wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit 9, mitochondrial (Cytochrome c oxidase polypeptide VIIA) (A0A1D8PHI5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit VII
- Cytochrome c oxidase subunit Va
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 7, mitochondrial
Sequence:
MALAPITGTLKRKIITDITIGFAAGFGLAYLYWEVEHKPIIAKRDAYYAQLRKQKEIEESA
Protein: Gastric inhibitory polypeptide receptor (GIP-R) (Glucose-dependent insulinotropic polypeptide receptor) (Q0P543)
Organism: Mus musculus (Mouse)
Function: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gastric inhibitory polypeptide
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- VIP peptides
- Pro-opiomelanocortin
- Guanine nucleotide-binding protein G
- Natriuretic peptides A
- Dipeptidyl peptidase 4
Sequence:
MPLRLLLLLLWLWGLQWAETDSEGQTTTGELYQRWEHYGQECQKMLETTEPPSGLACNGSFDMYACWNYTAANTTARVSCPWYLPWFRQVSAGFVFRQCGSDGQWGSWRDHTQCENPEKNGAFQDQTLILERLQIMYTVGYSLSLTTLLLALLILSLFRRLHCTRNYIHMNLFTSFMLRAAAILTRDQLLPPLGPYTGDQAPTPWNQALAACRTAQIMTQYCVGANYTWLLVEGVYLHHLLVIVGRSEKGHFRCYLLLGWGAPALFVIPWVIVRYLRENTQCWERNEVKAIWWIIRTPILITILINFLIFIRILGILVSKLRTRQMRCPDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQVEGSLRFAKLAFEIFLSSFQGFLVSVLYCFINKEVQSEIRQGWRHRRLRLSLQEQRPRPHQELAPRAVPLSSACREAAVGNALPSGMLHVPGDEVLESYC
Protein: Sodium calcium exchanger 1h (Sodium/calcium exchanger 1a isoform X1) (Sodium/calcium exchanger 1a precursor) (Solute carrier family 8 member 1a) (Q32SG8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGQSGTSSYFSLALNLSIFLLVFSYELTPVIAGSSKSSLDVDTSNANSSQETCGGSYECKEGVILPIWTPVNPSFGDKLARATVYFVGLFYMFLGVSIIADRFMASIEVITSQEKEITIKKPNGETTTTTVRIWNETVSNLTLMALGSSAPEILLSVVEVCGHNFDAGELGPNTIVGSAAFNMFVIIGLCVSVIPEGEHRKVKHLRVFFVTATWSIFAYTWLYLILAVISPGIVEVWEGLLTLFFFPICVLFAWVADRRLLFYKYVYKRYRVGKKRGIIIETEGEPELQSKADIEMDGGMLNSHAEEFLDGAVDNEDKDADEDEARREMAKILKELKQKHPEKEMEQLVELANYHVLSQQQKSRAFYRCQATRLMTGAGNILKKHAADQARKALGIHELRSEVSDNDISSKIFFDPGTYQCLENCGTVALNVVRRGGDLTSTVSVEYRTEDGTANAGSDYQFTEGVIIFKPGETEKEIRVDIIDDDIFEEDEHFLVHLSNVKVISEGANNGNPGTNHVDALAGLGLPSTATVTIFDDDHAGIFLFEEPIVHISESIGMMEVKVVRTSGARGVVVIPYKTIEGTAKGGGEDFEDTHGVLEFQNDEISKTIQINIIDDEEYEKNKNFFLEIGEPQLVEMSERKAMLLHECGGFVKTDKQLYGRDVYRKVQGRDKPIPSTIISISEDGEEETLTKKEKDERRIAEMGRPTLGEHVKLEVIIEESYEFKSTVDKLIKKTNLALLVGTNSWRDQFVEAITVNSGDDDDEECGQEKMPSCFDYVMHFLTVFWKVLFAFVPPTDYWNGWACFIVSIMMIGVLTAFIGDIASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAAIQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIFHQSQGRQFRVDPGTLAFSVTLFTIFAFVCIAVLMYRRRPEIGGELGGPRHPKIITTTLFFSLWLMYIILSSMEAYCIIKGF
