wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger CCHC domain-containing protein 12 (Smad-interacting zinc finger protein 1) (Q9CZA5)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator in the bone morphogenetic protein (BMP)-signaling pathway. It positively modulates BMP signaling by interacting with SMAD1 and associating with CBP in the transcription complex. It contributes to the BMP-induced enhancement of cholinergic-neuron-specific gene expression.
Interaction partners:
- Paraneoplastic antigen-like protein 8A
Sequence:
MASILSRLGSSRGQNSPLPPWAHSMLRSLGRSLGPLMASMAERNMRLFSGRAEPAQGEETFENWLSQVTGVLPDWHMPEEEKVRRLMRTLRGPAREVMRLLQAANPGLDVEDFLRAMKLVFGESESSVTAHSKFVNTVQEHGEKPSLYVIRLEVQLQNAIQAGVFAEREANQARLHQLLVGAEMSTDLRFRLKNLLRVYANEPERLPNFLELIRMIREEEEWEETFINPKRPRRAESVMERALSPMAFQSSPPIMISSIDCNVIEIDDSPDDSDEDVILVEPEDPPLPSSSASSFLGRAVSEDQVLVIESPNIFEIQAPSTSSGAGRKNNRGFGELRRARKRKHTIHCSHCGEEGHSKETCDNESDKGQVFENLIITLQELTHAEERARGAPGEPIGLSEPQ
Protein: Allograft inflammatory factor 1 (AIF-1) (Ionized calcium-binding adapter molecule 1) (Protein G1) (P55008)
Organism: Homo sapiens (Human)
Function: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O70200}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O70200}; Peripheral membrane protein {ECO:0000250|UniProtKB:O70200}; Cytoplasmic side {ECO:0000250|UniProtKB:O70200}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:O70200}. Note=Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis. {ECO:0000250|UniProtKB:O70200}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Glial fibrillary acidic protein
- RNA binding protein fox-1 homolog 3
- Macrosialin
- Macrophage colony-stimulating factor 1 receptor
- Interleukin-1 beta
- Complement C1q subcomponent subunit A
- Tumor necrosis factor
- Integrin alpha-M
- T-lymphocyte activation antigen CD86
Sequence:
MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKEKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKKLIGEVSSGSGETFSYPDFLRMMLGKRSAILKMILMYEEKAREKEKPTGPPAKKAISELP
Protein: Hadley, isoform B (A8JR58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fra mauro, isoform F
Sequence:
MNRTSLSSGSTSRRLPALLFVLLLCLVARTNGRPSQEDESDLAIIPPDADNVEIHKVKIVNGVMQEDHPVIMYKEDFVSEDYDPTKSETNPSHHKKHKRTRLHHAKQVTGTEKKEDQILFDILPDKPIVLEEDLKALPHSKVGAAQLAEPIKEEWLAKHPKKYHSRQRRQAPVSFEKVLQYYYGTPEIKFVSPLTYTHFRISVKGKKPHLVGPPNRRNQGQENIPTPDSVDSRGEFDLIHNSNQADADFSIYNRSSTTTARPIFQINDSDFVTSAPSWRPSNSIRRPPPTRSPVVGLPTMRPNARPVPQTGGVDSEPKVSRCVWAIVNCCTGESKKVRYNCFEEFGCHGAFWDINPCADEGVKQAELVPLVGFSPPVFAPSMPGRRPSSRKGAFQFPQDIGYQENSKCQRASKLCCSQRNIGSQYECFHHHGCSENIATIISTCS
Protein: Immunoglobulin superfamily member 8 (C9J8Z4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGALRPTLLPPSLPLLLLLMLGMGCWAREVLVPEGPLYRVAGTAVSISCNVTGYEGPAQQNFEWFLYRPEAPDTALGIVSTKDTQFSYAVFKSRVVAGEVQVQRLQGDAVVLKIARLQAQDAGIYECHTPSTDTRYLGSYSGKVELRVLPDVLQVSAAPPGPRGRQAPTSPPRMTVHEGQELALGCLARTSTQKHTHLAVSFGRSVPEAPVGRSTLQEVVGIRSDLAVEAGAPYAERLAAGELRLGKEGTDRYRMVVGGAQAGDAGTYHCTAAEWIQDPDGSWAQIAEKRAVLAHVDVQTL
