wanglab/gogpt-training-data huggingface dataset:
Protein: U3 small nucleolar ribonucleoprotein protein LCP5 (P40079)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U3 small nucleolar ribonucleoprotein. Required for the early cleavages at sites A0, A1 and A2 of the pre-ribosomal RNA. Participates in ribosome biogenesis.
Subcellular location: Nucleus, nucleolus.
Interaction partners:
- Nucleolar protein 56
- Ribosome biogenesis protein BMS1
- U3 small nucleolar RNA-associated protein 11
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 21
- U3 small nucleolar ribonucleoprotein protein IMP3
- Protein BFR2
- Nucleolar complex protein 4
- rRNA-processing protein FCF2
- Something about silencing protein 10
Sequence:
MSELNALLKDINGSLTATSESLERLSGIYSNSATDEIPESNQLHEHLFYDAKKPAEKVSLLSLKNGSMLGYINSLLMLIGNRLDDECKDPSAMDARERSIQHRVVLERGVKPLEKKLAYQLDKLTRAYVKMEKEYKDAEKRALEKSTLVNHSGNDDSEDDESSEDEIAYRPNTSGIINTNKKSSAYRVEETAKQENGEENDDNETGVYKPPKITAVLPPQQTHFEDRFDAREHKDRSNKSRMQAMEEYIRESSDQPDWSASIGADIVNHGRGGIKSLRDTEKERRVTSFEEDNFTRLNITNKAEKRKQKQRERNARMNVIGGEDFGIFSSKRKLEDSTSRRGAKKTRSAWDRAQRRL
Protein: Troponin I 1 (CeTNI-1) (TnI 1) (Q20334)
Organism: Caenorhabditis elegans
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T
- Troponin T
- Tropomyosin isoforms a/b/d/f
- TropoNin T
- EF-hand domain-containing protein
- Myosin, essential light chain
- Troponin T, skeletal muscle
- Myosin regulatory light chain 2
- Myosin-3
- Myosin regulatory light chain 1
Sequence:
MSQIDENIRYGGAANETDGEDAQRKAQEREAKKAEVRKRLEEAGQKKQKKGFLTPERKKKLRKLLMNKAAEDLKTQQLRKEQERVKVLAERTVALPNVDSIDDHAKLEAIYNDLFSRLCNLEEEKYDINHITTETETTINQLNIEVNDLRGKFVKPSLKKVSKYDNKFKKMAEAKKEDGSKNLRNNLKTVKKESVFTQIANKKKSDKPEWSKKKEEKKEESAPEPVIEPVEEEETAASEGEEEEEEADEE
Protein: Calpain-9 (EC 3.4.22.-) (Digestive tract-specific calpain) (New calpain 4) (nCL-4) (Protein CG36) (O14815)
Organism: Homo sapiens (Human)
Function: Calcium-regulated non-lysosomal thiol-protease.
Interaction partners:
- Gastrokine-1
- Calpastatin
Sequence:
MPYLYRAPGPQAHPVPKDARITHSSGQSFEQMRQECLQRGTLFEDADFPASNSSLFYSERPQIPFVWKRPGEIVKNPEFILGGATRTDICQGELGDCWLLAAIASLTLNQKALARVIPQDQSFGPGYAGIFHFQFWQHSEWLDVVIDDRLPTFRDRLVFLHSADHNEFWSALLEKAYAKLNGSYEALKGGSAIEAMEDFTGGVAETFQTKEAPENFYEILEKALKRGSLLGCFIDTRSAAESEARTPFGLIKGHAYSVTGIDQVSFRGQRIELIRIRNPWGQVEWNGSWSDSSPEWRSVGPAEQKRLCHTALDDGEFWMAFKDFKAHFDKVEICNLTPDALEEDAIHKWEVTVHQGSWVRGSTAGGCRNFLDTFWTNPQIKLSLTEKDEGQEECSFLVALMQKDRRKLKRFGANVLTIGYAIYECPDKDEHLNKDFFRYHASRARSKTFINLREVSDRFKLPPGEYILIPSTFEPHQEADFCLRIFSEKKAITRDMDGNVDIDLPEPPKPTPPDQETEEEQRFRALFEQVAGEDMEVTAEELEYVLNAVLQKKKDIKFKKLSLISCKNIISLMDTSGNGKLEFDEFKVFWDKLKQWINLFLRFDADKSGTMSTYELRTALKAAGFQLSSHLLQLIVLRYADEELQLDFDDFLNCLVRLENASRVFQALSTKNKEFIHLNINEFIHLTMNI
Protein: A-kinase anchor protein 7 isoforms delta and gamma (AKAP-7 isoforms delta and gamma) (A-kinase anchor protein 18) (AKAP-18) (Protein kinase A-anchoring protein 7 isoforms delta and gamma) (PRKA7 isoforms delta and gamma) (Q6JP77)
Organism: Rattus norvegicus (Rat)
Function: Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane.
