wanglab/gogpt-training-data huggingface dataset:
Protein: Metal-nicotianamine transporter YSL1 (Protein YELLOW STRIPE LIKE 1) (AtYSL1) (Q6R3L0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in iron loading of the seeds. Acts probably as a transporter of iron- and metal-nicotianamine chelates.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Oligopeptide transporter 3
- Nicotianamine synthase 1
- Nicotianamine synthase 3
- Ferric reduction oxidase 2
- Oligopeptide transporter 1
- Oligopeptide transporter 6
- Oligopeptide transporter 9
- Oligopeptide transporter 8
- Metal transporter Nramp4
- Fe
Sequence:
MEIEQRRIMKREGEEEEDNNQLSLQEEEPDTEEEMSGRTIEPWTKQITVRGVFVSIVIGVVFSVIAQKLNLTTGIVPNLNSSAALLAFVFVQTWTKILKKSGFVAKPFTRQENTMIQTSAVACYGIAVGGGFASYLLGLNHKTYVLSGVNLEGNSPKSVKEPGLGWMTAYLFVVCFIGLFVLIPLRKVMIVDLKLTYPSGLATAVLINGFHTQGDAQAKKQVRGFMKYFSFSFLWGFFQWFFSGIEDCGFAQFPTFGLKAWKQTFFFDFSMTFVGAGMICSHLVNLSLLLGAILSYGLMWPLLDKLKGSWFPDNLDEHNMKSIYGYKVFLSVALILGDGLYTFVKILFVTIANVNARLKNKPNDLDDVGHKKQRKDLKEDENFLRDKIPMWFAVSGYLTFAAVSTVVVPLIFPQLKWYYVIVAYIFAPSLAFCNAYGAGLTDINMAYNYGKIGLFVIAAVTGRENGVVAGLAGCGLIKSVVSVSCILMQDFKTAHYTMTSPKAMFASQMIGTVVGCIVTPLSFFLFYKAFDIGNPNGEFKAPYALIYRNMAILGVQGFSALPLHCLQMCYGFFGFAVLVNVVRDLTPAKIGRFMPLPTAMAVPFLVGAYFAIDMCVGTLIVFVWEKMNRKKAEFMVPAVASGLICGEGLWTLPAAVLALAGVKPPICMKFLAS
Protein: Gibberellin-regulated protein 1 (GAST1 protein homolog 1) (P46689)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
Subcellular location: Secreted.
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g19191
Sequence:
MAISKALIASLLISLLVLQLVQADVENSQKKNGYAKKIDCGSACVARCRLSRRPRLCHRACGTCCYRCNCVPPGTYGNYDKCQCYASLTTHGGRRKCP
Protein: Uridine phosphorylase (UPase) (UrdPase) (EC 2.4.2.3) (P12758)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate. Shows weak activity towards deoxyuridine and thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cytidine deaminase
- Thymidine phosphorylase
- Uridine kinase
- Pyrimidine/purine nucleoside phosphorylase
- Uracil phosphoribosyltransferase
- Thymidine kinase
- Cytosine deaminase
- Pyrimidine 5'-nucleotidase YjjG
- Purine nucleoside phosphorylase DeoD-type
- 5'/3'-nucleotidase SurE
Sequence:
MSKSDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL
Protein: Small glutamine-rich tetratricopeptide repeat-containing protein (Q54VG4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a co-chaperone and regulate the ATPase activity of heat shock proteins.