Protein: Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Coagulation factor XIIa light chain] (D3ZTE0)
Organism: Rattus norvegicus (Rat)
Function: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Antithrombin-III
- Plasma kallikrein
- Plasminogen
- Kininogen-1
- Plasma protease C1 inhibitor
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Coagulation factor XI
- WD repeat-containing protein 90
- Coagulation factor IX
- Histidine-rich glycoprotein
Sequence:
MTALLFLGSLLMSLDLTLSAPPWKSKEFKDGAGDPSVVLTVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYCLEPKKVKDHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQREKCFESQLLKFFHENEIWFRTGPGGVARCQCKGPQAVCKLLTSQVCRVNPCLNGGTCLLVEDHRLCHCPAGYAGPFCDLDLKATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDNDTRPWCYVWSGDRLSWDYCDLEQCQMPTLTSPVSPESHDMLKPRPPILQSSPRDSTRNQNVVSRTSTVVCGQRFRKRLSSLRRVVGGLVALPGSHPYIAALYWGDSFCAGSLIDPCWVLTAAHCLQKRPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLHEGFSSKTYQHDLALLRLRGRKNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLDRCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQEHTAF
Protein: N-acylneuraminate cytidylyltransferase B (EC 2.7.7.43) (CMP-sialic acid synthetase 2) (H9BFW7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the activation of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) to cytidine 5'-monophosphate 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (CMP-KDN), a substrate required for the addition of sialic acid. Also has weak activity towards N-acetylneuraminic acid (NeuNAc) and N-glycolylneuraminic acid (Neu5Gc).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22351762}.
Interaction partners:
- exo-alpha-sialidase
- Uncharacterized protein
- Alpha-2,8-sialyltransferase 8E
- Sialidase-1
- exo-alpha-sialidase
- ST3 beta-galactoside alpha-2,3-sialyltransferase 3a
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-galactoside alpha-2,6-sialyltransferase 2
Sequence:
MEGGRCAQVSSVPASPSSGHRHRAALILARGGSKGIPLKNIKNLAGVPLIGWVLRAALDSDVDSVWVSTDHDEIERVAKLWGAKVHRRSPEVSKDSSSSLETIQEFIRLRPEVDVICHIQATSPCLHPHHINEALQKITHQGFSYVLSVVRRHQFRWEELQENEDRNPKSFNINVAQRPRRQDWPGELYENGSFYFSTRKAWESGLTELGRIAYYEMPPEFSVDIDVDIDWPVAEQRVLRFGYFGREENAAVRLFLCKVSGCLTNGQIYMSVSGEDLVTINARDVAGIQMLQKENIEVILISSVNEPLSRGVLEKVSQRAGCGLSFTEQRNALEMQKLMDKRKLHWDQVAFMGSESEDVEIMSQAGLNGVPSDAPVAELIAAKYTCQRAGGHGAVREFAEYILSMKRKSSREENHERIDKHNF
Protein: Uncharacterized protein (Q6EUT2)
Organism: Caenorhabditis elegans
Interaction partners:
- Neuronal acetylcholine receptor subunit eat-2
- Innexin eat-5
- Uncharacterized protein
Sequence:
MRSLERIVETRIELLEWDSKETKEDCARCRALDCDIIFALLFTIVIACLLVLIMVFWLKGVLQYEDVYTRLLRDRGSV
Protein: F-box protein At3g54460 (Q9M1I1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative F-box protein At3g25750
- At3g29270
- F-box protein SKIP5
- Chromatin structure-remodeling complex protein SYD
- RuvB-like protein 1
- Probable zinc transporter 12
- Actin-related protein 5
- Actin-related protein 4
- MLO-like protein 1
- Protein EIN6 ENHANCER
Sequence:
MADDHKLCGFLCTVLSVDSPDLLQSGSSCFIFNDGSVTGFKSENGLILSLTNPISNLQSLISSKGDHDVENSGTIEDGRLETPQKRRKCVEGESSGKRKTPKSKRRVLSGSKEKTVQGRKRVKSIGMVNGSISVVQQLHALVANKCLKIICRVVKVDKGENGEERAVVLVDVYLPIELWSGWQFPKSQATAAALFKHLSCDWGLRVSILDGKSIWEEANGRIKAIWDLSDCHVFDCKLLCNAPNSPKRRLFKLHEIFKSLPSPGNHDVSYSSRVLPSTDSCVSGVWDLSDDVLISILMKLDTKDLFSIAAVCRLFRSLTSLIVPCMNLKLFPHQQAAVGWMLERERKAEVSSHPLYLSFDTEDGFSFYVNAVTGDIITEAAPMVKDFRGGMFCDEPGLGKTITALSLILKTQGTMADPPEGLPIVWCTHKSDKKCAYYEYTSDQFTSNSMSAVKRFQSPSSCRNQVSFEAFRPLLESKSLPFKQARLMDPDDQTLESKNSNFENEFETHIPASLDLKAQCRKSLGNVRKNLLPAYNGASELSEVMEAKRISNWKKCGMITGCKRKGLTDSDVESDIWMQCDSCSKWRRIIDEGVSVTGSAWFCSNNNDPAYQSCNDPEELWDKSQPIKYLQGFYTKGASGEESDNISFFTSVLREHKSSVSSTVKKALIWLAKLPLEKLSQMETVGLPGPVLGLKLDALGFQRIFRAFGLKSRVEKGVTKWFYPKFLENLVFDVPALKVALCQPLDTFRLYLSKATLIVVPTNLVNHWLTQIQKHVCSDQLRILVWADHIELSPHSLAWDYDVVITTFSRLSAEWNPRKKSPLIQVHWLRVMLDEGHTLGSSVSLTNKFQMAVSLTACNRWLLTGTPTPNTPNSQLSHIQPLLKFLHEEVYGENPKFWEAGILRPFEAEMEEGRLRLLQLLQRCMISSRKKDLQMIPPCIKKVTYLNFLPGHARSYNELVETVRRNILLADWNDPSHVESLLNSKQWKFRSITISNVRLSCCVAGHIKMTDAGHDIKETMDALLENDLDLWTEEYSFIQDSLIGGCNCKRCGEWCRLPVITPCRHLLCLDCVALDSERCTISGCGYLYEMQTPETLARPENPNPKWPVPKDLIELQPSYKQDDWNPDWQSTSSSKVSYLVDRLRKLHEGNKKSILSFNKTDNDNLEDNPPGTSEAFLGKELHGQDCGSQMVFVDKVLIFSQFLEHIHVIEQQLTTAGIKFGKMYSPMQSYNKMKALAMFQNDADCMALLMDGSGALGLDLSFVTHVFLMEPIWDKSLEEQVISRAHRMGAKRPIFVETLTMRGTIEEQMMRFLEDAEKSDRLLSGDYIEAKQETTRSRRTLHDLVESNYLSHLSFVRSDGKMEFAASQLAGLKDHQLA
Protein: Nickel and cobalt resistance protein CnrY (P56621)
Organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Function: Nickel and cobalt resistance proteins CnrA, CnrB, CnrC CnrH and CnrR may be involved in the regulation of CNR.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10671463}; Single-pass membrane protein {ECO:0000269|PubMed:10671463}.
Interaction partners:
Sequence:
MADVEEWLTHARKVTQEASIGVDVTSIQECISAEPAQRVLVARRDAWRAICCAAFAALVAFAAINRVATIMLEKPAPTWVATPSAASPFGLLIGK
Protein: Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11) (Q9D8C6)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MATYSLANERLRALEDIEREIGAILQNAGTAILELSKEKTNERLLDRQAAAFTTSVQHVEAELSAQIRYLTQVATGQPHEGSSYSSRKDCQMALKRVDYARLKISDVARTCEQMLEN
Protein: Beta-1,3-xylanase XYL4 (EC 3.2.1.32) (Beta-1,3-xylanase) (D5MP61)
Organism: Vibrio sp
Function: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydrolyze beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or p-nitrophenyl-beta-xyloside.
