wanglab/gogpt-training-data huggingface dataset:
Protein: Keratinocyte differentiation-associated protein (P85411)
Organism: Rattus norvegicus (Rat)
Function: May act as a soluble regulator of keratinocyte differentiation (By similarity). May play an important role in embryonic skin morphogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P60985}.
Interaction partners:
Sequence:
MKIPILPIVALLSLLALHAAQGAALGTPMEDTTSSNYPSGTEGLSEFLNFNKLQSAFKSDDFLNWHVLTDMFKKALPFINWEFFPKVKGLRSAVPDSQ
Protein: Carboxyl-terminal-processing peptidase 2, chloroplastic (EC 3.4.21.102) (D1 C-terminal processing protease 2) (Photosystem II D1 protein processing peptidase 2) (O23614)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511}.
Interaction partners:
- Protein LHCP TRANSLOCATION DEFECT
- Rhomboid-like protein 17, chloroplastic
- Rhomboid-like protein 16, chloroplastic
Sequence:
MEVLASSSLSPISFTKPNKINPNFSIQVKLWVKQPPKISKASKFSYARSRSNISRSNAANPGVVFVCNRFLCVIERNDQRKLSGKVMMKSSVNFRQNLSVALVRIVSVLLVSSISVVTTDSPPSWGLTEENLLFLEAWRTIDRAYIDKTFNGQSWFRYRETALRNEPMNTREETYMAIKKMVATLDDPFTRFLEPGKFKSLRSGTQGAVTGVGLSIGYPTASDGPPAGLVVISAAPGGPANRAGILPGDVIQGIDNTTTETLTIYDAAQMLQGPEGSAVELAIRSGPETRLLTLTRERVSVNPVKSRLCELPGSGSNSPKIGYIKLTTFNQNASSAVREAIETLRGNNVNAFVLDLRDNSGGSFPEGIEIAKFWLDKGVIVYICDSRGVRDIYDTDGSNAIATSEPLAVLVNKGTASASEILAGALKDNKRALVYGEPTYGKGKIQSVFELSDGSGLAVTVARYETPAHTDIDKVGVTPDHPLPKSFPKDEEAFCGCLKDPTAACYLNQGLLFSR
Protein: La-related protein 7 (La ribonucleoprotein domain family member 7) (Q7ZWE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function. Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II. The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (By similarity). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (By similarity). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing. Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes (By similarity). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4G0J3}.
Interaction partners:
- 7SK snRNA methylphosphate capping enzyme
- Protein HEXIM1
- Si:ch1073-157b13.1.
- Cyclin-dependent kinase 9
- Cyclin T1
- Cyclin T2
- La ribonucleoprotein 4Aa
- Cyclin-T2b
- Mitochondrial ribosomal protein L11
- La ribonucleoprotein 4B
Sequence:
