wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-1 receptor-like 2 (EC 3.2.2.6) (IL-36 receptor) (IL-36R) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2) (Q9HB29)
Organism: Homo sapiens (Human)
Function: Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways (By similarity). The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway.
Subcellular location: Membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:24829417}.
Interaction partners:
- Interleukin-36 receptor antagonist protein
- Interleukin-1 family member 10
- Interleukin-36 alpha
- Interleukin-1 receptor accessory protein
- Interleukin-36 beta
- Interleukin-36 gamma
- Interleukin-1 receptor type 1
- Acyl carrier protein, mitochondrial
- Interleukin-1 alpha
- Interleukin-1 beta
Sequence:
MWSLLLCGLSIALPLSVTADGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFRAYLIGGLIALVAVAVSVVYIYNIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG
Protein: Putrescine N-methyltransferase 2 (NtPMT2) (EC 2.1.1.53) (Q9SEH7)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Methyltransferase that mediates the conversion of putrescine to N-methylputrescine. Promotes leaves ripening.
Interaction partners:
- Arginase 1
- Arginase 1, mitochondrial-like
- arginase
Sequence:
MEVISTNTNGSTIFKSGAIPMNGHHNGTSKHQNGHKNGTSEQQNGTISLDNGNELLGNSNCIKPGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPTIEKIDIVEIDDVVVDVSRKFFPYLAANFNDPRVTLVLGDGAAFVKAAQAEYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEIDFKNPVNPIDKETAQVKSKLAPLKFYNSDIHKAAFILPSFARSMIES
Protein: Vacuolar protein sorting-associated protein 26B (Vesicle protein sorting 26B) (Q4G0F5)
Organism: Homo sapiens (Human)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8C0E2}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C0E2}. Early endosome {ECO:0000250|UniProtKB:Q8C0E2}. Late endosome {ECO:0000250|UniProtKB:Q8C0E2}. Note=Localizes to early and late endosomal structures (By similarity). {ECO:0000250|UniProtKB:Q8C0E2}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 26A
- TBC1 domain family member 5
- Sorting nexin-27
- Sorting nexin-3
- Sorting nexin-5
- Sorting nexin-6
Sequence:
MSFFGFGQSVEVEILLNDAESRKRAEHKTEDGKKEKYFLFYDGETVSGKVSLALKNPNKRLEHQGIKIEFIGQIELYYDRGNHHEFVSLVKDLARPGEITQSQAFDFEFTHVEKPYESYTGQNVKLRYFLRATISRRLNDVVKEMDIVVHTLSTYPELNSSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIKHMEIDIIKRETTGTGPNVYHENDTIAKYEIMDGAPVRGESIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEVVLWRKGDIVRKSMSHQAAIASQRFEGTTSLGEVRTPSQLSDNNCRQ
Protein: Heterogeneous nuclear ribonucleoprotein K, isoform A (Heterogeneous nuclear ribonucleoprotein K, isoform F) (LP16172p) (A1ZBW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKREMNDEGEGPQDQKRNRRNEETVRILIPSSIAGAVIGKGGQHIQKMRTQYKATVSVDDSQGPERTIQISADIESTLEIITEMLKYFEERDEDFDVRLLIHQSLAGCVIGKGGQKIKEIRDRIGCRFLKVFSNVAPQSTDRVVQTVGKQSQVIEAVREVITLTRDTPIKGAIHNYDPMNFDRVYADEYGGYGTGSGSTRPSQRGNNRNGGGAGGVAGGAAGGNGGGFNAGGARGNAGGRGGADRFGGAAGGAVAGAGMGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSDFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQSVHENGRRNI
Protein: Protein unc-50 homolog (Periodontal ligament-specific protein 22) (PDLs22) (Q9CQ61)
Organism: Mus musculus (Mouse)
Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity).