Protein: Transcription factor PRE4 (Basic helix-loop-helix protein 161) (AtbHLH161) (bHLH 161) (Protein BANQUO 3) (Protein PACLOBUTRAZOL RESISTANCE 4) (bHLH transcription factor bHLH161) (F4JCN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor that integrates multiple signaling pathways to regulate cell elongation and plant development. Regulates light responses by binding and inhibiting the activity of the bHLH transcription factor HFR1, a critical regulator of light signaling and shade avoidance. May have a regulatory role in various aspects of gibberellin-dependent growth and development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor IBH1
- Transcription factor bHLH150
- GDSL esterase/lipase At1g06990
- Core-2/I-branching beta-1,6-n-acetylglucosaminyltransferase family protein
- MATH domain and coiled-coil domain-containing protein At3g58210
- F-box protein At3g61340
- Gb|AAF32477.1
- Uncharacterized protein
- Uncharacterized protein
- Protein DOWNSTREAM OF FLC
Sequence:
MSSRKSRSRQTGASMITDEQINDLVLQLHRLLPELANNRRSGKVSASRVLQETCSYIRNLSKEVDDLSERLSQLLESTDSAQAALIRSLLMQ
Protein: Adenosine transporter, putative (Q57TQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMLGFESVSEFTVYITFIFFGMSAVVVTTSIFSIPFFFIEYYKYAQGDPNAEAEDQRFWNNVFTYYNATTFLVEFLLTLFMLTNLGRRIPLAVRLGAGLILSILAVFVVIMVTIIKTTETGAKVTIMLVGVINGVAATLCDTGNGALISPFPTKFFSAVVWGVAVCGIITSFFSIVIKASMESNYESMLTQSRIFFGLVVLLEVVSCILLVLLRKNPYAMKYAAEFRYAARERTNACENKESGASNGPAEQDEDSVAIDNNTTKGNVMTVTVDPDTMKDTDQVEDITNSQQMLKAKVSVVLKRVWPMLAAGFLAFSTTFLVYPGVFFAVKTDVPNGWYMTITAAMFHFGDFLSRLLLQFKRLQPSPRYVVVGTFARVFLIIPLVFCVRGIIGGTLLPYILSFLWGLTYGYFGGMALIHTPRTGSLTAAGERSLAANCAVIAILCGLFSGSMLALAVKEGLPQ
Protein: Lysine N-acyltransferase MbtK (N-acyltransferase MbtK) (EC 2.3.1.-) (Mycobactin synthase protein K) (P9WK15)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
Interaction partners:
- L-lysine N6-monooxygenase MbtG
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Protein Rv3402c
- Mycobactin import ATP-binding/permease protein IrtA
- Mycobactin import ATP-binding/permease protein IrtB
- Acyl-[acyl-carrier-protein] dehydrogenase MbtN
- Polyketide synthetase MbtC
- Peptide synthetase MbtF
Sequence:
MTKPTSAGQADDALVRLARERFDLPDQVRRLARPPVPSLEPPYGLRVAQLTDAEMLAEWMNRPHLAAAWEYDWPASRWRQHLNAQLEGTYSLPLIGSWHGTDGGYLELYWAAKDLISHYYDADPYDLGLHAAIADLSKVNRGFGPLLLPRIVASVFANEPRCRRIMFDPDHRNTATRRLCEWAGCKFLGEHDTTNRRMALYALEAPTTAA
Protein: Polyadenylate-binding protein 2-A (PABP-2-A) (Poly(A)-binding protein 2-A) (Nuclear poly(A)-binding protein 1-A) (Poly(A)-binding protein II-A) (PABII-A) (Polyadenylate-binding nuclear protein 1-A) (XLnPABP2-A) (nPABP2-A) (xPABPII-A) (Q9DDY9)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11677061, ECO:0000269|PubMed:15083517}. Cytoplasm {ECO:0000250|UniProtKB:Q86U42}. Note=Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. {ECO:0000250|UniProtKB:Q86U42}.
