wanglab/gogpt-training-data huggingface dataset:
Protein: Putative thrombospondin (Q968S4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNWTRVLLIGLTALALTFVEVASLSLDPVASAELEQFIRKGDVVISTRHIRPRRKLHISIEALFMIDFPMLKHKMSFFLDRKQQRVTLDISANGATESRNFEIPNINETSTIRSLALQFSKNRITLHVDCKASTHHDIDMNLAKLYTQMDDPVIKLFRERKYPLHFDGDMEHSLQRANCQKGNHRRGNRRMLRNKITEREKNKKRDVRGWYEPTIAREGVVDHRHQEVPTDVERGDIPVLNGDCEDALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGCKNPLTTDNQLRIEPDCRSANPCYPGVECLDSAAGPRCGHCPLGFIGDGKSCKPGVTCAHHMCYPGVQCHDTVNGAQCDSCPAGYEGDGRTCSLRNPCLDTPCPSGAQCLQVGYPPYFHCISCPMGHEVNGTSCRDMNECLLYDPCDELATCTNLSPGFQCSPCPVGFDGTHAHGYFADYYSVDYRRQTCLDVDECRTGFFRCPEHSTCINEIGSYRCQCHEGYVTNGTYSCLDRSSVFMCPDGTVCDRNAVCLRMDNIRHKCHCNVGWAGNGLICGRDTDVDGWPDQAIGCPELHCQRDNCPKLPNSGQEDADLDGHGDGCDDDADGDNVQNSQDNCWLAYNTEQLDSDGDKVGDVCDNCVLKYNPRQLDTDEDGLGDECDGDIDNDSIPNALDNCPLLPNPSQSDVDNDGVGDACDNCPNLPNPDQKDRDMDFVGDACHRDIDGDDDGVPNSLDNCPMVSNSDQLDTDGDGTGDECDDDMDGDGIPNYKDNCPLAKNPKQDDFNRNGKGDSCEDDEDVDGVPNGMDNCPNNSMIHHTDFRTLQTIPLDPKGLSQADPNWVVHANGTEIVQTLNSDPGLAVGKDAFGGVDFDGTFYINDDTDDDYAGFVFSYQSSYKYYVVQWKKGTQTYWEPRPFTASAAPGIQIKLVNSTEGPGPMMRNSLWHEGNTDGEARLLWKDPKNIAWKERTSYRWSLVHRPAIGLIRLQMHEGNRLIFDSGNVFDSTLKGGRLGVFCFSQRMIIWSNLQYKCNNRVKPLIYNDLSDYLKTKVELQD
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase 1 (EC 1.3.1.22) (SR type 1) (Steroid 5-alpha-reductase 1) (S5AR 1) (Q68FF9)
Organism: Mus musculus (Mouse)
Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Subcellular location: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 17-beta-hydroxysteroid dehydrogenase type 6
- Estradiol 17-beta-dehydrogenase 2
- Polyprenal reductase
- Aldo-keto reductase family 1 member C18
- Aldo-keto reductase family 1 member D1
- Aromatase
Sequence:
MELDELCLLDALVYLEGFLAFVAFVGLQMVGSSYGRYSSQWSGRRVPARPAWFLQELPSMAWPLYECIRPAAARLGNLPNRVLLAMFLIHYVQRTLVFPVLIRGGKPTLLFTFVLAFLFCTLNGYLQSRYLSQFAVYAEDWVTHPCFLTGFALWLVGMVINIHSDHILRNLRKPGETGYKIPRGGLFEYVSSANYFGELVEWCGFALASWSLQGVVFALFTLCALFTRARQHHQWYLEKFEDYPKTRKILIPFLL
Protein: D-alanyl-D-alanine carboxypeptidase DacA (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Beta-lactamase) (EC 3.5.2.6) (Penicillin-binding protein 5) (PBP-5) (P0AEB2)
Organism: Escherichia coli (strain K12)
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Subcellular location: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=N-terminal lies in the periplasmic space.
Interaction partners:
- D-alanyl-D-alanine carboxypeptidase DacB
- Penicillin-binding protein 1A
- Putative D-alanyl-D-alanine carboxypeptidase
- Peptidoglycan D,D-transpeptidase MrdA
- Penicillin-binding protein 1B
- Peptidoglycan glycosyltransferase MrdB
- Peptidoglycan D,D-transpeptidase FtsI
- D-alanyl-D-alanine carboxypeptidase DacD
- D-alanyl-D-alanine carboxypeptidase DacC
- Cell shape-determining protein MreB
Sequence:
MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG
Protein: Methionine-R-sulfoxide reductase B3 (MsrB3) (EC 1.8.4.12) (EC 1.8.4.14) (Q8IXL7)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. Isoform 2 is essential for hearing.