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
Interaction partners:
- Protein RIC-3
- Protein disulfide-isomerase TMX3
Sequence:
MLPSTSLSSSMHGNGVLNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARDDPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFVSNKYLVKRQSRDYDVEWGYAFDVHLNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVILLYPFAPLMVLYGLSLALGWNFTHTLCSFYKYRVK
Protein: Conserved ala-, pro-rich protein (O06555)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved hypothetical ala-, pro-rich protein
- DNA 3'-5' helicase
- Peptidoglycan endopeptidase RipA
- Conserved protein
- Possible conserved transmembrane alanine and glycine rich protein
- Conserved hypothetical cysteine rich protein
- Exported repetitive protein
- Probable peptidoglycan glycosyltransferase FtsW
- Possible Inv protein
- Polyprenol-phosphate-mannose-dependent alpha-
Sequence:
MRRLTNTEHRENTTVASTWSVCKGLAAVVITSAAAFALCPNAAADPATPQPNPTQQLPGLPALAQLSPIIQQAAMNPAQATQLLMAAASAFAGNPAVPTESKNVASSVNQFVAEPTNPDSAALGVPAPHGVALPEAIPVPHVPPLGAEPGVQAHLPTGIDPSHAAGPAPAVAPTVTPPVAAPPASAPAPAPDAAQPVAVPGPPPAPPAPRAAAPAPASAAPAPAAAPAPASGFGADAPPTQDFMYPSIGPNCVADGSNSIATALSVAGPAKIPLPGPGPGQTAYVFTAVGTPGPADVQRLPLNVTWVNLTTGKSGSATLRPRSDINPDGPTTLTVIADTGSGSIMSTIFGQVTTKDRQCQFMPTIGSTVVP
Protein: Rho family-interacting cell polarization regulator 2 (Q1LU99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization (By similarity). Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation. Maintains naive T lymphocytes in a quiescent state and prevents chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration. Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion. Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear. Plays a role for maintaining the structural organization of the basal domain of stereocilia. Involved in mechanosensory hair cell function (By similarity). Required for normal hearing.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4F9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Apical cell membrane {ECO:0000250|UniProtKB:Q7TP54}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q80U16}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q7TP54}.
Interaction partners:
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Dysferlin
- Taperin.
Sequence:
MAFPDITEDDLNELMREEAEDVFDDDGVSSRFPDIMAAGTHSPGGPNGIIRSQSFAGFSTLQERRSRCNSFMGNSAVQKKPISKPRKPHLSGHKSSSSSSSSREPQPKRVEEVYSALKQGLDEYLEVHQTELDKLTSLMKDMKRNSRLGVLYDLDKQIKTIERYMRRLEFHISKVDELYEGFCIQRRLRDGASKMKQAFTASPSTKGTRESLAEVNRRYKEYTENMSTFEGELENLLGEFHIKMKGLAGFARLCPGDQYEIFMRYGRQRWKLKGKIEGNSKQSWDGEEMIFMPLISDLINIKVTELKGLATHVLVGSVICETKDLFTAMPQVVAVDVNDLGTIKLNLEVAWFPFDVEDLTLSSGNVSKATALQRRVSVYSQGTPETPTFQDTSFFKWQPRRWEGQRLSFLHTLRETLIEKLRRSRSFGDLAALRPRSRSSLEVYSTLPDDVFENGGCGVAECKRLSFTFSDTSTSSPVPVQSNPEITVTPPETDPSSEPPPTSEEQLVEEECVEEDCGSISVSVSVSDPDLEWDQVETQGPETGSVALSLCSESQLSAVGPEDVVFLEPNVSDEALELKPVELDGEEGSLTRQLVRRLTSSDMLPETSALSWAGENSRTFMESSLEEVIQSLLLRLESLGQRCGELQDLEQEVMRLEDLLKCRVHAHRSRSSSLSLTVESALESFDFLNTSDFDDDDTGDDAGTLSRAVFFDMESERMGSGQHPEARGHLSEALTEDTGVGNSVAGSPLPLTTGNENLDVAVVIHLQYCNHLIQLLTSGGSQLQHKTYLHKLATQTLLLEELSERNFDRPSSCTSVPDVLPGLVERPALMSLWSDCSGGLFHTTLDRVLKHMHLSFALGLQQVLPHSPDSVIKMVVNEMMDRSELASSSTSPAQDVITVFQFHRYIVEHCITDMEQHLLDLAKEVMLEEALSCGDPERSLKELKKVSITCLQPRSQTLLAVAGLLTTDDPEVMKATTDFLSSAASHQPFRSKAVDCYTQALSESELHTQRAACAALSCLQAVESIDAVILLCDSVDEELRQIAIETLLTFGEDGRLAYEQLDTVPREMVRLGTRRGNAVTTSF