Interaction partners:
Sequence:
MAAVSSVASLRGADYENGLRGVAGPSDGGQDPGEDDPMGRGTLDLEMELLEQGRRSRRVGGRTTPGRRSGGRGGSGGGGAGGLEELEDEELEEEEPGELTGDQTIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSVEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFTGHPKGFAYIEFCDKESVRTSLALDESLFRGRQIKVVPKRTNRPGISTTDRGFPRARYRARASSYSSRSRFYSGYTPRPRGRVYRGRARATSWYTPY
Protein: Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT(m)) (EC 2.6.1.42) (O35855)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (By similarity). May also function as a transporter of branched chain alpha-keto acids (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O35854}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Cystathionine gamma-lyase
- Amine oxidase
- L-amino-acid oxidase
- Amine oxidase
- Glutamate--cysteine ligase regulatory subunit
- Branched-chain-amino-acid aminotransferase, cytosolic
- Glutamate--cysteine ligase catalytic subunit
- L-serine dehydratase/L-threonine deaminase
Sequence:
MAAATLGQVWARKLLPVPWLLCGSKRCVSSIFKAADLQIQMTKEPQKKPAPSQALLFGKTFTDHMLMVEWNNKAGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGGDQQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLYVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQREAQKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDLARTWGEFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRFQKELKAIQYGASAHDWMFRV
Protein: DCN1-like protein 1 (DCNL1) (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Squamous cell carcinoma-related oncogene) (Q96GG9)
Organism: Homo sapiens (Human)
Function: Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm {ECO:0000269|PubMed:26906416}. Note=The ubiquitinated form is localized in the cytoplasm. {ECO:0000269|PubMed:30587576}.
Interaction partners:
- Cullin-1
- NEDD8-conjugating enzyme Ubc12
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
- Cullin-3
- NEDD8-conjugating enzyme UBE2F
- Cullin-associated NEDD8-dissociated protein 1
- Cullin-2
- Cullin-4A
- Cullin-4B
Sequence:
MNKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKGSLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAWKFRAATQCEFSKQEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMAIAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPVLIDDFVEFARPQIAGTKSTTV
Protein: Protachykinin-1 (PPT) [Cleaved into: Substance P; Neurokinin A (NKA) (Neuromedin L) (Substance K); Neuropeptide K (NPK); Neuropeptide gamma; C-terminal-flanking peptide] (P06767)
Organism: Rattus norvegicus (Rat)
Function: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
Subcellular location: Secreted.
Interaction partners:
- Substance-K receptor
- Substance-P receptor
- VIP peptides
- Neuromedin-K receptor
- Tachykinin-4
- Angiotensinogen
- Kininogen-1
- Tachykinin-3
- Somatostatin
- Neurotensin/neuromedin N
Sequence:
MKILVAVAVFFLVSTQLFAEEIGANDDLNYWSDWSDSDQIKEAMPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQISHKRHKTDSFVGLMGKRALNSVAYERSAMQNYERRRK
Protein: Gamma-soluble NSF attachment protein (N-ethylmaleimide-sensitive factor attachment protein gamma) (D4A0E2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170, ECO:0000256|RuleBase:RU367013}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170, ECO:0000256|RuleBase:RU367013}.
