wanglab/gogpt-training-data huggingface dataset:
Protein: Histone acetyltransferase GCN5 (EC 2.3.1.48) (Q9VTZ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SAGA complex subunit Spt3
- Transcriptional adapter 2b
- Transcriptional adapter 1-2
- SAGA factor-like TAF6
- SAGA-associated factor 29kDa
- Protein will decrease acetylation
- Transcriptional adaptor 3, isoform C
- Transcriptional adapter 2A
- Transcription-associated protein 1
- Transcription initiation factor TFIID subunit 12
Sequence:
MSGGPSITIKSQPIDGNNTGNAAAQQQQQAANGAATAGASGAAGSAQNPGHGGAASGAGSVPAEGTRQNSLQRIQQRKQKVFNLPVPQKLAKLSMYSACQSEGCRCTGWKTPQENRHRDVESSYCPEFNEECRNTSCRHSLRSHIAHLDNISSSSMNELLGAIIDMENLFMSMQRVEDEDTKKVYQYLFRLLRQCVLTRQQAVIRGPLGDPPFETPCITKAVLSLVFYKYNHLSTPELQTMTEVAKTFLNFLNHYNFESPSTRRGDLTHEDASNYKINYTRWLVFCHVPAFCNSLRQCETSLVFGRTLLRTVFQCMSQQLKKKCISERDRFPEDKRSIITLMPKFLETLRAELLKDDSPIWDTSYRPSNSFVIQQRKRNQEVANVPIGPSAASIGGNKRTSVGEPLHKRIKKEPTDRPSSENLDDLPADVVMRAMKSVSESKTTNKAEILFPVNVSRDENVKAEEQKRAIEFHVVGNSLTKPVDKQTVLWLLGLQLVFAYQLPEMPREYISQLVFDTKHKTLALIKENQPIGGICFRPFPSQGFTEIVFCAVTMSEQVKGYGTHLMNHLKDYSIQRGIKHLLTFADCDAIGYFKKQGFSKDIKLARPVYAGYIKEYDSATLMHCELHPSIVNTQFIAVIRSQSEILKELIAQRHNEVQKVRPGLTCFKEGLPVIPVESIPGLREIGWKPQNRPARSSRPLEESTDPEKLATSFASVLQSVRQHTTAWPFLRPVTAAEVPDYYDHIKYPMDLKTMGERLKKGYYQTRRLFMADMARIFSNCRFYNSPDTEYYRCANSLERYFQTKMRELGLWDK
Protein: Candida glabrata strain CBS138 chromosome D complete sequence (Q6FVX6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- pyridoxal kinase
- pyridoxal kinase
- Candida glabrata strain CBS138 chromosome D complete sequence
- pyridoxal 5'-phosphate synthase
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MSKIQQIRNTIRSIGTGYGLMSLTWKAVPTEQEQAFGAMKKAIDLARASNHIAFFNVGEFYGKDRVNLHLVRDFFKKYPELREHVIISCKGAMDLSDLHAMGKYDDVVKSVEACTEAIGGFIEIFEPARLDMDICKEGEVYPKESIQALKDLCDKGVIGAISLSEVDEKVINAVAADFGEYLACVEVELSLFCDDILHNGVAKACSDHNMAIICYSPLGKGILTGQITKNSDIPDGDFRKMLKSFSDEALQHNQEIVSFIRTEIIEKRPAGKEITLPQVALAWIKHWNGDSSYPNAKFIPIPSGSSAARVAENFDEEKSTISDEEFKKLNKYAFNFKPVGARYEFVSDPTKH
Protein: Pre-mRNA 3'-end-processing factor FIP1 (hFip1) (FIP1-like 1 protein) (Factor interacting with PAP) (Rearranged in hypereosinophilia) (Q6UN15)
Organism: Homo sapiens (Human)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex.