Protein: LOC100001692 protein (Nuclear receptor subfamily 0 group B member 1) (A3KNP5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAYFDSGCHCSSERRQNSILYSILKNDSQSAQLGNQPRAPRLAVSMRACACGSKRKVSLRSPQTTCKAASAVLVKTLKFVKNVPCFRELPADDQHTLVRSGWAPLLVLGMAQDRIDFETSETQEPSMLQRILTSGQDKQDNQSHNGGVALTDVQGIKMFLRKCWGLDISTKEYAYLKGAILFNPDVAGLQCQHYIQALQSEANQALNEYVKMIHRGDSARFAKLFLALSMLRSINANVVAGLFFKPVIGAVNMEELLLEMFYGK
Protein: Interleukin-17D (IL-17D) (Interleukin-27) (IL-27) (Q8TAD2)
Organism: Homo sapiens (Human)
Function: Induces expression of IL6, CXCL8/IL8, and CSF2/GM-CSF from endothelial cells.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-25
- Interleukin-17 receptor B
- Tyrosine-protein kinase JAK2
- Interleukin-27 receptor subunit alpha
- Tyrosine-protein kinase JAK1
- Non-receptor tyrosine-protein kinase TYK2
- Interleukin-17 receptor A
- Interleukin-6 receptor subunit alpha
- Interleukin-17 receptor C
- Interleukin-17 receptor E
Sequence:
MLVAGFLLALPPSWAAGAPRAGRRPARPRGCADRPEELLEQLYGRLAAGVLSAFHHTLQLGPREQARNASCPAGGRPADRRFRPPTNLRSVSPWAYRISYDPARYPRYLPEAYCLCRGCLTGLFGEEDVRFRSAPVYMPTVVLRRTPACAGGRSVYTEAYVTIPVGCTCVPEPEKDADSINSSIDKQGAKLLLGPNDAPAGP
Protein: Galectin (Q6IQI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAGVLIQNMSFKVGQTLTITGVPKPDSTNFAINIGHSPEDIALHMNPRFDAHGDQCTIVCNSFQSGSWCEEHRDNNFPFIQDKEFQIKITFTNEEFLVTLPDGSEIHFPNRQGSEKYKYMHFEGEVRIQGVEIK
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial (Complex I-ASHI) (CI-ASHI) (NADH-ubiquinone oxidoreductase ASHI subunit) (Q02372)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
Sequence:
MAAARAGVLGVRWLQKAARNVVPLGARTASHITKDMLPGPYPKTPEERAAAAKKYNMRVEDYEPYPDDGTGYGDYPKLPDRSQQERDPWYDWDHPDLRLNWGEPMHWDLDMYIRNRVDTSPTPVNWNLMCKHLFGFVAFMLFMFWVGETYPAYQPVGPKQYPYNNLYLERGGDPNKEPEPVVHYEI
Protein: Uroplakin-1a (UP1a) (Tetraspanin-21) (Tspan-21) (Uroplakin Ia) (UPIa) (UPKa) (O00322)
Organism: Homo sapiens (Human)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uroplakin-3a
- Uroplakin-2
- Uroplakin-1b
- Putative postmeiotic segregation increased 2-like protein 11
- Leukocyte surface antigen CD53
- Leukocyte antigen CD37
Sequence:
MASAAAAEAEKGSPVVVGLLVVGNIIILLSGLSLFAETIWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRAATPEVVFPWPPLCCRRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTML
Protein: Putative capsid protein (Q4G3H1)
Organism: Penicillium stoloniferum virus F
Interaction partners:
Sequence:
MSFETSEGMSRPGDNPNKLNAKPRQSARPKTRNSTAQSNQTMRLGWIDPLPQVDTIFPLGLEPNVESIPAGEVELDFNLPETIAKPFADTVTSVGDRIQLVDDDKENIATSIYGLSFFKAARQLYSTMLDHEKAVNQPLKAVYYDETPIPAHMSGALGIIGHMKTKVGDVLVKDAGVLFKRGTAAGVTKFSEIDNDKTWNLDCSKLVWADHSSLSMIKRLASEKISQLVKQRYRVTDAQGHVYSVSMPQLTDQALPDYYDSIPDVAPNSDQLRVLTAALQMSLAQFRNDELPHDEDRSDLLTTLDLLYADGAYEISALRDQFELLMARYTTDFKWRVESIFKVGPPPAGTTGYGAQTVSSTGNTARWQFPLSDADINIGYLFSPSKSFSLFPKMVGYSKRAREDASASFANSDAKKFYAD
Protein: Protein translocase subunit SecD (Sec translocon accessory complex subunit SecD) (P0AG90)
Organism: Escherichia coli (strain K12)
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}.