Interaction partners:
Sequence:
DKARKINIIGYLFLKTGFLKWKPDYDSAASEYGKAAVAFKNAKQFEQAKDACLREAVAHESNRNLSSLCRAYEQAGMMLKEMQKLPEAVQLIEKASMMYLENGTPDTAAMALERAGKLIENVDPEKAVQLYQQTANVFENEERLRQAVELLGKASRLLVRGRRFDEAALSIQKEKNIYKEIENYPTCYKKTIAQVLVHLHRNDYVAAERCVRESYSIPGFNGSEDCAALEQLLEGYDQQDQDQVSEVCNSPLFKYMDNDYAKLGLSLVVPGGGIKKKSPATPQAKPEGAAGAAAEEEEDEYSGGLC
Protein: Outer dynein arm-docking complex subunit 3 (Coiled-coil domain-containing protein 151) (A5D8V7)
Organism: Homo sapiens (Human)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25192045}.
Interaction partners:
- Outer dynein arm-docking complex subunit 1
- Outer dynein arm-docking complex subunit 4
- Outer dynein arm-docking complex subunit 2
- Coiled-coil domain-containing protein 63
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 22 homolog
- Thioredoxin domain-containing protein 3
- Coiled-coil domain-containing protein 40
- Dynein axonemal intermediate chain 2
- Dynein axonemal intermediate chain 1
Sequence:
MTSPLCRAASANALPPQDQASTPSSRVKGREASGKPSHLRGKGTAQAWTPGRSKGGSFHRGAGKPSVHSQVAELHKKIQLLEGDRKAFFESSQWNIKKNQETISQLRKETKALELKLLDLLKGDEKVVQAVIREWKWEKPYLKNRTGQALEHLDHRLREKVKQQNALRHQVVLRQRRLEELQLQHSLRLLEMAEAQNRHTEVAKTMRNLENRLEKAQMKAQEAEHITSVYLQLKAYLMDESLNLENRLDSMEAEVVRTKHELEALHVVNQEALNARDIAKNQLQYLEETLVRERKKRERYISECKKRAEEKKLENERMERKTHREHLLLQSDDTIQDSLHAKEEELRQRWSMYQMEVIFGKVKDATGTDETHSLVRRFLAQGDTFAQLETLKSENEQTLVRLKQEKQQLQRELEDLKYSGEATLVSQQKLQAEAQERLKKEERRHAEAKDQLERALRAMQVAKDSLEHLASKLIHITVEDGRFAGKELDPQADNYVPNLLGLVEEKLLKLQAQLQGHDVQEMLCHIANREFLASLEGRLPEYNTRIALPLATSKDKFFDEESEEEDNEVVTRASLKIRSQKLIESHKKHRRSRRS
Protein: Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase) (P70712)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03017}.
Interaction partners:
- Kynurenine 3-monooxygenase
- Tryptophan 2,3-dioxygenase
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 1
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MEPSPLELPVDAVRRIATELNCDPTDERVALRLDEEDKLKRFKDCFYIPKMRDLPSIDLSLVNEDDNAIYFLGNSLGLQPKMVKTYLEEELDKWAKIGAYGHEVGKRPWIIGDESIVSLMKDIVGAHEKEIALMNALTVNLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRMIKPREGEETLRMEDILEVIEKEGDSIAVVLFSGLHFYTGQLFNIPAITQAGHAKGCFVGFDLAHAVGNVELHLHDWDVDFACWCSYKYLNSGAGGLAGAFIHEKHAHTIKPALVGWFGHELSTRFNMDNKLQLIPGVNGFRISNPPILLVCSLHASLEIFQQATMTALRRKSILLTGYLEYLLKHYHGGNDTENKRPVVNIITPSRAEERGCQLTLTFSISKKGVFKELEKRGVVCDKREPEGIRVAPVPLYNSFHDVYKFIRLLTAILDSTERN
Protein: Sister chromatid cohesion 1 protein 3 (SCC1 homolog 3) (AtRAD21-2) (Q9FQ19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in sister chromatid cohesion during mitosis.