MKVCQRKTIDTEKMSSVGDTACADLSEKKDNEKKKRSRVKQLLSDVKKQVEFWFGDVNLHKDRFMKSIIEQSRDGYIDIAVLTTFNRMKNLTADVKLIARALKNSTIVEVNDEGTRIRRKEPLGETPKDVDSRTVYVELLPKTVTHIWLERVFSKCGHVVYISIPRYKSTRHSKGFAFVEFETQEQAQKAVEMLNNPPEDAPRKPGIFPKTCRKKAVPFDAVTQDNDEDGKKKKTELKNSTSEETGSNNMDQDGMLESTVTSEPNLATLTSTVSKKAKKKRLRSQSFEASSGEDQFEMSSKMRKVEEEKSELKDLSSENKDEELNSLKKKDDSVLKAKRKRKKKLKERLKVGEEVIPLRVLSKKEWLDLKQEYLTLQKRCMAHLKQSVFQINQKPTNYHIVKLKEDDTNAFYKDTPKKELTSGPEFLSGVIVKISYNQPLPSKRCIKDMLSELSPVAYVDLLDGDTEGHVRFKSSEDAQKVIKARFEFQKKYNWNLELLSGDHERRYWQKILVDRQAKLNTPREKKRGTEKLISKAEKIIIAKAKEASNHIRFDD
Protein: CAP, isoform Y (A0A0B4KEH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNNRNRNRNRNRNKRNRNQNQNQNPSQNQNENHQQQAEGAEDREEQQDFQTQIAVAQSSSFVDDNGNSGSVSNGPTENSEEVTNTLEKTEKKEEIFEQPATVIQKEADSDAEMGAKNSKHRKEKSDKQASNGKSEEQVRPPPTIIRRPPGSPRQAKVIVHRIVREEDTANGKAQSPEPPKAVESKEQHMEVEDSKKEKPEAQQEIETKEERENEPSPKELPESSHLSEDAQQKHVEVEENQQVYDEVDYSKDETTDNNPQQEQHDSKEPEQYVLQLEKAMEFVENAHQQHVAAVQSYQKQRDTEQNAQQQEQNEAQHLQESTKAHQQNIAVPQILVDPKKREEGLAQQLHHDVKEEPILNNAQQQNDDTAPKSPKEVTIKVQFQTEDPYSQQPPPQKPTSKVIIHQIHVETTDEEQNAKPTFEEVSSTTGSLAGTLSPPPRYLVESPKNVSSGQFSNFSRNVQIQEMELNSDFSSGEFNSLQSPLVCEVDSESEGSVVLGPERSPSDQQVPSSSRVEQHEQVRQKRAQYRNALESHFMPQLLNPRYLDSILEENEWRNSTASSGGSDQTGIRTPKLNETFPRSQLDFSRRHKRREEAPSPLKLETKLLEESTDLESCTRLQSALSPQSEDAELVYLSSSASSSVSDLMELELEQAAALAERALVDLDTDASRLIARPDDEMSSTSTTTADRSETEAETETETEREGEQSRESTPVNANPTLASSQSSLLSAATPTPTPTPTPADREQLAKDTNVSGGSTVSFGAASPLAATREEFVRNMDKVRELIEMTRREQEQGELPRSPSPPPVPPPPASVPPYSPESSSFHLASLQLKRQESNDSHCSDSTTHSQCTAINLASPPPPPTAQPPTPPLRQKPAPPPVPQPVSPPAPPTPQSEPELSVADSVANANADVDADADTDTEAIKKLRLLCTEQLASMPYGEQVLEELASVAQNISDQSQNKMPYPMPQLPHIKELQLNANESKSSSAWLGLPTQSDPKLLVCLSPGQRDLVNNQTQPDDLLDAHQKFVERRGYHELSKAQVLEQDHQQQQSEMLKTAAMMRELRKSLSPPAPPVPPPPVPVKSAETAAKATAHENAKRDDASEQKQKIAACESSSLENKPRRAADLGAQQSAEQRQSSSTTTSSHKATTETMSSDTAKFPTLDSMESELARMFPQHKGDIFEEQRKRFSNIEFPSHQPVSQTKRYSNIETSSYESKKRMENGQVVYDVSTSSHEKKEQGDPPKDQPVPPVPPPPIMSATKLNGNTFIDGDVAPKNSQPSRESGSGSGNGTYEEFRQRAKAAADAFGEQREQQNGLDQDRVFKDFDRLSQQMHAELQSTREKREKSASMYDLSGFTRPASGHPRLDELQQRRHAHMQELEREIERSAKSRQERMSSVPRQMEATPPRTHEIPIELEPRSRRAESLCNLNEPPPRPHTTVGHYNHPVVQDDWSRYANDLGYSENIARPFAREVEICYQRQNQRTPHCIRAPRLSASTNDLSSSSQYSYDTFNAYGGRRTHAPMLNQAQQQQRPHYGSCYSMIERDPNPRYISTTSRRGVSPAPPPVATPQQQQVPPPAYDRQQRRSSLPRELHEQQLKYILSKEEELKFEVERLQQERRRLMEEMQRAPVLPAPQRRESYRPAAKLPTLSEDEVFRQQMAEEWMNKVAEREERRQHKIIRISKIEDEHDHSAVDKATISDEFLDRVKERRHKLSMPADSDWESGAESQPQPAAQSQPESDVEAPPVRILEGQAEANLRQLPRHLREFAKFSTSEQLPDGAQMERHEEQERREEATDNAHSSATKKTSIVKTYKVSRLPPSVQAFERSSSNSELQRPFVRRQLSDASRPAYRPNEVTRPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Protein RKD1 (AtRKD1) (RWP-RK domain-containing protein 1) (Q9M9U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852}.