Interaction partners:
- Protein translocase subunit SecY
- Protein-export membrane protein SecG
- Sec translocon accessory complex subunit YajC
- Membrane protein insertase YidC
- Protein translocase subunit SecE
- Protein translocase subunit SecF
- Protein translocase subunit SecA
- Protein-export protein SecB
- Signal recognition particle protein
- Queuine tRNA-ribosyltransferase
Sequence:
MLNRYPLWKYVMLIVVIVIGLLYALPNLFGEDPAVQITGARGVAASEQTLIQVQKTLQEEKITAKSVALEEGAILARFDSTDTQLRAREALMGVMGDKYVVALNLAPATPRWLAAIHAEPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDAKARDEAIAYLSKRHPDLVISSQGSNQLRAVMSDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAASGRVPGDSEVKQTREGQPVVLYKRVILTGDHITDSTSSQDEYNQPQVNISLDSAGGNIMSNFTKDNIGKPMATLFVEYKDSGKKDANGRAVLVKQEEVINIANIQSRLGNSFRITGINNPNEARQLSLLLRAGALIAPIQIVEERTIGPTLGMQNIEQGLEACLAGLLVSILFMIIFYKKFGLIATSALIANLILIVGIMSLLPGATLSMPGIAGIVLTLAVAVDANVLINERIKEELSNGRTVQQAIDEGYRGAFSSIFDANITTLIKVIILYAVGTGAIKGFAITTGIGVATSMFTAIVGTRAIVNLLYGGKRVKKLSI
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (NAXE) (YjeF N-terminal domain-containing protein 1) (YjeF_N1) (Q8NCW5)
Organism: Homo sapiens (Human)
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:11991719}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}.
Interaction partners:
- Apolipoprotein A-I
- ATP-dependent
- Pyridoxine-5'-phosphate oxidase
- Apolipoprotein A-II
- m7GpppN-mRNA hydrolase
- Uridine diphosphate glucose pyrophosphatase NUDT14
- Low-density lipoprotein receptor-related protein 2
Sequence:
MSRLRALLGLGLLVAGSRVPRIKSQTIACRSGPTWWGPQRLNSGGRWDSEVMASTVVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSRSPPTVLVICGPGNNGGDGLVCARHLKLFGYEPTIYYPKRPNKPLFTALVTQCQKMDIPFLGEMPAEPMTIDELYELVVDAIFGFSFKGDVREPFHSILSVLKGLTVPIASIDIPSGWDVEKGNAGGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPPYPDTECVYRLQ
Protein: Uncharacterized protein (C8JQS1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRFRSLGALSVLLLFLQLPGPSSEYELSINHEEVTDSDRRVLLEIAKAVKRVKRNPFKRDEGRSSVDSDLRQKEDNGDDNGGDEESEGKPENFQGSANDYCDKFEQHFSYFCVGETDQTDKNAYVIKKFCPSYKTACKHKAVTTSVSLTSWPTDPFAKEITVASRPLPSTSGRTSHSRRRDSDEDSDSAEDEEVYYAELRKRYPCKPDCDKRIFAHCTEECKCDYIYPVVQRFCNPPPMPMFLNTCRLWYHGCPKYERYHYASQFVYSKAEKGKVLPGSPDQASVNPYGLPQPAPLRNRALALAPIRRQKRDAENEDLVVPPPVPSEIQEREASLTAPESRAILQNYRENLKSGEKKKRRSRRKKLRRRRRHRQRFSFDKDFEEITTTKRPPTPRELWRALKQLNSLTSGPGAVGLKSSPATLKGGGEAQGGLDGLLASVTQPQRERDEAARQWATVEPTKETSQSFHQTPRSPHKAVETTPSVLSTDSPIPEDSSTPRGADRHSPNLVSGSPIQQIHILEIPQTNTGIIPSPSESTGSMVSFNGEVIGLYLPPEQEALLE
Protein: Polypeptide N-acetylgalactosaminyltransferase (C6S3M5)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037847}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037847}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MLPRMLKMKTVGTVLAVIWLFGLAFIYVQSTSSSLRPPGRHPPPLPQLDPLIPQNPPQNDEIRPKKSAPPIPTINLAEDTTIHERTEKDVTWKTFDVEKFLNKGKWHQGEDKYKANSFNQEASDALNPTRKIPDSREPQCRDVDYSKVGMQPTTVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRKERHAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFRKKHPYTFPGGSGNVFQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVYPQLENAELFCYETSSLVPLVQKFLFAEFSSI
Protein: 40S ribosomal protein S18, putative (Q38B69)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