Interaction partners:
- Golgi to ER traffic protein 4 homolog
- UV excision repair protein RAD23 homolog
- Ubiquitin-like domain-containing protein
- ATPase ASNA1 homolog
- Synaptobrevin-A
- Synaptobrevin-B
Sequence:
MASNKQKLAVSILNFLKVSMKEDAENAESLQVAVECIRDVFGVDENDSTLQVSAPLSEIFDKFIGENNTNTTTTTTTTTTKLSKEELLNQTYSEIPYELLESFKQFITILEQKGAFANEDSCETVIKATKQKFMESKAGEVKAIAEKLKNEGNAKLNEGKHQEALSCYNKAILYDNTNAIYFANRAATYSALQNFEKSIEDCLEAIKRNPNYGKAYTRMGSAYTSLGKFSEAMEAYNKAIELEPNNETFKASLANAERLAAAANNQAPAMPNIPGMPDLGGLDFGSLLSNPAIRGLANNLMSDPKMKEMMDNGDMASLLNNPDLLKMFGNLGKK
Protein: Aromatic peroxygenase (AaP) (EC 1.11.2.1) (B9W4V6)
Organism: Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita)
Function: Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Oxidizes toluene and naphthalene. Catalyzes the regioselective peroxide-dependent hydroxylation of propranolol and diclofenac to 5-hydroxypropranolol and 4'-hydroxydiclofenac. Catalyzes the regioselective peroxide-dependent hydroxylation of naphthalene to 1-naphthol or 2-naphthol via a naphthalene 1,2-oxide intermediate. Catalyzes the regioselective peroxide-dependent oxidation of pyridine to pyridine N-oxide. Halogenates monochlorodimedone and phenol. Oxidizes the sulfur-containing heterocycle dibenzothiophene to yield ring-hydroxylation products and to a lesser extent sulfoxidation products.
Interaction partners:
Sequence:
MKYFPLFPTLVFAARVVAFPAYASLAGLSQQELDAIIPTLEAREPGLPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHLVDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLTVAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTGVEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTPCLMYEKFVNITVKSLYPNPTVQLRKALNTNLDFFFQGVAAGCTQVFPYGRD
Protein: RING finger protein 37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RNF37) (U-box domain-containing protein 5) (UbcM4-interacting protein 5) (Q925F4)
Organism: Mus musculus (Mouse)
Function: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates.
Subcellular location: Nucleus {ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies. {ECO:0000250|UniProtKB:O94941}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Ubiquitin thioesterase OTU1
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 U
- Nucleoporin NUP42
- UV excision repair protein RAD23 homolog A
Sequence:
MVVNLCLPQFRPRIHCNKVSADGYEVENLISEDLIKRSHGFRTEYFIRPPIYVTVSFPFNVEICRVNIDLTTGGYQNVSGLELYTSALSSRVSQDAQDCWTTGPVETSVPDKEAFTLVGKVLLKNQNHVVFSHRGFKARPPFSPMEVTLLSPAVVAQELWNKGALSLSHVAHLKIGITHVTGSGISCIKRLEVWGQPARTCSQEVINSVLLIASESLPQDLDLHAPALPMESDCDPGGQSESQHSPCTLQDMSEVESDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNLSEAAWGRVPSDPFTGLAFTPQSQPLPHPSLKARIDRFLLQHSISGCRLLGRAQTPSAMTPSVITLPSRKRKTEQAEHSSHYSLGMSASSSATSPLFSPTTSEPTAKKMKATSELGLTDMDCSAGPVSHEQKLAQSLEIALTSTLGSMPSFTARLTKGQLQLGTRGSSACRRPASSSEHPRSVSGPECASCKQAFSSYSTNEPVYQLPCGHLLCRPCLSEKQRSQPMMCTACRQPVTSQDVLRVHF
Protein: Zinc finger protein 248 (Q8NDW4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MNKSQEQVSFKDVCVDFTQEEWYLLDPAQKILYRDVILENYSNLVSVGYCITKPEVIFKIEQGEEPWILEKGFPSQCHPERKWKVDDVLESSQENEDDHFWELLFHNNKTVSVENGDRGSKTFNLGTDPVSLRNYPYKICDSCEMNLKNISGLIISKKNCSRKKPDEFNVCEKLLLDIRHEKIPIGEKSYKYDQKRNAINYHQDLSQPSFGQSFEYSKNGQGFHDEAAFFTNKRSQIGETVCKYNECGRTFIESLKLNISQRPHLEMEPYGCSICGKSFCMNLRFGHQRALTKDNPYEYNEYGEIFCDNSAFIIHQGAYTRKILREYKVSDKTWEKSALLKHQIVHMGGKSYDYNENGSNFSKKSHLTQLRRAHTGEKTFECGECGKTFWEKSNLTQHQRTHTGEKPYECTECGKAFCQKPHLTNHQRTHTGEKPYECKQCGKTFCVKSNLTEHQRTHTGEKPYECNACGKSFCHRSALTVHQRTHTGEKPFICNECGKSFCVKSNLIVHQRTHTGEKPYKCNECGKTFCEKSALTKHQRTHTGEKPYECNACGKTFSQRSVLTKHQRIHTRVKALSTS
Protein: ER membrane protein complex subunit 8 (Neighbor of COX4) (O70378)
Organism: Mus musculus (Mouse)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43402}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43402}; Cytoplasmic side {ECO:0000250|UniProtKB:O43402}.