Interaction partners:
- Protein NLP3
- Protein NLP2
- Egg cell-secreted protein 1.5
- Protein NLP9
- Protein NLP1
Sequence:
MKSFCKLEYDQVFGKENNSFSFLNHSSLYSHQSELANPFFELEDEMLPSATSSNCFTSASSFLALPDLEPISIVSHEADILSVYGSASWTAEETMFVSDFAKKSETTTTKKRRCREECFSSCSVSKTLSKETISLYFYMPITQAARELNIGLTLLKKRCRELGIKRWPHRKLMSLQKLISNVKELEKMEGEENEDKLRNALEKLEKEKKTIEKLPDLKFEDKTKRLRQACFKANHKRKRRSGMSTPITSSSSSASASSSSYSSVSGFER
Protein: AT31036p (Uncharacterized protein, isoform D) (Uncharacterized protein, isoform E) (B9A0M7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein 706
- Histone PARylation factor 1-like
Sequence:
MLGKMSRNVTLSDEQSRLNARLEAHMVYICPECGKAFRTQAEWRQHLNTKHDYLKKTYSDFNFIQIDERFHECQLCFKWVENAHKTIALLQYHYFMHLEHSETYRCVHCRMAYTRRRALNVHLLDTHMREIEKYENKLRQMKRQQAKPTTAAAPAGNAEKPMAVKPRGRPKGSTNRKQNDLLQKALMDIDLNTEMEKSPVTALAAPVNEPKPISNVSELNLDRCLNAYEDIVRKEEKEVVPKYDDELDALCKEFFDDGPSAGKGEANEEQQQDDAHLQQGNQEVVIIEIDALGKEEVAQLKKEMKSDPISQPTKRRRISTTPSRDSDTEMSTNGLTKLISYLCPKCGKEIASMDGWRAHVFKKHDFEHIIENSFKILESGRKAMCLQCREVQPTTVRSQLQKHCFKHLPYRSYLKCTLCDRTKTSTSKILNHIRYNHQEELQRKNKTQLLIKPEPMWASPNKSGQAAMADDAGSEDDQGEQAVCEHCDRVFRSKWRYERHIASCRRSGAGKSVEGTVEALLNHLREGHMRMNAIWKTMQREKP
Protein: Zinc metalloprotease TldD homolog (EC 3.4.-.-) (Q7LXP6)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Zinc metalloprotease. Able to degrade azocasein in vitro.
Interaction partners:
- Zn-dependent protease, tldE protein homolog, putative
- Enolase
Sequence:
MFKYIKKAEELGASFADIRYERVIANEVTITEDRKYVSHGVDEGYSIRVIYNRNWGFKATDKITENEIEDTINHIYGDERVNIVYLPSKHDTIKIGKDINKNEEEKINDLHKVASQVNTLHPSIKSYSIKYYDEIFHKEYYSSEDREIIADGSSSSLSILVVAREGDVTVEVSEILSTQMGYIFDVFDINQVLANLQKRIINQLKGSTPKAGEYPVILAPEVVGIFTHEAIGHLSEADVTLNGSLYKLRNKRIGDEFLNISDLPAMDHPQSSLVYYDDEGVEGREVKIIENGILKEFMTDRYYSAYLGQPPTGNARAQSYRNFSLIRMRNTYMKPGDASLNELFEGIKEGYYLVSPIGGETSSNGTFQFAIQEGYRVENSEIKEPLRNIGISGNTISTLNAIEMISKDFGMSSGFCEKNGQTVQVSNGGPHIKVKKLKVGGYV
Protein: U7 snRNA-associated Sm-like protein LSm10 (Q969L4)
Organism: Homo sapiens (Human)
Function: Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to U7 snRNA. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:11574479}.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm11
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated proteins B and B'
- Small nuclear ribonucleoprotein Sm D2
- Cleavage and polyadenylation specificity factor subunit 3
- Symplekin
- U6 snRNA-associated Sm-like protein LSm3
Sequence:
MAVSHSVKERTISENSLIILLQGLQGRVTTVDLRDESVAHGRIDNVDAFMNIRLAKVTYTDRWGHQVKLDDLFVTGRNVRYVHIPDDVNITSTIEQQLQIIHRVRNFGGKGQGRWEFPPKNCK
Protein: Inner membrane protein YlaC (P0AAS0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Putative outer membrane protein YiaT
- Uncharacterized lipoprotein YgdI
Sequence:
MTEIQRLLTETIESLNTREKRDNKPRFSISFIRKHPGLFIGMYVAFFATLAVMLQSETLSGSVWLLVVLFILLNGFFFFDVYPRYRYEDIDVLDFRVCYNGEWYNTRFVPAALVEAILNSPRVADVHKEQLQKMIVRKGELSFYDIFTLARAESTS
Protein: V-type proton ATPase subunit D (V-ATPase subunit D) (V-ATPase 28 kDa accessory protein) (Vacuolar proton pump subunit D) (Q9Y5K8)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium.