- 60S ribosomal protein L39, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L29
- 40S ribosomal protein S26
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S8
- 40S ribosomal protein S16, putative
Sequence:
MSLTLQSESFQHIVRLLNTNVEGKRKVPFALRMVKGIGIRFAYMVCKKAGVDVERRAGTLSPEELEKISEVIADPAKFKIPEWFLNRQRDPKTGKTEHLTSSMVDTRLREDLERLRKIRAHRGVRHAYGLRVRGQHTCTSGRRGKTVGVSRTK
Protein: RNA-binding protein 38 (RNA-binding motif protein 38) (RNA-binding region-containing protein 1) (ssDNA-binding protein SEB4) (Q62176)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that specifically bind the 3'-UTR of CDKN1A transcripts, leading to maintain the stability of CDKN1A transcripts, thereby acting as a mediator of the p53/TP53 family to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor transcriptionally regulated by the p53/TP53 family to induce cell cycle arrest. Has the ability to induce cell cycle arrest in G1 and maintain the stability of CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA splicing factor. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2 (By similarity). Plays a role in myogenic differentiation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- ELAV-like protein 1
Sequence:
MLLQPACSPSVFPRPSAAPSAMHGSQKDTTFTKIFVGGLPYHTTDASLRKYFEGFGDIEEAVVITDRQTGKSRGYGFVTMADRAAADRACKDPNPIIDGRKANVNLAYLGAKPRSLQTGFAVGVQQLHPTLIQRTYGLTPHYIYPPAIVQPSVVIPATPVPSLSSPYLEYTPASPAYAQYPPATYDQYPYAASPAAATSFVGYGYPAAVPQALSAAAPAGTTFVQYQAPQLQPDRMQ
Protein: Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Acyl-CoA synthetase short-chain family member 3) (Propionate--CoA ligase) (EC 6.2.1.17) (A0A0G2K047)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Propionate is the preferred substrate but can also utilize acetate and butyrate with a much lower affinity.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28003429}.
Interaction partners:
- Ethylmalonyl-CoA decarboxylase
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Acetyl-coenzyme A synthetase, cytoplasmic
- Trifunctional enzyme subunit beta, mitochondrial
Sequence:
MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAGVARRALVAGFGGRGCRALTTSSGGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLENRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYAMLACARIGAIHSLIFGGFASKELSTRIDHVKPKVVVTASFGIEPGRKVEYMPLLEEALRIGQHKPDRLLIYNRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKCVPGYNVMILDDNMQKLKARSLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESVLSHGTVTDCAVVGKEDPLKGHVPLALCVLKKDVNATEEQVLEEIVKHVRQSIGPVAAFRNAVFVKQLPKTRSGKIPRSTLSALVNGKPYKVTPTIEDPSIFGHIEEVLKQAL
Protein: COP9 signalosome complex subunit 5 (EC 3.4.-.-) (O94454)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 7
- Cullin-1
- Cullin-3
- Ubiquitin-like protein 1
- Cullin-4
- Eukaryotic translation initiation factor 3 subunit H
- RING-box protein pip1
Sequence:
MNNQLENVFRFDEEKERAKIRESPWKHDPEFFRSVKISAVALLKMLRHVSQGMPLEVMGYVQGKVEGASLIILDSFALPVEGTETRVNAHEEAQEYSVQYHTLCKSVYRHENVIGWYHSHPNYGCWLSGVDVETQRQNQKYQDPFVAVVLDPKRSLESPYVNIGAFRTYPVGNDGSIRTKSRHHPSVLFKNLPSSKIEDAGAHAEAYYSLPITYFHSKAEKKVTEFLRNRNWSRSITECSILQNNEFLHDSEKLIDHLIHETGNNELPVASAYEQSKACCNELSTFLSQIDVQDKLFKE