Subcellular location: Nucleus.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 2
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage stimulation factor subunit 3
- WD repeat-containing protein 82
- Cleavage stimulation factor subunit 2
- Poly
Sequence:
MSAGEVERLVSELSGGTGGDEEEEWLYGGPWDVHVHSDLAKDLDENEVERPEEENASANPPSGIEDETAENGVPKPKVTETEDDSDSDSDDDEDDVHVTIGDIKTGAPQYGSYGTAPVNLNIKTGGRVYGTTGTKVKGVDLDAPGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIRMGLEVIPVTSTTNKITAEDCTMEVTPGAEIQDGRFNLFKVQQGRTGNSEKETALPSTKAEFTSPPSLFKTGLPPSRNSTSSQSQTSTASRKANSSVGKWQDRYGRAESPDLRRLPGAIDVIGQTITISRVEGRRRANENSNIQVLSERSATEVDNNFSKPPPFFPPGAPPTHLPPPPFLPPPPTVSTAPPLIPPPGFPPPPGAPPPSLIPTIESGHSSGYDSRSARAFPYGNVAFPHLPGSAPSWPSLVDTSKQWDYYARREKDRDRERDRDRERDRDRDRERERTRERERERDHSPTPSVFNSDEERYRYREYAERGYERHRASREKEERHRERRHREKEETRHKSSRSNSRRRHESEEGDSHRRHKHKKSKRSKEGKEAGSEPAPEQESTEATPAE
Protein: Tumor protein D52 (Protein N8) (P55327)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein MAL2
- Tumor protein D53
- Tumor protein D54
- Tumor protein D55
- Small ribosomal subunit protein uS2m
Sequence:
MDCREMDLYEDYQSPFDFDAGVNKSYLYLSPSGNSSPPGSPTLQKFGLLRTDPVPEEGEDVAATISATETLSEEEQEELRRELAKVEEEIQTLSQVLAAKEKHLAEIKRKLGINSLQELKQNIAKGWQDVTATSAYKKTSETLSQAGQKASAAFSSVGSVITKKLEDVKNSPTFKSFEEKVENLKSKVGGTKPAGGDFGEVLNSAANASATTTEPLPEKTQESL
Protein: Sfi1 spindle body domain-containing protein (Q382Z2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIEPGTLESGCGRSLWKLNDNTAESAPPPGRYLRITDRRLRMLSALVRDLRFEKLLEAAILAQSYWRGILSRRENKHRLPMLQERMRQREAVELIQHAYRNHLATRGPIKEKHELRAHRLLVQRLVVIQRHLRGRQSVVEERNRGLGVIVQLNEAILEARRRVAASIVIQSSWRMCAVRIRILRLLAATIRVQSVWRGHVGRVEARERRVRERLRKQDRLAVLLRHVYPVQKRWRGVLAIRKAKEYVEGLKKNVVAYLEEQERIVDAMWGRFKCVANVELSVLKILDVLRAYRSREECAKMYPSMLTRRRFLLRIVWKKRATHIAGIMREQQLTKWMLQRRREEVADAVLLLQCAVRRWFAQRKSMALRRALDWTHVCARKIQSMYKRQMGRRMFLEAKMATKLREEQRMISQLRHYCASKIQATWRMFTVWHENKDYLHFLHHGRHKYATTIRNAWITYRERQQKKVIIGMRLMEHQQKQSAQEQLLSVLRIQAMVRMFLVRSRMLRDGVQLRPTLAKLHRSARSIQMSWRRHAAYEYVSQLRFSRAYYDQHKVNMESLHTYATMIQSLVRAKVINPWLVAVRELELEQASTEEKERRREKMLKTYALFTKENMFPGAGNRLSACGPEALVAGGRTSLDTGSFVTPLRNTGTSYISEGPCSFSVKLCETCVLPTRSVSRSCLSGTSQSADICAQKGDEHQSLDTTSLHQVDGQRSPSSDQLDVVKSCTANAVHPPLRNMDTRSTTILGSLSAIFSGRPDLEGSADGRRTSAGLRGRETSHSSCPAGSEFASVTTSEYSSSLCYDPVVLAAVVALIQRCGRGFLSRASTRRSLQKSDRWLAAVDIQRMWRGFCARQLVEVYYEFYTEEVEVAAAE
Protein: Chymotrypsinogen A (EC 3.4.21.1) [Cleaved into: Chymotrypsin A chain A; Chymotrypsin A chain B; Chymotrypsin A chain C] (P00766)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
Protein: Intermembrane phospholipid transport system binding protein MlaB (P64602)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaB plays critical roles in both the assembly and activity of the complex. May act by modulating MlaF structure and stability.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:19383799}.