Interaction partners:
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 10
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 5
- Membrane magnesium transporter 2
- ER membrane protein complex subunit 9
Sequence:
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAERQRPRKEHPPGAGSHTLFVDCIPLFHGTLALTPMLEVALTLIDSWCKDNSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFGDAALIMVDNAKFTMDCAAPTIHVYEQHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRSDWTNPEINKAVLHLC
Protein: Large ribosomal subunit protein eL21B (60S ribosomal protein L21-B) (O42706)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL18A
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS14
Sequence:
MPHSYGIRARTRYTFQRGFREHGQIRLSTYLKTYKVGDIVDIKVNGAVQKGMPHKYYHGKTGVVYNVTQSSVGVLIYKVVGNRYMEKRVNVRIEHVKHSKCRQDFLDRVKANEAKRKEAKAQGKTVQLRRQPAPPATAHFVSTENNEPVTLHPVAYDTTI
Protein: WD repeat-containing protein slp1 (P78972)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for mad2-dependent spindle checkpoint activation. Promotes ubiquitin-dependent degradation of cdc13 by the anaphase promoting complex/cyclosome (APC/C).
Interaction partners:
- Mitotic spindle checkpoint component mad2
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit cut9
- Spindle assembly checkpoint component mad1
- Anaphase-promoting complex subunit 1
- Spindle assembly checkpoint protein bub3
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 8
- Spindle assembly checkpoint serine/threonine-protein kinase bub1
Sequence:
MEIAGNSSTISPTFSTPTKKRNLVFPNSPITPLHQQALLGRNGRSSKRCSPKSSFIRNSPKIDVVNTDWSIPLCGSPRNKSRPASRSDRFIPSRPNTANAFVNSISSDVPFDYSESVAEACGFDLNTRVLAFKLDAPEAKKPVDLRTQHNRPQRPVVTPAKRRFNTTPERVLDAPGIIDDYYLNLLDWSNLNVVAVALERNVYVWNADSGSVSALAETDESTYVASVKWSHDGSFLSVGLGNGLVDIYDVESQTKLRTMAGHQARVGCLSWNRHVLSSGSRSGAIHHHDVRIANHQIGTLQGHSSEVCGLAWRSDGLQLASGGNDNVVQIWDARSSIPKFTKTNHNAAVKAVAWCPWQSNLLATGGGTMDKQIHFWNAATGARVNTVDAGSQVTSLIWSPHSKEIMSTHGFPDNNLSIWSYSSSGLTKQVDIPAHDTRVLYSALSPDGRILSTAASDENLKFWRVYDGDHVKRPIPITKTPSSSITIR
Protein: Epstein-Barr nuclear antigen 6 (EBNA-6) (EBV nuclear antigen 6) (Epstein-Barr nuclear antigen 3C) (EBNA-3C) (EBV nuclear antigen 3C) (Epstein-Barr nuclear antigen 4B) (EBNA-4B) (EBV nuclear antigen 4B) (P03204)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays an essential role for the activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Targets host chromatin through interactions with host transcription factors, especially RBPJ and IRF4. Alternatively, EBNA6 also regulates the transcription of the EBV oncogene LMP1 in a cell cycle-dependent manner. Modulates the activity of several host proteins involved in cell cycle regulation including host cyclin A, MYC, RB, p21 and p27 mainly through binding to the host SCF(SKP2) complex. Inhibits the promoter of host H2AX and targets H2AX to proteasomal degradation in order to promote latency and cell proliferation. Upregulates host PIM1 expression and stabilization. Potentiates PIM1 to promote cell proliferation by inhibiting the growth suppressive properties of p21.