Interaction partners:
Sequence:
MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKSNWQQEIAKGQYINHSETLFETLGYGSTGGGDNGGGDNGGTNPPEPCNEEFGYRYVSDSTIEVFHKNNGWSAEWNYVCLNGLCLQGEIKNGEYVKQFDAQLGSTYGIEFKVADGESQFITDKSVTFENKQCGSTGTPGGGDNGSGGDNGGDNGSGGDNGSGGGTDPSQCSADFGYNYRSDTEIEVFHKDLGWSASWNYICLDDYCVPGDKSGDSYNRSFNATLGSDYKITFKVEDSASQFITEKNITFVNTSCAQ
Protein: Sad1 and UNC84 domain containing 1 (E9PHI4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCDDCKGKRHLDAHTAAHSQSPRLPGRAGTLWHIWACAGYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK
Protein: Glutathione S-transferase A2 (EC 2.5.1.18) (GST HA subunit 2) (GST class-alpha member 2) (GST-gamma) (GSTA2-2) (GTH2) (P09210)
Organism: Homo sapiens (Human)
Function: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase A1
- Glutathione S-transferase A4
- Glutathione S-transferase A5
- Cytochrome P450 1A1
- Glutathione S-transferase A3
- Epoxide hydrolase 1
- Cytochrome P450 1A2
- Cytochrome P450 3A4)
- Glutathione reductase, mitochondrial
- Cytochrome P450 2E1
Sequence:
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
Protein: Islet cell autoantigen 1 (E9PDL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRYAQDKSVVNKMQQKYWETKQAFIKATGKKEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRNPLCRFHQEVETFRHRAISDTWLTVNRMEQCRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESFKGYQPYEFTTLKSLQDPMKKLVEKEEKKKINQQESTDAAVQEPSQLISLEEENQRKESSSFKTEDGKSILSALDKGSTHTACSGPIDELLDMKSEEGACLGPVAGTPEPEGADKDDLLLLSEIFNASSLEEGEFSKEWAAVFGDGQVKEPVPTMALGEPDPKAQTGSGFLPSQLLDQNMKDLQASLQEPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHELLNA
Protein: Heme-binding-like protein At3g10130, chloroplastic (Q9SR77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
- 1-aminocyclopropane-1-carboxylate oxidase 3
- UDP-glycosyltransferase 72B3
- Protein disulfide-isomerase like 2-2
Sequence:
MMMISSSSITSSLSLLSSSPEKLPLINPIQRCPITYSGFRTASVNRAIRRQPQSPAVSATESRVSLVLALASQASSVSQRLLADLAMETAKYVFPKRFDSSTNLEEAFMSVPDLETMNFRVLFRTDKYEIRQVEPYFVAETIMPGETGFDSYGASKSFNVLAEYLFGKNTIKEKMEMTTPVVTRKVQSVGEKMEMTTPVITSKAKDQNQWRMSFVMPSKYGSNLPLPKDPSVKIQQVPRKIVAVVAFSGYVTDEEIERRERELRRALQNDKKFRVRDGVSFEVAQYNPPFTLPFMRRNEVSLEVENKED
Protein: Transmembrane protein 225 (Q9TZ35)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRKVGAIGVLILLGFIFNAVSVFTDSWLVWSYAKIQVTRGIVPYSSSEPTWLAAASWMMFISFGLFFPVILIYLHASHKVYHHGCCHSIRHNFNGISLLCSLIVILQAVAFILMAANASDYYGSLGYSAYFALVSGILTTIAMSLSGHVSRHDCH
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase 25 kDa subunit) (SPase 25 kDa subunit) (Q15005)
Organism: Homo sapiens (Human)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q28250}.