Subcellular location: [Isoform Gamma]: Nucleus {ECO:0000250|UniProtKB:F8VQ58, ECO:0000250|UniProtKB:Q9P0M2}. Cytoplasm {ECO:0000250|UniProtKB:F8VQ58, ECO:0000250|UniProtKB:Q9P0M2}.; SUBCELLULAR LOCATION: [Isoform Delta]: Nucleus {ECO:0000269|PubMed:15037626}. Cell membrane {ECO:0000269|PubMed:15037626}. Note=Cotranslocates with AQP2 to the plasma membrane in response to arginine-vasopressin (AVP) stimulation in inner medullary collecting duct (IMCD) cells. {ECO:0000269|PubMed:15037626}.
Interaction partners:
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase catalytic subunit alpha
- 3',5'-cyclic-AMP phosphodiesterase 4D
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- A-kinase anchor protein 6
- cAMP-dependent protein kinase catalytic subunit beta
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
- Superoxide dismutase, mitochondrial
- Endoribonuclease YbeY
- Small ribosomal subunit protein mS29
Sequence:
MERPAAGEIDANKCDHLSRGEEGTGDLETSPVGSLADLPFAAVDIQDDCGLPDVPQGNVPQGNPKRSKENRGDRNDHVKKRKKAKKDYQPNYFLSIPITNKKITAGIKVLQNSILRQDNRLTKAMVGDGSFHITLLVMQLLNEDEVNIGTDALLELKPFVEEILEGKHLTLPFHGIGTFQGQVGFVKLADGDHVSALLEIAETAKRTFQEKGILAGESRTFKPHLTFMKLSKAPMLWKKGVRKIEPGLYEQFIDHRFGEEILYQIDLCSMLKKKQSNGYYHCESSIVIGEKDRKEPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSVKAEEGDRNGDGSDNNRK
Protein: ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein) (Q9EPJ9)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein 2
- ADP-ribosylation factor 6
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor GTPase-activating protein 3
- ADP-ribosylation factor 5
- ADP-ribosylation factor 3
- Coatomer subunit beta'
- ADP-ribosylation factor 4
- Mannosyl-oligosaccharide glucosidase
Sequence:
MASPRTRKVLKEVRAQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLETQDDYEPSWSLQDKYSSRAAALFRDKVATLAEGKEWSLESSPAQNWTPPQPKTLQFTAHRASGQPQSAAASGDKAFEDWLNDDLGSYQGAQENRYVGFGNTVPPQKREDDFLNNAMSSLYSGWSSFTTGASKFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGRIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEDSSDRPLEGHSYQNSSGDNSQNSNIDQSFWETFGSAEPPKAKSPSSDSWTCADASTGRRSSDSWDVWGSGSASNNKNSNSDGWESWEGASGEGRAKATKKAAPSTADEGWDNQNW
Protein: Down syndrome cell adhesion molecule 1, isoform AH (Q0E9K0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQFYGADILMEYVIRGNAAVLKCSIPSFVADFVRVESWIDEEGTELRPSENYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSKAPSVPTGVMVFQQQVPLLSTFAMLCQAQAFPVPVFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFTFGDEPTNVEDSVSVTCLISSGDLPIDIEWLFNDYGISSFSGMTVYRGGKRTSMLTIDNVHARHAGKYSCRARNHASAVNFTTELIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Envelope glycoprotein E (gE) (gE-1) (P04488)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells (By similarity). In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips.
Subcellular location: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell junction. Host Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. The heterodimer gE/gI then redistributes to cell junctions to promote cell-cell spread later in the infection.