Subcellular location: [Isoform 1]: Endoplasmic reticulum.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion.
Interaction partners:
- Mitochondrial peptide methionine sulfoxide reductase
Sequence:
MSPRRTLPRPLSLCLSLCLCLCLAAALGSAQSGSCRDKKNCKVVFSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSYGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPADSSGTAEGGSGVASPAQADKAEL
Protein: rRNA biogenesis protein RRP36 (Ribosomal RNA-processing protein 36) (Q12481)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:20038530}.
Interaction partners:
- Something about silencing protein 10
- Nucleolar protein 19
- U3 small nucleolar RNA-associated protein 25
- Casein kinase II subunit beta
- KRR1 small subunit processome component
- Essential nuclear protein 1
- Ribosomal RNA-processing protein 9
- U3 small nucleolar RNA-associated protein 6
- Suppressor of glycerol defect protein 1
- Protein SQS1
Sequence:
MSYYFKNLKPDLNSDVEEDDGNLLESIMANKSKREIDEQESSDDELKTLSFGSLKKAETVIDEEDFKDTKPVHKKPITTTYREESFDEDEDSEDQSDEDAGFFEEDSEDETHHGQKVPKKKSKHAPVEQSSKKRVPRVRNIPGLEIPRNKRSNLYQDIRFDKSTGKALDSSIIRKRYQFLDEYREKEIDELQKLLQERKFLSKIDQGEREEMEQRLKSMKSRLQSMKNKDLEREILKEYENDMNKNNNTRYHLKKSEKRKVVQKWKFDHMKAKQREKVMERKRKKRLGKEFKQFEFHNRR
Protein: GEO09608p1 (RH08789p) (Short spindle 7) (Q8IR95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Cuticular protein 60D, isoform A
Sequence:
MKSVTFVLCLLVLGAHSLLVFAVDCEIGGHQFKTGEKYTPEGRCLQYTCQAPKQVTALGCPAIASLKPCKMEEDLSKPYPGCCPKFNC
Protein: Glucagon-like peptide 2 receptor (GLP-2 receptor) (GLP-2-R) (GLP-2R) (O95838)
Organism: Homo sapiens (Human)
Function: This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-glucagon
- Guanine nucleotide-binding protein G
- Glucagon-like peptide 1 receptor
- Guanine nucleotide-binding protein G
- Probable non-functional immunoglobulin heavy variable 3-16
- Dipeptidyl peptidase 4
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
- Sodium/glucose cotransporter 1
- Gastric inhibitory polypeptide
Sequence:
MKLGSSRAGPGRGSAGLLPGVHELPMGIPAPWGTSPLSFHRKCSLWAPGRPFLTLVLLVSIKQVTGSLLEETTRKWAQYKQACLRDLLKEPSGIFCNGTFDQYVCWPHSSPGNVSVPCPSYLPWWSEESSGRAYRHCLAQGTWQTIENATDIWQDDSECSENHSFKQNVDRYALLSTLQLMYTVGYSFSLISLFLALTLLLFLRKLHCTRNYIHMNLFASFILRTLAVLVKDVVFYNSYSKRPDNENGWMSYLSEMSTSCRSVQVLLHYFVGANYLWLLVEGLYLHTLLEPTVLPERRLWPRYLLLGWAFPVLFVVPWGFARAHLENTGCWTTNGNKKIWWIIRGPMMLCVTVNFFIFLKILKLLISKLKAHQMCFRDYKYRLAKSTLVLIPLLGVHEILFSFITDDQVEGFAKLIRLFIQLTLSSFHGFLVALQYGFANGEVKAELRKYWVRFLLARHSGCRACVLGKDFRFLGKCPKKLSEGDGAEKLRKLQPSLNSGRLLHLAMRGLGELGAQPQQDHARWPRGSSLSECSEGDVTMANTMEEILEESEI
Protein: GTP-binding nuclear protein Ran (EC 3.6.5.-) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) (P62828)
Organism: Rattus norvegicus (Rat)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
Interaction partners:
- Exportin-1
- Exportin-5
- Regulator of chromosome condensation
- Ran-specific GTPase-activating protein
- E3 SUMO-protein ligase RanBP2
- Snurportin-1
- Importin subunit beta-1
- Eukaryotic translation initiation factor 5A-1
- Exportin-T
- Ran GTPase-activating protein 1
Sequence:
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Protein: IS1536, resolvase (O07773)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MACCRNRGMNLAAWAERNGVARVTAYRWFHAGLLPVPARKVGRLILVDELASEAGAQPKTAVYARVSSADQKSDLDRQVARVTSWATAEQIPVDKVVTEVGSVLNGHRRKFPAVLRDLSVTRIVVEHRDRFCRFGSEYVHAALAAQGRELVVVDSAEVDDDLVWDMTEILTSMCARLYGKRAAQNRAKRAVAAAAVDDHEAA