Subcellular location: Host nucleus {ECO:0000269|PubMed:24314664, ECO:0000269|PubMed:24429368, ECO:0000269|PubMed:25121590}. Host nucleus matrix {ECO:0000269|PubMed:2161150}. Note=Associated with the nuclear matrix.
Interaction partners:
Sequence:
MESFEGQGDSRQSPDNERGDNVQTTGEHDQDPGPGPPSSGASERLVPEESYSRDQQPWGQSRGDENRGWMQRIRRRRRRRAALSGHLLDTEDNVPPWLPPHDITPYTARNIRDAACRAVKQSHLQALSNLILDSGLDTQHILCFVMAARQRLQDIRRGPLVAEGGVGWRHWLLTSPSQSWPMGYRTATLRTLTPVPNRVGADSIMLTATFGCQNAARTLNTFSATVWTPPHAGPREQERYAREAEVRFLRGKWQRRYRRIYDLIELCGSLHHIWQNLLQTEENLLDFVRFMGVMSSCNNPAVNYWFHKTIGNFKPYYPWNAPPNENPYHARRGIKEHVIQNAFRKAQIQGLSMLATGGEPRGDATSETSSDEDTGRQGSDVELESSDDELPYIDPNMEPVQQRPVMFVSRVPAKKPRKLPWPTPKTHPVKRTNVKTSDRSDKAEAQSTPERPGPSEQSSVTVEPAHPTPVEMPMVILHQPPPVPKPVPVKPTPPPSRRRRGACVVYDDDVIEVIDVETTEDSSSVSQPNKPHRKHQDGFQRSGRRQKRAAPPTVSPSDTGPPAVGPPAAGPPAAGPPAAGPPAAGPPAAGPPAAGPRILAPLSAGPPAAGPHIVTPPSARPRIMAPPVVRMFMRERQLPQSTGRKPQCFWEMRAGREITQMQQEPSSHLQSATQPTTPRPSWAPSVCALSVMDAGKAQPIESSHLSSMSPTQPISHEEQPRYEDPDAPLDLSLHPDVAAQPAPQAPYQGYQEPPAPQAPYQGYQEPPPPQAPYQGYQEPPAHGLQSSSYPGYAGPWTPRSQHPCYRHPWAPWSQDPVHGHTQGPWDPRAPHLPPQWDGSAGHGQDQVSQFPHLQSETGPPRLQLSLVPLVSSSAPSWSSPQPRAPIRPIPTRFPPPPMPLQDSMAVGCDSSGTACPSMPFASDYSQGAFTPLDINATTPKRPRVEESSHGPARCSQATAEAQEILSDNSEISVFPKDAKQTDYDASTESELD
Protein: Mucin (Q61916)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
TTQTSSPNTGKTSTTSTTQTSSPNTGKTSTISTTQTSSPNTGKARPPRTPQTSSPNTGKTSTISTTQTSSPNTGKTSTISTTQTSSPNTGKASTISTTQTISTSGSTMPSSETTHECKQELCNWTNWLDGSYPGSGRNSGDFDTFVNLRSKGYKFCEKPRNVECRAQFFPNTPLEELGQNVTCSREEGLICLNKNQLPPMCYNYEIRIECCTVVNNCSTASVTTHPTSHGVSTKTETNWTTHVYSSPTKDTSSHSATIDTKTWTSGISHTTTQPVTTHCQLQCNWTKWFDTDFPVPGPHGGDLETYSNIERSGERLCHREEITQLQCRAKNYPEREMEDLGQVVKCDPSVGLVC
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial (Complex I-9kD) (CI-9kD) (NADH-ubiquinone oxidoreductase 9 kDa subunit) (Q8BK30)
Organism: Mus musculus (Mouse)
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. May be the terminally assembled subunit of Complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 2
Sequence:
MAVSLLLRGGRIRALKAVLLEARVFPGELVSVVRLSTESEKSAKEKELHPKTQSVLKEPEPTDTTTYKNLQHHDYNTYTFLDLNLDLSKFRLPQPSSGRESPRH
Protein: Scaffold attachment factor B, isoform D (A0A0B4KGV9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPEAGKKIAELRVCDLKSELEKRELETVGPKAVLIERLEKSLRAEGLDPATHLIVPGAKAKKPFAMPMKDLQSEVVIKEEPIDANEEEVKVEQQDDYQNGNDYSHHADDDGHEIDQVGDVDDECVILDDDDEEDEDHVYDDEPQSGDGDAEGKAQDDGAENNGDDKAIIHGEEENTGDTGNMDNDESINLTIGEDEQKLLHDEASDDKSIKSVKPANKSEKSNSKDADKKNDDGARSKKRDEKSGDKKDSSEQKSSGKSSNQKDDKGSWSPAMILASAG
Protein: Aminopeptidase ltah-1.1 (EC 3.4.11.6) (Aminopeptidase-1) (AP-1) (Arginine aminopeptidase 1) (Leukotriene A4 hydrolase homolog ltah-1.1) (G5EFT4)
Organism: Caenorhabditis elegans
Function: Aminopeptidase which preferentially removes N-terminal Arg and Lys residues from peptides and proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9774412}.