Interaction partners:
Sequence:
MDRGAVVGFLLGVCVVSCLAGTPKTSWRRVSVGEDVSLLPAPGPTGRGPTQKLLWAVEPLDGCGPLHPSWVSLMPPKQVPETVVDAACMRAPVPLAMAYAPPAPSATGGLRTDFVWQERAAVVNRSLVIHGVRETDSGLYTLSVGDIKDPARQVASVVLVVQPAPVPTPPPTPADYDEDDNDEGEDESLAGTPASGTPRLPPPPAPPRSWPSAPEVSHVRGVTVRMETPEAILFSPGETFSTNVSIHAIAHDDQTYSMDVVWLRFDVPTSCAEMRIYESCLYHPQLPECLSPADAPCAASTWTSRLAVRSYAGCSRTNPPPRCSAEAHMEPVPGLAWQAASVNLEFRDASPQHSGLYLCVVYVNDHIHAWGHITISTAAQYRNAVVEQPLPQRGADLAEPTHPHVGAPPHAPPTHGALRLGAVMGAALLLSALGLSVWACMTCWRRRAWRAVKSRASGKGPTYIRVADSELYADWSSDSEGERDQVPWLAPPERPDSPSTNGSGFEILSPTAPSVYPRSDGHQSRRQLTTFGSGRPDRRYSQASDSSVFW
Protein: Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)] (Q06625)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glycogen phosphorylase
- 1,4-alpha-glucan-branching enzyme
- Glucoamylase, intracellular sporulation-specific
- Phosphoglucomutase 2
- Glycogen [starch] synthase isoform 2
- UTP--glucose-1-phosphate uridylyltransferase
- Phosphoglucomutase 1
- Glycogen [starch] synthase isoform 1
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Phosphoribomutase
Sequence:
MNRSLLLRLSDTGEPITSCSYGKGVLTLPPIPLPKDAPKDQPLYTVKLLVSAGSPVARDGLVWTNCPPDHNTPFKRDKFYKKIIHSSFHEDDCIDLNVYAPGSYCFYLSFRNDNEKLETTRKYYFVALPMLYINDQFLPLNSIALQSVVSKWLGSDWEPILSKIAAKNYNMVHFTPLQERGESNSPYSIYDQLQFDQEHFKSPEDVKNLVEHIHRDLNMLSLTDIVFNHTANNSPWLVEHPEAGYNHITAPHLISAIELDQELLNFSRNLKSWGYPTELKNIEDLFKIMDGIKVHVLGSLKLWEYYAVNVQTALRDIKAHWNDESNESYSFPENIKDISSDFVKLASFVKDNVTEPNFGTLGERNSNRINVPKFIQLLKLINDGGSDDSESSLATAQNILNEVNLPLYREYDDDVSEILEQLFNRIKYLRLDDGGPKQGPVTVDVPLTEPYFTRFKGKDGTDYALANNGWIWNGNPLVDFASQNSRAYLRREVIVWGDCVKLRYGKSPEDSPYLWERMSKYIEMNAKIFDGFRIDNCHSTPIHVGEYFLDLARKYNPNLYVVAELFSGSETLDCLFVERLGISSLIREAMQAWSEEELSRLVHKHGGRPIGSYKFVPMDDFSYPADINLNEEHCFNDSNDNSIRCVSEIMIPKILTATPPHALFMDCTHDNETPFEKRTVEDTLPNAALVALCSSAIGSVYGYDEIFPHLLNLVTEKRHYDISTPTGSPSIGITKVKATLNSIRTSIGEKAYDIEDSEMHVHHQGQYITFHRMDVKSGKGWYLIARMKFSDNDDPNETLPPVVLNQSTCSLRFSYALERVGDEIPNDDKFIKGIPTKLKELEGFDISYDDSKKISTIKLPNEFPQGSIAIFETQQNGVDESLDHFIRSGALKATSSLTLESINSVLYRSEPEEYDVSAGEGGAYIIPNFGKPVYCGLQGWVSVLRKIVFYNDLAHPLSANLRNGHWALDYTISRLNYYSDEAGINEVQNWLRSRFDRVKKLPSYLVPSYFALIIGILYGCCRLKAIQLMSRNIGKSTLFVQSLSMTSIQMVSRMKSTSILPGENVPSMAAGLPHFSVNYMRCWGRDVFISLRGMLLTTGRFDEAKAHILAFAKTLKHGLIPNLLDAGRNPRYNARDAAWFFLQAVQDYVYIVPDGEKILQEQVTRRFPLDDTYIPVDDPRAFSYSSTLEEIIYEILSRHAKGIKFREANAGPNLDRVMTDKGFNVEIHVDWSTGLIHGGSQYNCGTWMDKMGESEKAGSVGIPGTPRDGAAIEINGLLKSALRFVIELKNKGLFKFSDVETQDGGRIDFTEWNQLLQDNFEKRYYVPEDPSQDADYDVSAKLGVNRRGIYRDLYKSGKPYEDYQLRPNFAIAMTVAPELFVPEHAIKAITIADEVLRGPVGMRTLDPSDYNYRPYYNNGEDSDDFATSKGRNYHQGPEWVWLYGYFLRAFHHFHFKTSPRCQNAAKEKPSSYLYQQLYYRLKGHRKWIFESVWAGLTELTNKDGEVCNDSSPTQAWSSACLLDLFYDLWDAYEDDS
Protein: Nuclear pore complex protein NUP50B (Nucleoporin 50B) (Q9LW88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP107
- AAA-type ATPase family protein
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP93A
- Nuclear pore complex protein NUP93B
- Nuclear pore complex protein NUP88
- Mitotic spindle checkpoint protein MAD2