Interaction partners:
- Signal peptidase complex subunit 3
- Signal peptidase complex subunit 1
- Signal peptidase complex catalytic subunit SEC11C
- Signal peptidase complex catalytic subunit SEC11
- Translocon-associated protein subunit gamma
- Protein transport protein Sec61 subunit beta
- Alkaline phosphatase, tissue-nonspecific isozyme
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Calcium load-activated calcium channel
- Protein transport protein Sec61 subunit gamma
Sequence:
MAAAAVQGGRSGGSGGCSGAGGASNCGTGSGRSGLLDKWKIDDKPVKIDKWDGSAVKNSLDDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIFLVAHRKDPTGMDPDDIWQLSSSLKRFDDKYTLKLTFISGRTKQQREAEFTKSIAKFFDHSGTLVMDAYEPEISRLHDSLAIERKIK
Protein: D-spinophilin, core domains (Q9GQA3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
DIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSSILENKIRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVCSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLASRGGLANRQLPSANGNSSTSNGAAVDLGQLSNGNLLKRSRSNSRSSDCTLDDTDEEEEREGSALNLAGAPVAHETISLSNGNSHLLANVNNLLQHHPPAMATVIATPSNGHLGTTTPILLNSTSSASSSSSNQSTAREAQINQLYAQVHKDPSKQQHQQQQQQQQQAQAVTTSIPSIFKNALGSPADNGLNDFHRGSMTTFGTGPATSSNRDLNSSYDSILGSNDKLAENDPAESWMYPSRRRVAPNGSKVPLPGSSFTDQLNQALSDRERRLGDGSSRHSSDDYTEINKSQSAAAINCKTLINEIRQAVNEAQPKGALAAAAPPANPAAAVRPHHRSASPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Major urinary protein 18 (A0A096MK41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLLLLLLCLGLTLVCGHAEEASFERGNLDVDKLNGDWFSIVVASNKREKIEENGSMRVFMQHIDVLENSLGFKFRIKENGECRELYLVAYKTPEDGEYFVEYDGGNTFTILKTDYDRYVMFHLVNFKNGETFQLMELYGRTKDLSSDFKKKFAKLCEAHGITRDNIIDLTKTDRCLQARG
Protein: Nigrocin-2GRc (Grahamin-2) (P85070)
Organism: Odorrana grahami (Yunnanfu frog) (Rana grahami)
Function: Antimicrobial peptide active at least against the Gram-positive bacterium S.aureus but with otherwise unclear activity spectrum. Lacks hemolytic activity against rabbit or human erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:16487561}.
Interaction partners:
Sequence:
MFTMKKSMLLLFFLGTISLSLCEQERNADEEERRDEEVAKMEEIKRGLLSGILGAGKNIVCGLSGLC
Protein: DnaJ homolog subfamily B member 2 (Heat shock 40 kDa protein 3) (Heat shock protein J1) (HSJ-1) (P25686)
Organism: Homo sapiens (Human)
Function: Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family. In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins. Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes. Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins.
Subcellular location: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:12754272, ECO:0000269|PubMed:21625540}. Nucleus {ECO:0000269|PubMed:12754272}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12754272}; Lipid-anchor {ECO:0000269|PubMed:12754272}; Cytoplasmic side {ECO:0000269|PubMed:12754272}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 6
- GrpE protein homolog 1, mitochondrial
- Heat shock 70 kDa protein 1-like
- Stress-70 protein, mitochondrial
- Heat shock-related 70 kDa protein 2
- Heat shock protein 105 kDa
- Heat shock protein beta-8
Sequence:
MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTSRSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPAGGREAQHRRQGRPKAQHQDPGLGGTQEGARGEATKRSPSPEEKASRCLIL
Protein: Cold shock domain-containing protein E1 (N-ras upstream gene protein) (Protein UNR) (O75534)
Organism: Homo sapiens (Human)
Function: RNA-binding protein involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Required for efficient formation of stress granules.