Interaction partners:
- Intermembrane phospholipid transport system binding protein MlaD
- Intermembrane phospholipid transport system ATP-binding protein MlaF
- Intermembrane phospholipid transport system permease protein MlaE
- Intermembrane phospholipid transport system binding protein MlaC
- Intermembrane phospholipid transport system lipoprotein MlaA
- Acid stress protein IbaG
Sequence:
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLHLIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR
Protein: H-2 class I histocompatibility antigen, D-K alpha chain (H-2D(K)) (P14426)
Organism: Mus musculus (Mouse)
Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MGAMVPRTLLLLLAAALAPAQTRAGPHSLRYFETVVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRDEPRVRWMEQEGPEYWERETQIAKGNEQSFRVDLRTLLRYYNQSEGGSHTIQRLSGCDVGSDWRLLRGYEQFAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERDRAYLEGTCVEWLRRYLELGNATLLHTDSPKAHVTHHPRSKVEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAVAIIGAVVAFVMMMRRNTGGKGGDYTLTPGSQSSEMSLPDCKA
Protein: Ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase 3) (EC 3.6.1.5) (CD39 antigen-like 3) (Ecto-ATP diphosphohydrolase 3) (Ecto-ATPDase 3) (Ecto-ATPase 3) (Ecto-apyrase 3) (HB6) (O75355)
Organism: Homo sapiens (Human)
Function: Has a threefold preference for the hydrolysis of ATP over ADP.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BFW6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleoside triphosphate diphosphohydrolase 6
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Nucleoside diphosphate phosphatase ENTPD5
- Soluble calcium-activated nucleotidase 1
- Ectonucleoside triphosphate diphosphohydrolase 4
- CTP synthase 2
- CTP synthase 1
- Adenosine kinase
- Ribonucleoside-diphosphate reductase large subunit
Sequence:
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTMGHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQPKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARSYCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRLPIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Protein: Putative E3 ubiquitin-protein ligase XBAT35 (EC 2.3.2.27) (Ankyrin repeat domain and RING finger-containing protein XBAT35) (Protein XB3 homolog 5) (RING-type E3 ubiquitin transferase XBAT35) (Q4FE47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Interaction partners:
- E3 ubiquitin-protein ligase XBAT33
- Putative E3 ubiquitin-protein ligase XBAT31
- E3 ubiquitin-protein ligase XBAT32
- At4g02725
- Ankyrin repeat domain-containing protein EMB506, chloroplastic
- Protein ELC
- Polyadenylate-binding protein-interacting protein 5
- Agamous-like MADS-box protein AGL70
Sequence:
MGQQQSKGELLYQQVSYGNSEGIRALHRDGGDLEWMDREGKTPLILACMNSELFDVAKTLIELGSNVNAYRPGRHAGTPLHHAAKRGLENTVKLLLSHGANPLVLNDDCQTPLEVARVKGFSNVVRAIEKHICLFSGWMREFYGPTFLDLFAPQLLSRRVWVVIVPTGSRNPTKPFKLELVVYASLQDAQPRTVMPLWKANLEEPKAKQSDTSVMIVDNSTIPSRRMKKRRVCASHGRRRPQVVRQTRLKFAPSTEGDSQQLKWFCDACKGIPQPMHPPVFLQAPPSAPPPPSEDGLAMGMNASLHTTMSDPSNLNHHSIGQASSSSGPSSSTAPPSGKASAFGFNSHGIGIVLESSPSAPPLTDDDIATVDDGPIHYPSIDSTPVDLPSAASLPASTEGERKEDGNTGTCAICLDAPSEAVCVPCGHVAGCMSCLKEIKSKNWGCPVCRAKIDQVIKLYRV
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (Q10283)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA). Hmg1 catalyzes the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate. The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19486165}; Multi-pass membrane protein {ECO:0000269|PubMed:19486165}. Nucleus envelope {ECO:0000269|PubMed:19486165}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Mevalonate kinase
- Squalene epoxidase erg1
- Lanosterol 14-alpha demethylase erg11
- INSIG family protein
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Sterol regulatory element-binding protein cleavage-activating protein
- Squalene synthase
- C-4 methylsterol oxidase erg25
- Isopentenyl-diphosphate delta-isomerase
Sequence:
MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQIPAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDSSSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVLLSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRHFSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGNDSSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAISSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPEKKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDVTRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTMRGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRFCTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTVEDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPATDALKSVNSRVPGR
Protein: Cell division cycle 5-like protein (Cdc5-like protein) (Pombe Cdc5-related protein) (O08837)
Organism: Rattus norvegicus (Rat)
Function: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:11694351, ECO:0000269|PubMed:11884640}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00625}. Cytoplasm {ECO:0000269|PubMed:11694351}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000303|PubMed:11694351}.
