
- Somatostatin
- Cholecystokinin
- Promotilin
Sequence:
MMAGMKIQLVCMLLLAFSSWSLCSDSEEEMKALEADFLTNMHTSKISKAHVPSWKMTLLNVCSLVNNLNSPAEETGEVHEEELVARRKLPTALDGFSLEAMLTIYQLHKICHSRAFQHWELIQEDILDTGNDKNGKEEVIKRKIPYILKRQLYENKPRRPYILKRDSYYY
Protein: Protein TolA (A0A140NBY9)
Organism: Escherichia coli (strain B / BL21-DE3)
Interaction partners:
Sequence:
MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGGGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKAKAEADAKAAEEAAKKAAADAKKKAEAEAAKAAAEAQKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADKKAAAEKAAADKKAAAAKAAAEKAAAAKAAAEADDIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAGQIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKP
Protein: Kelch repeat and BTB domain-containing protein 4 (BTB and kelch domain-containing protein 4) (Q9NVX7)
Organism: Homo sapiens (Human)
Interaction partners:
- Cullin-3
Sequence:
MKGGNADSWQREKLASMESPEEPGASMDENYFVNYTFKDRSHSGRVAQGIMKLCLEEELFADVTISVEGREFQLHRLVLSAQSCFFRSMFTSNLKEAHNRVIVLQDVSESVFQLLVDYIYHGTVKLRAEELQEIYEVSDMYQLTSLFEECSRFLARTVQVGNCLQVMWLADRHSDPELYTAAKHCAKTHLAQLQNTEEFLHLPHRLLTDIISDGVPCSQNPTEAIEAWINFNKEEREAFAESLRTSLKEIGENVHIYLIGKESSRTHSLAVSLHCAEDDSISVSGQNSLCHQITAACKHGGDLYVVGGSIPRRMWKCNNATVDWEWCAPLPRDRLQHTLVSVPGKDAIYSLGGKTLQDTLSNAVIYYRVGDNVWTETTQLEVAVSGAAGANLNGIIYLLGGEENDLDFFTKPSRLIQCFDTETDKCHVKPYVLPFAGRMHAAVHKDLVFIVAEGDSLVCYNPLLDSFTRLCLPEAWSSAPSLWKIASCNGSIYVFRDRYKKGDANTYKLDPATSAVTVTRGIKVLLTNLQFVLA
Protein: HORMA domain-containing protein 2 (Q5SQP1)
Organism: Mus musculus (Mouse)
Function: Essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes. Required for the DNA double-strand break-independent, BRCA1-dependent activation of ATR on the sex chromosomes that is essential for normal sex body formation.
Subcellular location: Nucleus. Chromosome. Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the male and female prophase I stage of meiosis. TRIP13 is required for depletion from synapsed chromosomes.
Interaction partners:
- Synaptonemal complex protein 3
- Meiotic recombination protein SPO11
- Meiotic recombination protein REC8 homolog
- Meiotic recombination protein DMC1/LIM15 homolog
- Pachytene checkpoint protein 2 homolog
- Synaptonemal complex protein 2
- Synaptonemal complex protein 1
- Synaptonemal complex central element protein 1
- Telomere repeats-binding bouquet formation protein 1
- Structural maintenance of chromosomes protein 3
Sequence:
MATAQLSHNTRTLKASKNTIFPSQVTNEHESLVVVKKLFATCISCITYLRGLFPESSYRDRRLDDLSLKILREDKKCPGSLHIIKWIQGCFDALEKRYLHMAVLTLYTNPKEPEKVTEIYQFRFKYTKKGTTMDFDSSSTSFESGTDSEDIKKACSLLIRQLYILMQNLGPLPNDVILTMKLHYYNSVTPHDYQPPGFKEAVNSHFLLFEGEPVSLRMGSVSSGFHSMKVKVTTEATRMLDGENSVSQDDGTTEIAHQGLDCDEEEEACGSQVQRMNFVHIEPSFESSRKKKKVSEPVTVFIPNRK