- SUMO-conjugating enzyme SCE1
Sequence:
MGDSDNAIPFSRKRTALKELSRDNPGLDDDDEDTSALESGTFNTASKEVLASRRIIRVRRTDRSATAPPASNPFTGIRLVPFTAPAPSTAAAETTKPLSAGKQETLADGRSDATKETDGDSKEKSDAIDAVGKQETQGDEISAKTKDIIDGGEKEMSEAVNSVEGGGAVNKNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDGNEDTEKNGDSGALSSFHQHSSSKNAFTGLASTGFSASSFSFGLVPQEGSTGSGSEQSSFSFGQANNGNSSLFGASVATSITTKSTETTTAFPSKQDVSVETGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFACVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSKPSVAEAAAPLKTPENSPSAEDA
Protein: Mitochondrial E3 ubiquitin protein ligase 1 (EC 2.3.2.27) (Mitochondrial E3 ubiquitin protein transferase 1) (Q9VZJ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Plays a role in the control of mitochondrial morphology by promoting mitochondrial fission. Negatively regulates the mitochondrial fusion protein marf by promoting its ubiquitination, acting in a pathway that is parallel to the park/pink1 regulatory pathway.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q969V5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein kinase Pink1, mitochondrial
- Ubiquitin carboxyl-terminal hydrolase 30 homolog
- E3 ubiquitin-protein ligase parkin
- Transmembrane GTPase Marf
- LD47671p
- Ubiquitin-conjugating enzyme E2-17 kDa
Sequence:
MEFLHESVALGVDLLILGLCAREYVHYKRTAKVLKAAPQYNIDGDLKSVVERQRDKKIPYAVIRGTVTPIGVPLRSSLVPSVSGVLQIVKLHEHRVTRGFAGFWTEQHKLLHESANEMPFELRNQSHGVEIVDALSAAVLDVDVVYDNYEPSNLSLFDHVFGFFSGVRQRGLQTTEEVLREGSFLTAIGELELDGDTLRMQPSNEGPLFLTTATKSTLIKRFEDAKTTTILKLVVCSTISAILVAFIAKKLYRKRKQEREEAKIRERLDTERRERRARSRPHTLSQDQLCVVCSTNPKEIILLPCGHVCLCEDCAQKISVTCPVCRGSIVSKAAAFIA
Protein: Gap junction alpha-1 protein (Connexin-43) (Cx43) (Short fin protein) (O57474)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Plays an essential role in gap junction communication in the ventricles (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
Interaction partners:
- Tight junction protein 1a
- Proto-oncogene tyrosine-protein kinase Src
- Mitogen-activated protein kinase
- Tight junction protein 1b
- Mitogen-activated protein kinase
- Gap junction protein
- Casein kinase I isoform delta-B
- Cadherin-2
- Tubulin beta chain
- Cyclin-dependent kinase 1
Sequence:
MGDWSALGRLLDKVQAYSTAGGKVWLSVLFIFRILVLGTAVESAWGDEQSAFKCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSTPTLLYLAHVFYLMRKEEKLNRKEEELKAVQNDGGDVELHLKKIELKKFKHGLEEHGKVKMKGSLLRTYIFSIIFKSICEVVFLVIQWYLYGFSLSAVYTCERTPCPHRVDCFLSRPTEKTIFIIFMLVVSLFSLLLNIIELFYVLFKRIKDRVKSRQNTQFPTGTLSPTPKELSTTKYAYYNGCSSPTAPLSPMSPPGYKLATGERTNSCRNYNKQANEQNWANYSTEQNRLGQNGSTISNSHAQAFDYPDDTHEHKKLTPGHELQPLALIDARPCSRASSRMSSRARPDDLDV
Protein: Peptidase S1 domain-containing protein (Q9D8H5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELALPAILFTFFPGVLLGSEVLPTDSDSPSTTTGRRSIDLDSVCGRPRTSGRIVSGQDAQLGRWPWQVSVRENGAHVCGGSLIAEDWVLTAAHCFNQGQSLSIYTVLLGTISSYPEDNEPK
Protein: Stomatin (Q5XI04)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Prohibitin 1
- Flotillin-1
- Prohibitin.