Subcellular location: Nucleus.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein SCC2
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 5
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Structural maintenance of chromosomes protein 4
- Wings apart-like protein 2
- Wings apart-like protein 1
- Structural maintenance of chromosomes protein 2-1
- Protein GRAVITROPIC IN THE LIGHT 1
Sequence:
MFYSHTLLARKGPLGTVWCAAHVHQRLKKSQYTSINIPDTVDNIMFPEVPLALRTSSHLLVGVVRIYSKKVDYLYNDWNLLNTWVAKAFVSTQVNLPEDARQAPPESVTLPQALNLDEFDLEDDTLDMEFDNHTRSEEDITLTDQIPTGIDPYVAVTFDEDIISESIPMDVDQSTEPVSRHTGEIDVETAHETGPDNEPRDSNIAFDTGTYSPRNVTEEFTEVQDPRQSNLTEERIPNSERNDATSPGTVPEIERMRDAAHDLSPTSHPSFAAQQQDVRVERTESLDETLNEKEPTIPSIDEEMLNSGRHSAFELRSGSPGSAAGSEEERADFVHPSPQLVLQPSPPPQPQRRARKRKNFDGVTVLTNKNISERLKDPSDTLRKRKKMPSSKLKFWRMNNQSRKDQNFNEPLFTGFSDDLRNVFEKDYVASKPHLAVSDETLPEPASVSPTREAEVEINPVSPIPDSTNPDSTVQLSPAQQTEDVLDSAGPRPAHAESVATEAQSPRTFDNDDMGIEHLRDGGFPVYMPSPPPRSSPFRTDDFTTQSGNWETESYRTEPSTSTVPEDLPGQRNLGLSPVSERTDEELYFLEVGGNSPVGTPASQDSAALTGRARALAQYLKQRSSSSPTTSSHPSGDLSLSEILAGKTRKLAARMFFETLVLKSRGLIDMQQDRPYGDIALKLMPALFSKVQT
Protein: Late cornified envelope protein 1C (Late envelope protein 3) (Q5T751)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 1B
- Late cornified envelope protein 1E
- Late cornified envelope protein 1F
- Late cornified envelope protein 2D
- Late cornified envelope protein 1A
- Late cornified envelope protein 2C
- Late cornified envelope protein 1D
- Late cornified envelope protein 2A
- Late cornified envelope protein 2B
- Late cornified envelope protein 3E
Sequence:
MSCQQSQQQCQPPPKCTPKCPPKCPTPKCPPKCPPKCPPVSSCCSVSSGGCCGSSSGGSCGSSSGGCCSSGGGGCCLSHHRRRRSHCHRPQSSGCCSQPSGGSSCCGGGSGQHSGGCC
Protein: Vacuolar protein sorting-associated protein 16 homolog (A0A8I6GL61)
Organism: Rattus norvegicus (Rat)
Subcellular location: Late endosome membrane {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007949}. Lysosome membrane {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007949}. Note=Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. {ECO:0000256|PIRNR:PIRNR007949}.