Interaction partners:
- Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein
- C2H2-type domain-containing protein
- AP-1 complex subunit mu-1-I
- MHD domain-containing protein
- Aminopeptidase-like protein AC3.5
- AP-1 complex subunit gamma
Sequence:
MAPPHPRDPSTAANYEQVTVSHYALKWKVDFEKKHIAGDVSITLDVKQDTERIVLDTRDLSVQSVALNLNGEPKKAGFTLEDNQALGQKLVITTESLKSGDRPVLEIKYESSNNAAALQFLTAEQTTDRVAPYLFSQCQAINARSIVPCMDTPSVKSTYEAEVCVPIGLTCLMSAIGQGSTPSECGKRTIFSFKQPVSIPSYLLAIVVGHLERKEISERCAVWAEPSQAEASFYEFAETEKILKVAEDVAGPYVWGRYDLVVLPATFPFGGMENPCLTFITPTLLAGDRSLVNVIAHEISHSWTGNLVTNFSWEHFWLNEGFTVFLERKIHGKMYGELERQFESESGYEEALVRTVNDVFGPDHEYTKLVQNLGNADPDDAFSSVPYEKGSALLFTIEQALGDNSRFEQFLRDYIQKYAYKTVSTEEWKEYLYDSFTDKKVILDNIDWNLWLHKAGLPPKPKYDSTPMQACKDLAAKWTTEGSEAPTDGEVFAKMSNSQKLAVLDAVRVNKTMFGDRMPALTATYKLDQAKNAELKFSWLMLGLETKWSPIVDASLAFALAVGRMKYCKPIYRSLFGWSATRDRAISQFKANIPNMHPITVKAIQSLLK
Protein: Small VCP interacting protein, isoform A (Small VCP interacting protein, isoform B) (Q8IQC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH01724p
- Uncharacterized protein
- Transitional endoplasmic reticulum ATPase TER94
- Nuclear protein localization protein 4 homolog
- GM09977p
- UBX domain-containing protein 6
- UBX domain-containing protein 4
- CG15717-PA
Sequence:
MGACLSCCGQSAEETNLMPSPEERRQQQLDAAEKRRQENEHRGIKNPDSVRRQQQRAEEMQRREEEAARQGQGQSNLRWQTS
Protein: Perilipin-5 (Lipid storage droplet protein 5) (Q00G26)
Organism: Homo sapiens (Human)
Function: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity).