Subcellular location: Cytoplasm. Cytoplasm, Stress granule {ECO:0000305|PubMed:29395067}. Cytoplasm, P-body {ECO:0000269|PubMed:32354837}.
Interaction partners:
- Polyadenylate-binding protein 1
- Heterogeneous nuclear ribonucleoprotein Q
- Serine-threonine kinase receptor-associated protein
- Y-box-binding protein 1
- Heterogeneous nuclear ribonucleoprotein U
- Insulin-like growth factor 2 mRNA-binding protein 1
- Heterogeneous nuclear ribonucleoprotein D0
- ATP-dependent RNA helicase A
- Polyadenylate-binding protein-interacting protein 1
- Ras GTPase-activating protein-binding protein 1
Sequence:
MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAVKLVKIKQEILPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTPEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQGVVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDPLPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNISTDRRDKLERATNIEVLSNTFQFTNEAREMGVIAAMRDGFGFIKCVDRDVRMFFHFSEILDGNQLHIADEVEFTVVPDMLSAQRNHAIRIKKLPKGTVSFHSHSDHRFLGTVEKEATFSNPKTTSPNKGKEKEAEDGIIAYDDCGVKLTIAFQAKDVEGSTSPQIGDKVEFSISDKQRPGQQVATCVRLLGRNSNSKRLLGYVATLKDNFGFIETANHDKEIFFHYSEFSGDVDSLELGDMVEYSLSKGKGNKVSAEKVNKTHSVNGITEEADPTIYSGKVIRPLRSVDPTQTEYQGMIEIVEEGDMKGEVYPFGIVGMANKGDCLQKGESVKFQLCVLGQNAQTMAYNITPLRRATVECVKDQFGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (B7Z0E0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Isocitric dehydrogenase subunit beta
- Probable isocitrate dehydrogenase subunit alpha, mitochondrial
- Cytoplasmic aconitate hydratase
- Cytoplasmic aconitate hydratase
- Probable citrate synthase, mitochondrial
- Citrate synthase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase
Sequence:
MFALRRTAAMMTSVHRQPHLSQAVFRANFAISAADPKTHKISMDNERMSAVSEHSSVVCSPEQMAQKIKAGPVVDVLGDEMTRIIWDSIKSQLILPFLDIELHTYDLGIENRDKTEDQVTIDCAEAIKKYNVGIKCATITPDEKRVEEFNLKKMWKSPNGTIRNILGGTVFREAIICKNVPRLVTGWQKPIVIGRHAHADQYKAVDYVVPGPGKLTLTWKGTDGQVIDEVINDFKGPGIALGMFNTDDSIVDFAHASFKYALDRKLPLYMSTKNTILKKYDGRFKDIFEDLYNKQYKKEYEAAGIWYEHRLIDDMVAYAMKSEGGFVWACKNYDGDVQSDSVAQGYGSLGLMTSVLLCPDGKTVEAEAAHGTVTRHFRFYQQGKETSTNPIASIFAWTRGLLHRAKLDNNEPLKQFADTLEQVCIDTIESGAMTKDLAICIKGNINAVTRRDYQETFEFINTLAKNLEGALAKNAVAAK
Protein: At2g45180 (Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein) (Expressed protein) (Putative proline-rich protein) (Q42044)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g10300
- Pentatricopeptide repeat-containing protein At1g03540
- Curculin-like
- Cytochrome b561 and DOMON domain-containing protein At4g12980
- GDSL esterase/lipase At5g62930
- GDSL esterase/lipase At1g09390
- Tetraspanin-18
- Copper ion binding protein
- Filament-like plant protein 2
- GDSL esterase/lipase LIP-4
Sequence:
MASKALAVTALLITLNLLFFTFVTSTKCPPTTPKPPKTPKSPKKAPAVKPTCPTDTLKLGVCADLLGLVNVVVGSPPKTPCCTLLQGLANLEAAVCLCTALKANVLGINLNVPIDLTLLLNYCGKKVPHGFQCS