Subcellular location: Membrane {ECO:0000305|PubMed:21844891}; Peripheral membrane protein {ECO:0000305|PubMed:21844891}; Cytoplasmic side {ECO:0000305|PubMed:21844891}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P39942}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21844891}. Cell projection, cilium {ECO:0000269|PubMed:21844891}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000269|PubMed:21844891}.
Interaction partners:
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit C 1
Sequence:
MSGKDRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRLKKIQEKKKILKEKSEKDLEQRRAAGEVLEPANLLAEEKDEDLLFE
Protein: Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II) (Q9JJY3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization. Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15764706}; Lipid-anchor {ECO:0000269|PubMed:15764706}. Cell membrane {ECO:0000269|PubMed:17272284, ECO:0000269|PubMed:21550973}; Lipid-anchor {ECO:0000269|PubMed:17272284}. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:15764706).
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Ceramide synthase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Ceramide synthase 4
- Ceramide glucosyltransferase
- Ceramide kinase
- Ceramide synthase 5
Sequence:
MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLLASFIPTTYEKRQRADDPCCLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKNPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGANSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
Protein: NO-associated protein 1, chloroplastic/mitochondrial (AtNOA1) (Dubious mitochondrial nitric oxide synthase 1) (AtNOS1) (EC 1.14.13.39) (GTPase NOA1) (Protein RESISTANT TO INHIBITION BY FOSMIDOMYCIN 1) (Q66GP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits cGTPase activity; binds and hydrolyzes specifically GTP. May participate in ribosome assembly and stability and thus regulates protein synthesis in chloroplasts. The GTPase activity requires MgCl(2)and the presence of either KCl or (NH(4))(2)SO(4). Involved in the post-transcriptional regulation of the methylerythritol phosphate (MEP) pathway. Involved in chlorophyll-a fluorescence regulation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16272429}. Plastid, chloroplast {ECO:0000269|PubMed:18469163}. Note=Was initially thought to be mitochondrial (PubMed:16272429). In fact seems to be chloroplastic (PubMed:18469163). {ECO:0000269|PubMed:16272429, ECO:0000269|PubMed:18469163}.
Interaction partners:
- Arginase 2, chloroplastic/mitochondrial
- Arginase 1, mitochondrial
- Arginine decarboxylase 2
- Nitrate reductase 1
- Ribosome biogenesis protein BOP1 homolog
- Nitrate reductase 2
- Pescadillo homolog
- Argininosuccinate synthase, chloroplastic
- Arginine decarboxylase 1, chloroplastic
- Argininosuccinate lyase, chloroplastic
Sequence:
MALRTLSTFPSLPRRHTTTRREPNLTVIYRNPTTSIVCKSIANSEPPVSLSERDGFAAAAPTPGERFLENQRAHEAQKVVKKEIKKEKKKKKEEIIARKVVDTSVSCCYGCGAPLQTSDVDSPGFVDLVTYELKKKHHQLRTMICGRCQLLSHGHMITAVGGNGGYPGGKQFVSADELREKLSHLRHEKALIVKLVDIVDFNGSFLARVRDLVGANPIILVITKIDLLPKGTDMNCIGDWVVEVTMRKKLNVLSVHLTSSKSLDGVSGVASEIQKEKKGRDVYILGAANVGKSAFINALLKTMAERDPVAAAAQKYKPIQSAVPGTTLGPIQINAFVGGEKLYDTPGVHLHHRQAAVVHSDDLPALAPQNRLRGQSFDISTLPTQSSSSPKGESLNGYTFFWGGLVRIDILKALPETCFTFYGPKALEIHAVPTKTATAFYEKELGVLLTPPSGKNQMQEWKGLQSHRLLQIEINDAKRPASDVAISGLGWISIEPIRKTRGTEPRDLNEAEHEIHICVSVPKPVEVFLRPTLPIGTSGTEWYQYRELTDKEEEVRPKWYF
Protein: Monocarboxylate transporter 3 (MCT 3) (Proton-coupled monocarboxylate transporter 3) (Solute carrier family 16 member 8) (O35308)
Organism: Mus musculus (Mouse)
Function: Probable retinal pigment epithelium (RPE)-specific proton-coupled L-lactate transporter (By similarity). May facilitate transport of lactate and H(+) out of the retina and could therefore play an essential role in maintenance of metabolic and ionic homeostasis of the outer retina.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:11287345, ECO:0000269|PubMed:12601063}; Multi-pass membrane protein {ECO:0000255}. Note=Basolateral sorting signals (BLSS) in C-terminal cytoplasmic tail ensure its basolateral expression (By similarity). Colocalizes with BSG in basolateral cell membrane of the retinal pigment epithelium (PubMed:18524945). {ECO:0000250|UniProtKB:O95907, ECO:0000269|PubMed:18524945}.