Subcellular location: Lipid droplet {ECO:0000269|PubMed:17234449}. Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}. Mitochondrion {ECO:0000250|UniProtKB:M0R7Z9}. Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. {ECO:0000250|UniProtKB:Q8BVZ1}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 2
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Hormone-sensitive lipase
- Peroxisome proliferator-activated receptor alpha
Sequence:
MSEEEAAQIPRSSVWEQDQQNVVQRVVALPLVRATCTAVCDVYSAAKDRHPLLGSACRLAENCVCGLTTRALDHAQPLLEHLQPQLATMNSLACRGLDKLEEKLPFLQQPSETVVTSAKDVVASSVTGVVDLARRGRRWSVELKRSVSHAVDVVLEKSEELVDHFLPMTEEELAALAAEAEGPEVGSVEDQRRQQGYFVRLGSLSARIRHLAYEHSVGKLRQSKHRAQDTLAQLQETLELIDHMQCGVTPTAPACPGKVHELWGEWGQRPPESRRRSQAELETLVLSRSLTQELQGTVEALESSVRGLPAGAQEKVAEVRRSVDALQTAFADARCFRDVPAAALAEGRGRVAHAHACVDELLELVVQAVPLPWLVGPFAPILVERPEPLPDLADLVDEVIGGPDPRWAHLDWPAQQRAWEAEHRDGSGNGDGDRMGVAGDICEQEPETPSCPVKHTLMPELDF
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (EC 3.2.1.113) (Man(9)-alpha-mannosidase) (Man9-mannosidase) (Mannosidase alpha class 1A member 1) (Processing alpha-1,2-mannosidase IA) (Alpha-1,2-mannosidase IA) (P33908)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Alpha-mannosidase 2
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
- Alpha-mannosidase 2x
- Mannosyl-oligosaccharide glucosidase
Sequence:
MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDNLARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPIGVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHLSHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEKYYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2) (Q15057)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).
Subcellular location: Cell membrane {ECO:0000269|PubMed:30905672}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with RAB35 at the membrane protrusions of HEK293T cells. {ECO:0000269|PubMed:30905672}.
Interaction partners:
- Ras-related protein Rab-35
- ADP-ribosylation factor 6
- ADP-ribosylation factor 5
- ADP-ribosylation factor 1
Sequence:
MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDRLVVDAAKEKREMEQKHSTIQQKDFSSDDSKLEYNVDAANGIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDNPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIATAYREKGDESEKLDKKSSPSTGSLDSGNESKEKLLKGESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEANVEKMGIKKPQPGQRQEKEAYIRAKYVERKFVDKYSISLSPPEQQKKFVSKSSEEKRLSISKFGPGDQVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEGERQDSSMFLDSKHLNPGLQLYRASYEKNLPKMAEALAHGADVNWANSEENKATPLIQAVLGGSLVTCEFLLQNGANVNQRDVQGRGPLHHATVLGHTGQVCLFLKRGANQHATDEEGKDPLSIAVEAANADIVTLLRLARMNEEMRESEGLYGQPGDETYQDIFRDFSQMASNNPEKLNRFQQDSQKF
Protein: Methionine aminopeptidase 1 (MAP 1) (MetAP 1) (EC 3.4.11.18) (Peptidase M) (P9WK21)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Interaction partners:
- Adenylate kinase
- Large ribosomal subunit protein uL18
- Protein translocase subunit SecY
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL4
Sequence:
MRPLARLRGRRVVPQRSAGELDAMAAAGAVVAAALRAIRAAAAPGTSSLSLDEIAESVIRESGATPSFLGYHGYPASICASINDRVVHGIPSTAEVLAPGDLVSIDCGAVLDGWHGDAAITFGVGALSDADEALSEATRESLQAGIAAMVVGNRLTDVAHAIETGTRAAELRYGRSFGIVAGYGGHGIGRQMHMDPFLPNEGAPGRGPLLAAGSVLAIEPMLTLGTTKTVVLDDKWTVTTADGSRAAHWEHTVAVTDDGPRILTLG
Protein: NAD(P)H-dependent oxidoreductase (NADPH-flavin oxidoreductase) (Q7BGI8)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MDREQVVALQHQRFAAKKYDPNRRISQKDWEALVEVGRLAPSSIGLEPWKMLLLKNERMKEDLKPMAWGALFGLEGASHFVIYLARKGVTYDSDYVKKVMHEVKKRDYDTNSRFAQIIKNFQENDMKLNSERSLFDWASKQTYIQMANMMMAAAMLGIDSCPIEGYDQEKVEAYLEEKGYLNTAEFGVSVMACFGYRNQEITPKTRWKTEVIYEVIE