Protein: Glutamate receptor ionotropic, kainate 5 (GluK5) (Glutamate receptor KA-2) (KA2) (Q63273)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1373632, ECO:0000269|PubMed:22509486}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:12954862}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q61626}; Multi-pass membrane protein {ECO:0000255}. Note=Association with GRIK2 is required for its cell membrane localization. {ECO:0000269|PubMed:22509486}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 3
- Glutamate receptor ionotropic, NMDA 2D
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 3B
Sequence:
MPAELLLLLIVAFANPSCQVLSSLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNATTLDINLSQTLANKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCPKEEDHRAKGLGMENIGGIFVVLICGLIIAVFVAVMEFIWSTRRSAESEEVSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKLYSAGAGGDAGAHGGPQRLLDDPGPPGGPRPQAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGTPAEATSPPRPRPGPTGPRELTEHE
Protein: Staphylococcal nuclease domain-containing protein 1 (EC 3.1.31.1) (100 kDa coactivator) (p100 co-activator) (Q78PY7)
Organism: Mus musculus (Mouse)
Function: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (By similarity). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (By similarity). Functions as a bridging factor between STAT6 and the basal transcription factor (By similarity). Plays a role in PIM1 regulation of MYB activity (By similarity). Functions as a transcriptional coactivator for STAT5.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7KZF4}. Nucleus {ECO:0000250|UniProtKB:Q7KZF4}. Melanosome {ECO:0000250|UniProtKB:Q7KZF4}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus. {ECO:0000250|UniProtKB:Q7KZF4}.
Interaction partners:
- Protein LYRIC
- Fragile X messenger ribonucleoprotein 1
- Protein argonaute-2
- Signal transducer and transcription activator 6
- Neutral alpha-glucosidase AB
- Signal transducer and activator of transcription
- Endoribonuclease Dicer
- RNA-binding protein FXR1
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
Sequence:
MASSAQSSGSSGGPAVPTVQRGIVKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDGKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKASKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPGHHLVTVMLSGIKCPTFRRETDGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNLLGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVPPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGDNIQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHMDGANLSVLLVEQALSKVHFTAERSAYYKPLLSAEEAAKQRKEKVWAHYEERPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDISSHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKVHVFYIDYGNREILPSTRLGTLPPAFSTRVLPAQATEYAFAFIQVPQDEDARTDAVDSVVRDIQNTQCLLNVEHLSASCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR
Protein: Snake venom metalloproteinase fibrolase (SVMP) (EC 3.4.24.72) (Fibrinolytic proteinase) (Non-hemorrhagic fibrinolytic metalloproteinase) (VlF) (P83255)
Organism: Macrovipera lebetinus (Levantine viper) (Vipera lebetina)
Function: Has fibrino(geno)lytic activity on the alpha and beta chains of fibrinogen (FGA and FGB). Inhibits human ADP- and collagen-induced platelet aggregation on platelet-rich plasma but does not affect the thrombin-induced aggregation of rabbit washed platelets. Slightly degrades plasminogen.
Subcellular location: Secreted {ECO:0000269|PubMed:10962108}.
Interaction partners:
Sequence:
ERFAPRYIELVIVADHSVATKYNDNVTAILSWVHQLVNNIILFYRDLNVHFTLSAVEVWSNGDLINVQPEATVTLNLFGEWRERDLLNRRMHDNAQLLNNVALDDNTIGLAYDEGMCDPKYSVGIVKDHSAINRMVAATMAHEIGHNLGMNHDGSQCNCGGNGCVMSAVLMQQHSYQFSDCSKDEYQRYLTNHNPQCILNQP
Protein: Superoxide dismutase [Cu-Zn] 1 (EC 1.15.1.1) (Copper/zinc superoxide dismutase 1) (P24704)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20406884}. Nucleus {ECO:0000269|PubMed:20406884}.