Interaction partners:
- Basigin
Sequence:
MGAGGPRRGAGPPDGGWGWVVLGACFVVTGFAYGFPKAVSVFFRELKRDFGAGYSDTAWVSSIMLAMLYGTGPLSSILVTRFGCRPVMLAGGLLASAGMILASFASRLVELYLTAGVLTGLGLALNFQPSLIMLGLYFERRRPLANGLAAAGSPVFLSMLSPLGQLLGERFGWRGGFLLFGGLLLHCCACGAVMRPPPGPPPRRDPSPHGGPARRRRLLDVAVCTDRAFVVYVVTKFLMALGLFVPAILLVNYAKDAGVPDAEAAFLLSIVGFVDIVARPACGALAGLGRLRPHVPYLFSLALLANGLTDLISARARSYGTLVAFCIAFGLSYGMVGALQFEVLMATVGAPRFPSALGLVLLVEAVAVLIGPPSAGRLVDALKNYEIIFYLAGSEVALAGVFMAVTTYCCLRCSKNISSGRSAEGGASDPEDVEAERDSEPMPASTEEPGSLEALEVLSPRAGSPEQEPEEEAVPELDHESIGGHEARGQKA
Protein: Left-right determination factor (Q9PW55)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR037402}.
Interaction partners:
Sequence:
MTSVRAACLLCAALFAMARGFTHEDMKDALLKKLGLNEIPQIHKRDLENLVIPTHVKNKYISMLKLHHSRKRRSLPSLAGILRGIPGNADISGEFVYSDTTRQRVVFEMTSRIPENSEVTMAELKLYKKAPHKRSIPERKGHRPVNNARVSIYWVEPQKDGSNRTSLVDSRLIPIHETGWKSFDVTQAVQYWSRSRMEMPMHLEVWIEGERPGSYAAEMAKCVHFTTQDPDDNTLGKPELVLYTLNLEEFGSSGDCENNKDREMCCREQYFINFRALTWTQYWIIEPSGYQAFRCKGGCRQPKRNYGYGERKCAVVESAPLPMMYLVKKGDYTEIEVAEFPNMIVEKCGCAMDNISVV
Protein: BNIP3L protein (Nineteen kD interacting protein-3 like) (Q8VBW4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MSHLVEPPPPLHNNNNNCEEGEQSLPPPAGLNSSWVELPMNSSNGNGNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVDGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
Protein: TSC22 domain family protein 2 (Q9CVK3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNSLATSVFSIAIPVDGDEDSASGGGVVAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELVERNSLLERENALLKSLSNNDQLSQLPAQQANPGSTSQQQAMIAQPPQPTQPPQQPNVSSA
Protein: Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a) [Cleaved into: Tumor necrosis factor receptor superfamily member 1A, membrane form; Tumor necrosis factor-binding protein 1 (TBPI)] (P19438)
Organism: Homo sapiens (Human)
Function: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22801493}; Single-pass type I membrane protein {ECO:0000269|PubMed:22801493}. Golgi apparatus membrane {ECO:0000269|PubMed:22801493}; Single-pass type I membrane protein {ECO:0000269|PubMed:22801493}. Secreted {ECO:0000269|PubMed:22801493}. Note=A secreted form is produced through proteolytic processing.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted. Note=Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.