Protein: Ubiquitinyl hydrolase 1 (O45351)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKKDAKDHARNRLMDCYIKKAPTYAAIVKIEHFENDDASSKDFEPFVVYSLNKKKRWEINEESLNSSTEGCLQNDLLNNCIYHSNPVNSAQMATAKKYEKVIGYHIVRIPVNHKKVFDKKCTRDLSYRYRDSIGNVPRDLTVLQYEMKEVEHGKEDFAKENISPEVNNPSKTIGFYNLEEHFVARKQQKSKGWLTVN
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P48833)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000269|PubMed:22842159}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22842159}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida sperm-binding protein 1
- Zona pellucida sperm-binding protein 4
- NOBOX oogenesis homeobox
- Growth/differentiation factor 9
- Factor in the germline alpha
Sequence:
YGLFVCLLLWGGSELCCPQPLWFWQGGTRQPAPSVTPVVVECLEARLVVTVSRDLFGTGKLIQEADLSLGPEGCEPQASTDAVVRFEVGLHECGNSVQVTDDSLVYSSFLLHDPRPAGNLSILRTNRAEVPIECRYPRQGNVSSRAILPTWVPFWTTVLSEERLVFSLRLMEENWSREKMSPTFHLGDTAHLQAEVRTGSHPPLLLFVDRCVATPTRDQSGSPYHTIVDLHGCLVDGLSDGASKFKAPRPKPDVLQFMVAVFHFANDSRHTVYITCHLRVIPAQQAPDRLNKACSFNQSSSSWAPVEGSADICECCGNGDCDLIAGSPMNQNHAARSSLRSRRHVTEEADVTVGPLIFLGKAGDPAGTEGLASAAQATLVLGLRMATIVFLAVAAVVLGLTRGRHAASHPRSASQ
Protein: 6-hydroxynicotinate 3-monooxygenase (6-HNA monooxygenase) (EC 1.14.13.114) (P86491)
Organism: Pseudomonas fluorescens
Function: Flavin-dependent monooxygenase (FMO) that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a step in the aerobic nicotinate degradation pathway. Uses NADH in preference to NADPH as an electron donor.
Interaction partners:
Sequence:
MSQSPRIAVVGAGLGGAAAAKLLLQEGFNVRVYEQAPSFSRLGAGIHVGPNVMKILRRIGIEDALNEQGSHPDYWYSRHWQTGDVLAQIPLGDYAVKEYGASYLTVHRGDFHALLVEALPDSVMAYGKFLTKVEDRGNVVVMHFADGTTEEADIVIGPDGVNSRIREELLGPELPKYAGYLAHRAVFPTPEVKAGMLPFDACVKWWSDDRHMMTYFVTGKADELYYVTGVPVEKWDLNDRWLESSKEEMREAFSGWHPTVQALIDATVEVTKWSLLERDPLPLWSRGRLVLLGDACHPMKPHMAQGAAMAIEDGAMLARCLKEVGAHNHELAFALYEANRAERASKVQRISHDNTWLRTNEDPSWCFGYDVFNVPLVEPKVKAAA
Protein: Casein kinase I (CK1) (DdCK1) (EC 2.7.11.1) (Q556Y4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. May have a role in DNA repair mechanism and support vegetative growth of the cells.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Protein LTV1 homolog
- Bystin
- Serine/threonine-protein kinase rio2
- Pre-rRNA-processing protein TSR1 homolog
- RNA-binding protein NOB1
- Small ribosomal subunit protein uS3
- RNA-binding protein pno1
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
Sequence:
MDLRIGGKYRISRKIGGGSFGEIYLGTNISTNEEVAIKLEPAKAIHPQLLFESKLYKIFQGGIGIPAVKWFGFDGDYNIMVMDLLGPSLEDLFNYCGRKFSLKTVLMLGDQMLRRIEFIHSNNFIHRDIKPDNFLMGIGKRGHVVNLIDFGLAKRYRDPKTHQHIPYREHKNLTGTARYASLNTHQGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAYTKRDKYEKICDKKAQTKIDTLCQGFPSEFATFLNYTRFLKFEDKPDFLYLRKLLREMFVREGYRYDYMFDWVIVRKLREKPPLERPLSNDNKQIQQQIQQQQQAQQQLQQQAQQQQQQTTTTTTTSSSQPSNVKNISTVSNIATTTTDEQFRQLLSTPSYNNVDSDQSPQQTTTTTSSSNPNQTTFYRQNKVVVPQSSSTTTKPPAK