Interaction partners:
- Superoxide dismutase 1, chloroplastic
- Superoxide dismutase 1, mitochondrial
- Copper chaperone for superoxide dismutase, chloroplastic/cytosolic
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 3, chloroplastic
- Superoxide dismutase 2, mitochondrial
- Superoxide dismutase 2, chloroplastic
- Catalase-1
- Superoxide dismutase 3
- Catalase-2
Sequence:
MAKGVAVLNSSEGVTGTIFFTQEGDGVTTVSGTVSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPDGKTHGAPEDANRHAGDLGNITVGDDGTATFTITDCQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSLATGNAGGRVACGIIGLQG
Protein: ER membrane protein complex subunit 10 (Hematopoietic signal peptide-containing membrane domain-containing protein 1) (Q5UCC4)
Organism: Homo sapiens (Human)
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 (Probable). Promotes angiogenesis and tissue repair in the heart after myocardial infarction. Stimulates cardiac endothelial cell migration and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling pathways.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000305|PubMed:22119785, ECO:0000305|PubMed:32439656, ECO:0000305|PubMed:32459176}; Single-pass type I membrane protein {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:19570817, ECO:0000269|PubMed:20680400, ECO:0000269|PubMed:28931551}.
Interaction partners:
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 5
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 8
- ER membrane protein complex subunit 9
- ER membrane protein complex subunit 6
Sequence:
MAAASAGATRLLLLLLMAVAAPSRARGSGCRAGTGARGAGAEGREGEACGTVGLLLEHSFEIDDSANFRKRGSLLWNQQDGTLSLSQRQLSEEERGRLRDVAALNGLYRVRIPRRPGALDGLEAGGYVSSFVPACSLVESHLSDQLTLHVDVAGNVVGVSVVTHPGGCRGHEVEDVDLELFNTSVQLQPPTTAPGPETAAFIERLEMEQAQKAKNPQEQKSFFAKYWMYIIPVVLFLMMSGAPDTGGQGGGGGGGGGGGSGR
Protein: RING finger protein 32 (Q9H0A6)
Organism: Homo sapiens (Human)
Function: May play a role in sperm formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11890671}.
Interaction partners:
- Limb region 1 protein homolog
- Nucleolar MIF4G domain-containing protein 1
Sequence:
MLKNKGHSSKKDNLAVNAVALQDHILHDLQLRNLSVADHSKTQVQKKENKSLKRDTKAIIDTGLKKTTQCPKLEDSEKEYVLDPKPPPLTLAQKLGLIGPPPPPLSSDEWEKVKQRSLLQGDSVQPCPICKEEFELRPQVLLSCSHVFHKACLQAFEKFTNKKTCPLCRKNQYQTRVIHDGARLFRIKCVTRIQAYWRGCVVRKWYRNLRKTVPPTDAKLRKKFFEKKFTEISHRILCSYNTNIEELFAEIDQCLAINRSVLQQLEEKCGHEITEEEWEKIQVQALRRETHECSICLAPLSAAGGQRVGAGRRSREMALLSCSHVFHHACLLALEEFSVGDRPPFHACPLCRSCYQKKILEC
Protein: Selenoprotein P (SeP) (Plasma selenoprotein P) (P70274)
Organism: Mus musculus (Mouse)
Function: Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium (By similarity). May supply selenium to tissues such as brain and testis.
Subcellular location: Secreted {ECO:0000269|PubMed:18174160}. Note=Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium. {ECO:0000269|PubMed:18174160}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit E
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS5
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit L
Sequence:
MWRSLGLALALCLLPYGGAESQGQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGYFNISYIVVNHQGSPSQLKHSHLKKQVSEHIAVYRQEEDGIDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEERCGNCNLTSLEDEDFCKTVTSATANKTAEPSEAHSHHKHHNKHGQEHLGSSKPSENQQPGPSETTLPPSGLHHHHRHRGQHRQGHLESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLIFEKSGSAIAUQCAENLPSLCSUQGLFAEEKVTESCQCRSPPAAUQNQPMNPMEANPNUSUDNQTRKUKUHSN
Protein: Protein phosphatase 1D (EC 3.1.3.16) (Protein phosphatase 2C isoform delta) (PP2C-delta) (Protein phosphatase magnesium-dependent 1 delta) (p53-induced protein phosphatase 1) (Q9QZ67)
Organism: Mus musculus (Mouse)
Function: Involved in the negative regulation of p53 expression. Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Mediates MAPK14 dephosphorylation and inactivation (By similarity). Is also an important regulator of global heterochromatin silencing and critical in maintaining genome integrity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15297}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15297}.