- Acid-sensing ion channel 3
- Flotillin-2
- Prohibitin-2
- Band 3 anion transport protein
Sequence:
MSDKRQSGHVQSQRVPESFRDNSKAELGPCGWILVAVSFIFVLITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIMGSHH
Protein: Kinesin, putative (Q38CC9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAIEYPDNGYIYVCLRVRSVPTLSELELSCSSRKCGAGRMSPRHRPPRSTTRASQRICVSTLENIVALHDPKSLDDAACAVRDAQHVVQLLVGRSLRTVGKHSKRRPLMSTATANYFEFDNCLASMDADSMLQMPIVRNSDFIRPPEYGSQEDVYLSTAVHAVSAAVEGINSCVFAYGQTGSGKTYTLFGDAAYIQRDPGVVPRTMDDLFMRLEAIKRNYEENTETDYSFRVQLSFFEIYQNEAFCLFSRKGPLRVTFVRDSSGREALVIHELQRHFVTAADKAMPLVELGFGRRQTGETGMNAHSSRSHTILQLHVTQWRTDKVTRETVELNALLNIVDLAGSERQKTAKTDGKSRDEGIEINQSLTTLSRVINEISQGSKYVNYRDSLLTMVLRDYLGGNSKTFMIATISPVAFCYQESCATMQYAKGVRKIRNRPVVNTTFQTRNSLLELNAALKQENEKLRQHVENLLKVAGSGHSIDGLLSESDARDSDSGEITICGTIPHKTLRCGAPIKRYGTVSEAVFSTADHCAVPLVVTVHRKYKNSTGIGVANVEGSRIGISSLTRNVVQFHLSDLLSGAEGSGQLVARPKIPQLKCLETSHGLVEFERMPSNSCERRYWVRYVPPCKEGDEAVLHKKVVCHMNGIKHSDGDQWSLTHGDVFCVYIDSVGDDSEKSFVTFHYVDANCLARHGRYMESNDMPEDIASQLAPVSAPGSAEEQLSQLKHNRTNLLEVLRWQAQSVDYQCQLMGVPLLRQGSETVKEKSDGGSDRHSCYTPNSRGFDAHYDNETSPLPRPMLPYGDHIHTHMHSVKPMDMSTAAHAFQRTSNWKCCSVGAGALAESQRDCLRESEVCSWRFAKRSVEFGEVARCLAELERSSSLSQPVTANVVNSPPMESGIMEDGKGIKFIGCGDEAVVRVEKGTDTIVHMPYQKGGDEFDGGERKVKGLRESKTSTPSGAANPLRNGPHPREGARTSPLPGTRMSLVGDFCSELNADTVVGYSANANIFHLTSDGVRERELWVRIRSLERSVEDLRGQKSVLESKLRIAQDANTELELSEAQLKDELSQLTKEFLDSAADHSKLKGEISNLGAILHSMEGALMEVSVVSEFEMNEQFPIMAEKILMLRALTRMWKRRAMGSVARGTFTSGSRSSTNVSLTSGEGRTRGVVQASRDDLHLELSDTRAQQFLKEHVPDFPANTSVVEHSEKETAAESVFVVGTVLVGLEREKNQLVTDVNRERDEGEHYKGLVFRVQGDVNDLKMNAKKRESPTTEKMAERMAVSSVRSRQLVEAGRKRDASDMNLWTTDQADSNIRKKSLDNKVTLLQEQRMLLKQQQREYDRRAASLACKVEELRYTLSCLREKVQDNGPNGFKDANDLYQRVEELINEAMSGFGGQGCHSTSPPDFKFTGEMITLVLMGLRILLDRLKVELYVLNRQSLHRFALIAPAVHLRPETQFRYYMHKLRGTISGIARKPQCVGADWTVTEADILSGLVSHRRRQAGDALYGLLIWYDHWDVAAKTDHICYVELIRNRDHVMQIARLVRQESLVNTNATSCQNLLPDERRASTLGKEIPRSGKNIGATDITVTASRNILGKLSARVKNSTLGNAMTKWKKCPPGSTSFRGTSASSTLHSPSQESGLTFLSLAPNTTFTPLDFPSREPMRLSKSGHLQKQSQSNSASEKPSGSTVEKFGRRSRIIVVPVSEADITVAASTGLPRRSRTFNYARNLSTAYFSERELQPRALTKACTRFSRSKTFAALGNMAHGKPCHLSNMASKSSSVCEGRNGKSMSSCSFLPV