Protein: COP9 signalosome complex subunit 2 (Signalosome subunit 2) (Protein FUSCA 12) (Q8W207)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex-related / CSN complex-like protein
Sequence:
MASDADMEDYGFEYSDEEQEEQDVDIENQYYNSKGMVETEPEEALSGFAEVVQMEPEKADWGFKALKQTVKIYYRLGKYKEMMEAYTEMLTYIKSAVTRNYSEKCINNIMDFVSGSASQNTGLLQEFYQTTLKALEEAKNERLWFKTNLKLCNIWFDIGEYRRMTKILKELHKSCQKEDGTDDQKKGSQLLEVYAIEIQIYTETKDNKKLKQLYHKALAIKSAIPHPRIMGIIRECGGKMHMAERQWEEAATDFFEAFKNYDEAGNQRRIQCLKYLVLANMLMESEVNPFDGQEAKPYKNDPEILAMTNLIAAYQRNEIIEFERILKSNRRTIMDDPFIRNYMEDLLKKVRTQVLLKLIKPYTKIGIPFISKELNVPETDVTELLVSLILDSRIDGHIDEMNRYLLRGDSGNGRKLHKAVDKWNSQLKSLSSNITSRVC
Protein: Adrenodoxin-like protein 2, mitochondrial (Ferredoxin-2) (Q8SZA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for ecdysteroidogenesis in the prothoracic gland which is necessary for larval to pupal transition.
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme IscU
- Cysteine desulfurase, mitochondrial
- LYR motif-containing protein 4 homolog
- NADH dehydrogenase 23 kDa subunit
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 1
- Frataxin homolog, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MLVINSCRAASRLALRSLNLRSPIATRTFSTGLALKTKDVVNITFVRANGDKIKTSGKVGDSLLDVVVNNNVDLDGFGACEGTLTCSTCHLIFKTSDFEKLPDKPGDEELDMLDLAYELTDTSRLGCQITLSKDMEGLEVHVPSTINDARAA
Protein: Small ribosomal subunit protein uS13 (40S ribosomal protein S18) (Ke-3) (Ke3) (P62269)
Organism: Homo sapiens (Human)
Function: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein P1
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS4, X isoform
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS17
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MSLVIPEKFQHILRVLNTNIDGRRKIAFAITAIKGVGRRYAHVVLRKADIDLTKRAGELTEDEVERVITIMQNPRQYKIPDWFLNRQKDVKDGKYSQVLANGLDNKLREDLERLKKIRAHRGLRHFWGLRVRGQHTKTTGRRGRTVGVSKKK
Protein: Proteasome subunit alpha type-4 (Proteasome component DD4) (P34119)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-6
- Proteasome subunit beta type-2
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-2
Sequence:
MARRYDQRTTIFSPEGRVYQVEYAMTAIRHAGATVGILAKDGIVLAAEKKTTAKLLDSSTSISEKMFKIDEHVVCAVAGITSDANILINYARLSSQRFFYQYQEPMPVEQLVSQICDTKQGYTQYGGLRPFGVSFLYAGWDRHYGFQLYQSDPSGNFAGWKATSIGGENSQVAQSVLRSNYKPDISLKEALQLALKVLTKTMDRSNINSEKLEFSYFTKQGDNVVYHIFTAAELDAFIKETDLEQETEDN
Protein: D-alanyl-D-alanine endopeptidase (DD-endopeptidase) (EC 3.4.21.-) (Penicillin-binding protein 7) (PBP-7) (P0AFI5)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi.
Subcellular location: Periplasm.