Interaction partners:
- Lymphotoxin-alpha
- Baculoviral IAP repeat-containing protein 2
- TNF receptor-associated factor 5
- Ubiquitin carboxyl-terminal hydrolase CYLD
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Tumor necrosis factor
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 2
Sequence:
MGLSTVPDLLLPLVLLELLVGIYPSGVIGLVPHLGDREKRDSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQDTDCRECESGSFTASENHLRHCLSCSKCRKEMGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCLNGTVHLSCQEKQNTVCTCHAGFFLRENECVSCSNCKKSLECTKLCLPQIENVKGTEDSGTTVLLPLVIFFGLCLLSLLFIGLMYRYQRWKSKLYSIVCGKSTPEKEGELEGTTTKPLAPNPSFSPTPGFTPTLGFSPVPSSTFTSSSTYTPGDCPNFAAPRREVAPPYQGADPILATALASDPIPNPLQKWEDSAHKPQSLDTDDPATLYAVVENVPPLRWKEFVRRLGLSDHEIDRLELQNGRCLREAQYSMLATWRRRTPRREATLELLGRVLRDMDLLGCLEDIEEALCGPAALPPAPSLLR
Protein: BORCS8-MEF2B readthrough (H3BNR1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPVPRATDKDHSTQPGTMGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSANRLFQYASTDMDRVLLKYTEYSEPHESRTNTDILETLKRRGIGLDGPELEPDEGPEEPGEKFRRLAGEGGDPALPRPRLYPAAPAMPSPDVVYGALPPPGCDPSGLGEALPAQSRPSPFRPAAPKAGPPGLVHPLFSPSHLTSKTPPPLYLPTEGRRSDLPGGLAGPRGGLNTSRSLYSGLQNPCSTATPGPPLGSFPFLPGGPPVGAEAWARRVPQPAAPPRRPPQSASSLSASLRPPGAPATFLRPSPIPCSSPGPWQSLCGLGPPCAGCPWPTAGPGRRSPGGTSPERSPGTARARGDPTSLQASSEKTQQ
Protein: Aspartate-semialdehyde dehydrogenase (Non-phosphorylating) (EC 1.2.1.-) (E1V7V8)
Organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
Function: Involved in the degradation of ectoine, which allows H.elongata to utilize ectoine as both a carbon and a nitrogen source for growth. Probably catalyzes the NAD(+)-dependent oxidation of L-aspartate-semialdehyde to L-aspartate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Diaminobutyrate--2-oxoglutarate transaminase
- Aspartokinase
- Aspartate-semialdehyde dehydrogenase
- Diaminobutyrate--2-oxoglutarate transaminase
- Homoserine dehydrogenase
- Transcriptional regulatory protein DoeX
- Ectoine hydrolase
- Aspartate aminotransferase / aromatic amino acid aminotransferase
- Argininosuccinate synthase
- Adenylosuccinate synthetase
Sequence:
MTLSNQLSDLRLFRQYAYIDGKWTHGDAGREEAVFDPATGEAIGHIPVLEVEQIRGAVDAAEAAFVQWRALRADERCERLLAWYDLLQANREDLATIMTLEQGKPLPDARGEVEYGASFVRWFAEEGKRTFGDTIPSHIPNAALGTIKEPVGIAALITPWNFPLAMITRKAAAAMAAGCPVIVKPAHETPYSALALAELAERAGIPAGVFNVVLGEAAEVSKLLCDDERIKALSFTGSTRVGRLLLEQSANTVKRVSLELGGNAPFIVGPDMDPREAAFAAVAAKFQTAGQDCLAANRILVHESIHDAFVEQFAERMAALTVGNGLESEVDLGPLIHGQAVEKASAIVDDALSRGATLVAGDQREAPGPNFFMPTLLTGVTPEMQVWREENFAPVAGITSYRDDDEVIEMANDTEYGLAAYVYTHDIRRIWKLLRALEYGMVSVNSVKMTGPPVPFGGVKQSGLGREGGVTGIDEYLETKYYCLGALGSVSGS
Protein: Metalloendopeptidase (EC 3.4.24.-) (F1REP3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYLLVVVISLLLSSGPVQSRPVEDLIEKMSKKTGGNFTKKGNLLVSSVIETSKHAGENTDGPVILFGDIAFPRGLQNADQCTARGCKWDRSRDGLVYVPYQISRAYSPREVAVIEQGLQSFSAVSCIRFVPHTGERNYLNIKSESGCYSYLGRIGGGQVVSLQRQGCVYFSTVQHELLHALGFHHEQNRSDRDNHIRILYQNIIPAQQYNFNKQNTNNLGTPYDYNSVMQYSRYAFSMNNQPTMVPVPNANVVLGEAQSMSPNDILRINRLYCSTFNISY