Interaction partners:
- Pleiotropic regulator 1
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SPF27
- SNW domain-containing protein 1
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-processing-splicing factor 8
- Protein BUD31 homolog
- Cell division cycle 40.
- 116 kDa U5 small nuclear ribonucleoprotein component
- RNA helicase aquarius
Sequence:
MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKTAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEVARQTAEESGITNSASSTLLSEYNVTNNSIALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVTNATPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREMDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKNVGFATNNSEHITYLEHSPYEKFSKEDLKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPAQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLLKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQQRYADLLMEKETLQAKF
Protein: Neudesin (Neuron-derived neurotrophic factor) (Secreted protein of unknown function) (SPUF protein) (Q9CQ45)
Organism: Mus musculus (Mouse)
Function: Acts as a neurotrophic factor in postnatal mature neurons, enhancing neuronal survival. Promotes cell proliferation and neurogenesis in undifferentiated neural pro-genitor cells at the embryonic stage and inhibits differentiation of astrocytes. Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways. Neurotrophic activity is enhanced by binding to heme. Acts also as an anorexigenic neurotrophic factor that contributes to energy balance.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:15605373}. Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum {ECO:0000269|PubMed:31536960}. Note=Localized to mitochondria and endoplasmic reticulum by PINK1 and PARK7. {ECO:0000250|UniProtKB:Q9UMX5}.
Interaction partners:
- Cytochrome b5 type B
- Cytochrome b5
Sequence:
MARPAPWWRLRLLAALVLALALVPVPSAWAGQTPRPAERGPPVRLFTEEELARYGGEEEDQPIYLAVKGVVFDVTSGKEFYGRGAPYNALAGKDSSRGVAKMSLDPADLTHDTTGLTAKELEALDDVFSKVYKAKYPIVGYTARRILNEDGSPNLDFKPEDQPHFDIKDEF
Protein: Acyltransferase-like protein (Q8VWP8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
RGKSHVKPGKLIGRKECPLVTFDLPYLAFYYNQKLLFYKNDGGGEFEDKVEKLKEGLRVVLEEFYQLGGKLGKDDDGVLRVDYDDDMDGVEVVEAVAEGITVDELTGDDGTSSFKELIPFNGVLNLEGLHRPLLSIQLTKLKDGVAMGCAFNHAVLDGTSTWHFMSSWAQICNGTSSSVVVPPFLDRTTARNTRVKLDLSPVVSCNGDDATKQGQPAPQMREKLFRFSEAAVDKIKSRVNSTPPPSDGSKPFSTFQSLAVHIWRHVSQARNLKPEDYTVFTVFADCRKRVDPPMPDSYFGNLIQAIFTATAAGLLLENPPSFGASVIQKAIESHDAKAIDERNKAWEAAPKIFQFKDAGVNCVAVGSSPRFKVYEVDFGWGKPVGVRSGSNNRFDGMVYLYQGKSGGRSIDVEITMEAQAMEKLEKDKEFLMEV
Protein: Interferon alpha-4 (IFN-alpha-4) (Interferon alpha-4B) (Interferon alpha-76) (Interferon alpha-M1) (P05014)
Organism: Homo sapiens (Human)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 1
- Ubiquitin-like protein ISG15
- Interferon regulatory factor 7
- Interferon alpha-21
- Interferon regulatory factor 3
- Interferon alpha-5
- Interferon gamma receptor 1
- Interferon alpha/beta receptor 2
- Interferon alpha-8
- Interferon alpha-17
Sequence:
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRHDFGFPEEEFDGHQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD
Protein: Spermatogenesis-associated protein 7 (HSD-3.1) (Spermatogenesis-associated protein HSD3) (Q9P0W8)
Organism: Homo sapiens (Human)
Function: Involved in the maintenance of both rod and cone photoreceptor cells (By similarity). It is required for recruitment and proper localization of RPGRIP1 to the photoreceptor connecting cilium (CC), as well as photoreceptor-specific localization of proximal CC proteins at the distal CC (By similarity). Maintenance of protein localization at the photoreceptor-specific distal CC is essential for normal microtubule stability and to prevent photoreceptor degeneration (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25398945}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25398945}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25398945}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q80VP2}. Note=Localizes to the microtubule network. {ECO:0000269|PubMed:25398945}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Aryl-hydrocarbon-interacting protein-like 1
- Retinol dehydrogenase 12
- Lecithin retinol acyltransferase
- Protein RD3
- Lebercilin
- Tubby-related protein 1
- Retinoid isomerohydrolase
- Inosine-5'-monophosphate dehydrogenase 1
- X-linked retinitis pigmentosa GTPase regulator
Sequence:
MDGSRRVRATSVLPRYGPPCLFKGHLSTKSNAFCTDSSSLRLSTLQLVKNHMAVHYNKILSAKAAVDCSVPVSVSTSIKYADQQRREKLKKELAQCEKEFKLTKTAMRANYKNNSKSLFNTLQKPSGEPQIEDDMLKEEMNGFSSFARSLVPSSERLHLSLHKSSKVITNGPEKNSSSSPSSVDYAASGPRKLSSGALYGRRPRSTFPNSHRFQLVISKAPSGDLLDKHSELFSNKQLPFTPRTLKTEAKSFLSQYRYYTPAKRKKDFTDQRIEAETQTELSFKSELGTAETKNMTDSEMNIKQASNCVTYDAKEKIAPLPLEGHDSTWDEIKDDALQHSSPRAMCQYSLKPPSTRKIYSDEEELLYLSFIEDVTDEILKLGLFSNRFLERLFERHIKQNKHLEEEKMRHLLHVLKVDLGCTSEENSVKQNDVDMLNVFDFEKAGNSEPNELKNESEVTIQQERQQYQKALDMLLSAPKDENEIFPSPTEFFMPIYKSKHSEGVIIQQVNDETNLETSTLDENHPSISDSLTDRETSVNVIEGDSDPEKVEISNGLCGLNTSPSQSVQFSSVKGDNNHDMELSTLKIMEMSIEDCPLDV
Protein: Kinase (EC 2.7.-.-) (B2RXC2)
Organism: Mus musculus (Mouse)
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A.
- Calmodulin-1
- Inositol-tetrakisphosphate 1-kinase
- Inositol polyphosphate 5-phosphatase K
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Inositol-trisphosphate 3-kinase C
- Inositol-trisphosphate 3-kinase A
- Multiple inositol polyphosphate phosphatase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sequence:
MAVYCYALNSLVIMNSTNELKSGGPRPSGSETPQPSGRAALSPGSVFSPGRGASFLFPPAESLSLEEPGSPGGWRSGRRRLNSSSGSGGGSSSSNSSSSSGVGSPSWAGRLRGDAQQVVAARILSPPGPEEAQRKLRILQRELQNVQVNQKVGMFEAQIQAQSSAIQAPRSPRLGRARSPSPCPFRSSSQPPERVLAPCSPSEERRTKSWGEQCTETPDTNSGRRSRLSTHPSKDKEGVAPLLGPASPTRLGTQSPSTSVRMERGTPASPRCGSPTPMETDKRVAPSLERFGTSLTLATKVAASAASAGPHPGHDSALMETGCELGGMRPWEAQMERRGQFLGKETGSTPEPVRTHMREPPGRVGRGIHSVGGQGSWTPEVIKRPEERAVTAQSSEPSEDPRWSRLPVDLDSVGPEKGGNRIPGMRGPQQTLDSEREGSPALGLLGGSQAAQPGARGVEEDVHYGRMLEPLPPGEVTTKLKEPQCLPGDRMGMQPESSIVWPSALEEAPLIWTRDTGVQSKGTWGSQLPDGDAHPSCQEMPPDQKDKASLKEACSPSNIPAIPAVIITDMGAQEDGGLEEIQGSPRGPLPLRKLSSSSASSTGFSSSYDDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVQWSPFVMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMADVLRPFVPAYHGDVVKDGERYNQMDDLLADFDSPCVMDCKMGVRTYLEEELTKARKKPSLRKDMYQKMVEVDPEAPTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGSVNRDFKKTKTREQVTEAFREFTKGNQNILIAYRDRLKAIRATLEISPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGKTTPLPEGQTLQHDVPWQEGNREDGYLSGLDNLIDILTEMSQGSPLT