Interaction partners:
- D-alanyl-D-alanine carboxypeptidase DacB
- Penicillin-binding protein 1A
- Soluble lytic murein transglycosylase
- Peptidoglycan D,D-transpeptidase FtsI
- Murein DD-endopeptidase MepH
- Peptidoglycan D,D-transpeptidase MrdA
- Penicillin-binding protein 1B
- Murein DD-endopeptidase MepM
- D-alanyl-D-alanine-carboxypeptidase/endopeptidase AmpH
- Putative D-alanyl-D-alanine carboxypeptidase
Sequence:
MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND
Protein: Mitochondrial antiviral signaling (C7C1L6)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MSSFSREKLSLHLRRRMGVFVTRVKATELIIYLPCLTPSDKEEILAKKDFSGNYAAMQLLLDYVQKRMNWPEELMSALEMLEHQDLADELKAEWNKHNQNNPYPPSAAATTAVRTPVHPIPSTSSEGSPSSLVLPAQPAPPEVAAPPEASLPPEVAPEALPPPVVAPQPEAPPSSVPDAPKAAVSPEIASEAAPSPVVVLKAEPQATPPSPVSAEEPTVISEPSASSQPGPIETVSLEDNSSHSDAPTQIALSETTPTSSGSDLIPAVTQIPLAVSHLALSQTESTPAALARFQSPERLPVQDTLSHTVKVTTFHQEAVEDSDPTQVTEDDQHTELSQSQHFSPATASASPPVDTSTNEDDVNFSKPEVLRSEVMDSQPYSGDSTRLQRSVSDLVLATDGVNRPVVVPDPFTTSTHLPCQGNGVPEEINEPLSHNEPQEDTFESSWLSSLGDQEVLHNVAHVSEDASIQNNDGQTPNIVVHVSEESCIWNQDGQTQSMLGTKNVGVSGTPRPVPNRNGQSQGLIMIVNGDDASPSTKHPDAPTGSVAVGSSSAEKRHPLEPMGTEIPMEARAVPELKQEGTIGESYYLLGAAVVAVSLFMAWRMMN
Protein: Estrogen-related receptor gamma (Q6Q6F4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MSNKDRHIESSCPSYIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPTLYGPTGALGPSGTGAKRYEDCSSTITEDSQIKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLTVGMMREGVRLDRVRGGRQKYKRRIDAENSPYLNPQLALPPKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVNIGWAKHIPGFSTLSLADQMSLLQSAWMEILILRVVYRSLSFEDKLVYAEDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHVEDPRRAGKLLMTLPLLRQTSTKAVQHFYSIKQDGKVPMHKLFLELLEAKV
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (O97227)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha
- 3-methyl-2-oxobutanoate dehydrogenase
- Dihydrolipoyl dehydrogenase, apicoplast
- Dihydrolipoyl dehydrogenase
- 2-oxoglutarate dehydrogenase E1 component
- acetate--CoA ligase
- Pyruvate dehydrogenase E1 component subunit beta
- Succinate--CoA ligase subunit beta, mitochondrial
- Glycine cleavage system H protein
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MFVKNVLNVLRRIEGKSFKGRHYLNTSAIHFKIVKCKLFDIGEGISEVEITKWHKNEGDQVSEMESLLTVQSDKAAVDITSKYNGVLVKKYLNENDMLKVGSYFCEIDTDDDIIERDEEEVEKEENNKKEEDGESDLSLNDDISNNDYIKASPGVKRKAKEYKVNLNKVGDYFNKVNISLEDLELYYNNVVKNEYSNNINNNDMDIIEEVSLKGIKLAMCKSMNESLQVPLFHLNEMCIINNLIKMRKEYKEQQKNLQTKETNITITCILIKLISNVLKEFPILNSKFNFKTNTYTMYKNHNISIAVDTPHGLLVPNIKNVQNKNILDIQKDLLSLRDKANNMQLDKSDITNGTITVSNFGAISGTFATPIVFDNQACIIGIGKMEKKLLLKDESNNLNSLNDILVADTINFTFGADHRYIDGATLAQFSKMLKMNIENCASLGPLLE
Protein: Translocating chain-associated membrane protein (Q6P4U7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Translocating chain-associated membrane protein
- Transmembrane protein 123.
- PAT complex subunit CCDC47
Sequence:
MGIRKKTTKNPPVLSHEFVIQNHADIVSCVAMVFLLGLMFEITSKVAVLFITVQYNVTIPANGGPEEATVNYFHYGLKDVATIFFYMLVAIIMHAIIQEYVLDKINRKMHFSKTKHSKFNESGQLSAFYLFSCLWGASILVSENILSNPVSLWDGYPHTLMQFQMKFYYICQLGYWLHAIPELYFQKAKKEDIPRQLVYISLYLVHIAGAYALNLNRLGLVLLVLHYFVELIFHVSRLIYFSNEERQSGFTVWAVLFVLGRLLTLSLSVLTVGFGLAGAEKQGLNLAEGSFNVLFVRVTVLAAICITQAFMMWKFINFQLRRWREQAQTQTLKKKSSSSKSKSKKANGVNGSVGASGADSPRARKEKSS