Interaction partners:
- Serine/threonine-protein kinase Chk2
- Serine-protein kinase ATM
- Runt-related transcription factor 2
- Serine/threonine-protein kinase Chk1
- Cellular tumor antigen p53
- Core-binding factor subunit beta
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPAAEDKPAPVPRRALGLPATPTLAGVGPSEKGPAAARDPAPDAAASLPAGRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHSGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGKFVVSPEPDTSVHTLDPRKHKYIILGSDGLWNMVPPQDAISMCQDQEEKKYLMGEQGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELFLNLTDSPTYNSQETCVMTSSPSSTPPIKSPEEDAWPRLSSKDHIPALVRSNAFSEKFLEVPAEIARGNIQTVVMTSKDSETLEENCPKALTLRIHDSLNNTLSVGLIPTNSTNTIMDQKNLKMSTPGQMKAQEVERTPPANFKRTLEESNSGPLMKKHRRNGLSRSSGAQASSLPTASQRRHSVKLTLRRRLRGQRKMGNPLLHQHRKTVCVC
Protein: Glypican-4 precursor (Knypek) (B3DJ94)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}.
Interaction partners:
Sequence:
MKMIVVFTVCMSVVVLASAQADQKSKNCNEVRTAYSSKGFNVNDVPNKGVQGAHLKVCPQGFSCCTLEMEEKLSQLSRVDLKVPVHQLSSNLQSTFTQRHRHFDQFFRELLDNAEKSLNHMFVRTYGLMYVKNKELFEGFFSDLRRYYSHGSSEVNLDDMLAEFWSELLERMFRLVNVQYEFSDSYMECVSRHTDQLKPFGDVPRKLRLQLTRSFIAVRAFTRGLTLMPDVVRKVSTVSASPSCVRASMKMLYCPYCSGQVALKPCKNYCLNVMRGCLANQADLDTEWNNFLDSMLGLAERLEGPFNFESVVDPIDVKISDAIMNMQENSMQVSQKVFQGCGQPKLSMGFRSRRSAKDSGFPGRFRPYSPEARPTTAAGTTLDRLLTDVKKKLKHAKKFWSTLPDTVCVGERIAPSDDCWNGTAKSRYESVVMSSGLANQVSNPDVEVDITKPDMVIRRQIAVLKEMTSWLKAAYTGNDISFTSDDAGSGEESGSGCDSPSCEGDGDIYFSTPAPGKPRILKTPEVEQASSGTRLAPCSLALALASLLLTLLTLQTR
Protein: Heavy metal-associated isoprenylated plant protein 36 (AtHIP36) (Q84J88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 9
- Glucan endo-1,3-beta-glucosidase 8
- Beta-glucosidase 8
- Heavy metal-associated isoprenylated plant protein 39
- Heavy metal-associated isoprenylated plant protein 1
- Protein STRICTOSIDINE SYNTHASE-LIKE 3
- Phosphatidate phosphatase PAH2
Sequence:
MDLGTEIKSDTRQEEQRHVFEDYPEPLRYTTWVLRVSIHCEGCKRKIKKILSKIDGVYTTNIDVKQQKVTVIGNVEPEILIKKIMKAGRHAELWPTSMENNINNDCNYQKKPKKDNEETSGDEDDDENNNNNNGGGDVGGGGGGGGGNFDQVKQVVTFVNGQLQPQGDGAPKKKKKKKKKKKSLGNTTVVMEGGGGGGGGGGPPQNDGPPETVIYSAPQDHHIIHGPPPHLHHHQQQNHPYPTVHSPPRHHPQQMYGPGPGLPPPSFYHTQPQTAPSYTVSYNTVHGPINNGGNETASYYTAPPSHPTSYYSYEYVDTGYESPPPEFYSYRSQPSESFESLSEGNPNSCCVM
Protein: Protein FAM174C (Q9BVV8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGPRVLQPPLLLLLLALLLAALPCGAEEASPLRPAQVTLSPPPAVTNGSQPGAPHNSTHTRPPGASGSALTRSFYVILGFCGLTALYFLIRAFRLKKPQRRRYGLLANTEDPTEMASLDSDEETVFESRNLR