Protein: D 3 phosphoglycerate dehydrogenase putative (D-3-phosphoglycerate dehydrogenase, putative) (D-phosphoglycerate dehydrogenase (EC 1.1.1.95)) (Q76KF5)
Organism: Entamoeba histolytica
Interaction partners:
- phosphoserine transaminase
- phosphoglycerate mutase
- phosphoglycerate mutase
- phosphoserine transaminase
- Aldehyde dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Pyruvate kinase
Sequence:
MKIVVITEKPFAENAVKGIREILEKAGHEVVMIEKYKKKEDVIERIKDADGVIVRSDKIDEEIIKAGEKVKIIVRAGAGYDNIDIEACNQGKIVVMNTPGQNRNGVAELCIGMMIFGFRKGFKEGKGRELKDKTLGICGCGYVGKRVKEIAEGIGMKIKVYDPFITTENQVKKIEELFEECQVISLHLPLTKETKGKIGYELIKKLPYGGMICNTARKEIIDEEGLIRIMREREDLIYITDVAPTSKVFNNEFKGRFFATPIKIGAETEESNINAGMAAASQICDFFTNGTVKFQVNKF
Protein: AlkB homolog 7 (M0QZI0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGQGLFGAIHGFRETEKSRWSEASRAILQRVQAAAFGPGQTLLSSVHVLDLEARGYIKPHVDSIKFCGATIAGLSLLSPSVMRLVHTQEPGEWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGERRIPRGRRISVICRSLPEGMGPGESGQPPPAC
Protein: MICOS complex subunit MIC26 (Apolipoprotein O) (MICOS complex subunit MIC23) (Protein FAM121B) (Q9BUR5)
Organism: Homo sapiens (Human)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a crucial role in crista junction formation and mitochondrial function. Can promote cardiac lipotoxicity by enhancing mitochondrial respiration and fatty acid metabolism in cardiac myoblasts. Promotes cholesterol efflux from macrophage cells. Detected in HDL, LDL and VLDL. Secreted by a microsomal triglyceride transfer protein (MTTP)-dependent mechanism, probably as a VLDL-associated protein that is subsequently transferred to HDL.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25764979}; Single-pass membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:25764979}. Mitochondrion {ECO:0000269|PubMed:25781180}. Golgi apparatus membrane {ECO:0000269|PubMed:25764979}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25764979}. Note=Exists in three distinct forms: a glycosylated and secreted form, an ER/Golgi-resident form and a non-glycosylated mitochondrial form. {ECO:0000269|PubMed:25764979}.
Interaction partners:
- MICOS complex subunit MIC25
- MICOS complex subunit MIC13
- MICOS complex subunit MIC60
- MICOS complex subunit MIC27
- MICOS complex subunit MIC19
- MICOS complex subunit MIC10
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial
- DnaJ homolog subfamily C member 11
- Sorting and assembly machinery component 50 homolog
- Metaxin-2
Sequence:
MFKVIQRSVGPASLSLLTFKVYAAPKKDSPPKNSVKVDELSLYSVPEGQSKYVEEARSQLEESISQLRHYCEPYTTWCQETYSQTKPKMQSLVQWGLDSYDYLQNAPPGFFPRLGVIGFAGLIGLLLARGSKIKKLVYPPGFMGLAASLYYPQQAIVFAQVSGERLYDWGLRGYIVIEDLWKENFQKPGNVKNSPGTK