Interaction partners:
Sequence:
MDCYTANWNPLGDSAFYRKYELYSMDWDLKEELKDCLVAAAPYGGPIALLRNCWRKEKAASVRPVLEMYSASGMPLASLLWKSGPVVALGWSAEEELLCVQEDGAVLVYGLHGDFRRHFSMGNEVLQNRVLDARIFHTEFGSGVAILTGAYRFTLSANVGDLKLRRMPEVPGLQSAPSCWTTLCHERVAHILLAVGPDLYLLDHATCSAVTPAGLAPGVSSFLQMAVSFTYRYLALFTDTGYIWMGTASLKEKLCEFNCNIRAPPKQMVWCSRPRSKEKAVVVAWERRLMVVGNAPESIQFVLDEDSYLVPELDGVRIFSRSTHEFLHEVPVASEEIFKIASMAPGALLLEAQKEYEKESQKADEYLREIQELGQLIQAVQQCIEAAGHEHQPDMQKRLLRAASFGKCFLDRFPPDSFVHMCQDLRVLNAIRDYHIGIPLTYTQYKQLTIQVLLDRLVLRRLYPLAIQICEYLRLPEVQGVSRILAHWACYKVQQKDVSDEDVARAINQKLGDTPGVSYSDIAARAYGCGRAELAIKLLEYEPRSGEQVPLLLKMKRSKLALSKAIESGDTDLVFTVLLHLKNELNRGDFFMTLRNQPMALSLYRQFCKHQELDTLKDLYNQDDNHQELGSFHIRASYAAEERIEGRVAALQTAADAFYKAKNEFAAKATEDQMRLLRLQRRLEDELGGRFLDLSLHDTVTTLILGGHNKRAEQLARDFRIPDKRLWWLKLSALADLEEWEELEKFSKSKKSPIGYLPFVEICMKQHNKHEAKKYASRVGPEQKVKALLLVGGADKTPVHIK
Protein: Syncytin-2 (ERV-FRD provirus ancestral Env polyprotein) (Envelope polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] (P61554)
Organism: Gorilla gorilla gorilla (Western lowland gorilla)
Function: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (By similarity).
Subcellular location: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.
Interaction partners:
- Sodium-dependent lysophosphatidylcholine symporter 1
- RNA helicase
Sequence:
MGLLLLVLILTPSLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYRWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVTAKRKNGTNVGTLPSTVCNVTFTVDSNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSSRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQLIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSQLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKALTTMQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPLTGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRRPRNIQESPF
Protein: Vacuolar-sorting protein SNF7 (DOA4-independent degradation protein 1) (Sucrose nonfermenting protein 7) (Vacuolar protein-sorting-associated protein 32) (P39929)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting. Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen. ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface. Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces. SNF7 filaments then form spirals that could function as spiral springs. The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission. SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles. ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12194857}. Endosome membrane {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}; Peripheral membrane protein {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}. Nucleus envelope {ECO:0000269|PubMed:25303532}.
Interaction partners:
- pH-response regulator protein palA/RIM20
- Vacuolar protein-sorting-associated protein 46
- Vacuolar protein sorting-associated protein 4
- Vacuolar protein sorting-associated protein 28
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein SNF8
- Vacuolar protein-sorting-associated protein 24
- DOA4-independent degradation protein 4
- Vacuolar-sorting protein BRO1
Sequence:
MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKVEGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDEDELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL
Protein: ApoN protein (Q2KIH2)
Organism: Bos taurus (Bovine)
Interaction partners:
- Cytochrome P450 2E1
Sequence:
MMRAVLLLCCVLMSPVAAFPRNAQEGVLTFQPSISEIGHPLNLLSNQILLPDPKTCQDLLHVAPSLAPLPEYLSNLALEVVLEEIGCTTEAHILQLQLVKIGGKDTTETLIRESKKHNEGEGTGQVKVILKDLGRSPGELRRAQRSVTLPEACRQEDRWVLYETAKMIAEFAEKLPNTELVKEFKAAATDVTQKCTDESWEYLQAVSNQLVKSPEMKDFTMPMQDQLYFIKRSMTILMHIVVEFIKTQVQNIFG
Protein: Uncharacterized protein (Q389Z3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP synthase delta chain
- Uncharacterized protein
- Uncharacterized protein
- Transmembrane protein
- Uncharacterized protein
- ATP synthase, epsilon chain, putative
- Uncharacterized protein
- Uncharacterized protein
- ATP synthase F1 subunit gamma protein, putative
- ATPase subunit 9, putative
Sequence:
MRRTFISFSAASAAAAAPVTSTKMQTLHKLLTGEVSFKNKAPVKDCNIVHQFGENWATELSAYAKTLPAEQQKIIVRQIARVKLTRYTVAELAAYCGDGPALLDETARAANIEQGVAFVKAKGVEAFEKYVAEESTNANWKPEEAKKFIEDVKAKAK