Protein: Growth arrest-specific 7a (Growth arrest-specific protein 7a isoform X1) (E7FA03)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MFCQTSPGSTSPARRQNKEIKETKITINCVTFPVSTSTPEQELLKPNEWSYCDYFWTDKRDLQGATVTGFEVLLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSMFPMAAQEEGTLGEAWAQLKKSLADEAEVHLKFSSKLQSEVEKPLLTFRGDNFKKDMKKYDHHIADLRKQLVSRYAAVEKARKALADRQKDLEVKTQQLEIKLSNKSEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTSMELEKLEVERIEMIQQHLRQYTTLRHETDMFNQSTLEPVDQLLQSVDPAKDRELWVKEHKTGDRRPVDMDI
Protein: DNA replication protein 16.7 (Gene product 16.7) (gp16.7) (Protein p16.7) (P16517)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells. Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid. Required for the second pull step of DNA ejection.
Subcellular location: Host cell membrane {ECO:0000255, ECO:0000269|PubMed:11169113}; Single-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:11169113}.
Interaction partners:
Sequence:
MEAILMIGVLALCVIFLLSGRNNKKKQEARELEDYLEDLNKRVVQRTQILSELNEVISNRSIDKTVNLSACEVAVLDLYEQSNIRIPSDIIEDLVNQRLQSEQEVLNYIETQRTYWKLENQKKLYRGSLK
Protein: D-amino acid dehydrogenase 2 (EC 1.4.99.-) (Q9HU99)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Oxidative deamination of D-amino acids.
Interaction partners:
- RidA family protein
- Histidinol-phosphate aminotransferase 1
- 4-hydroxyphenylpyruvate dioxygenase
- D-amino acid dehydrogenase 1
- 3-dehydroshikimate dehydratase
- Aromatic-amino-acid aminotransferase
- Aspartate aminotransferase
- Histidinol-phosphate aminotransferase 2
- Probable aminotransferase
- Probable binding protein component of ABC transporter
Sequence:
MAQRVCIIGAGVVGLATAYALVREGFDVTLVEARERGGLETSYANGGQLSYRYVAPLADSGVPAQALGWLLRNDAPLRLRPRLDPAQWRWLLGFLAACRGSLNRRNAAHLLRLALLSQRTLQDWREEDGLDGFDWRRNGKLVAFRQPASFARARQGLADPSAQFVLTAAECLALEPALSAAPFVGGIHTPDEEVADCHAFCVQLAERLQASGHCRQLHGRRVTKIVEGGAAVRGVEVGGDLIEADHVVLAAGYRSAELMLPGLRLPLYPLKGYSLTLPVGAQHRAPDTSITDYDRKIVYARIGERLRIAAMVDIVGFDPGLEPARLALLRQQARDTFPQGGDFDAAVEWAGMRPATPTGVPLVGNGGYRNLWLNLGHGALGFTLACGSGRLLAEQIGRRPPSIDTTGLLPRGALAG
Protein: Adipokinetic hormone receptor, isoform C (Q7KTL9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Adipokinetic hormone
- triacylglycerol lipase
- Pro-corazonin
Sequence:
MAKVAEENDHRDLSNWSNVNDTNGTIHLTKDMVFNDGHRLSITVYSILFVISTIGNSTVLYLLTKRRLRGPLRIDIMLMHLAIADLMVTLLLMPMEIVWAWTVQWLSTDLMCRLMSFFRVFGLYLSSYVMVCISLDRYFAILKPLKRSYNRGRIMLACAWLGSVVCSIPQAFLFHLEEHPAVTGYFQCVIFNSFRSDFDEKLYQAASMCSMYAFPLIMFIYCYGAIYLEIYRKSQRVLKDVIAERFRRSNDDVLSRAKKRTLKMTITIVIVFIICWTPYYTISMWYWLDKHSAGKINPLLRKALFIFASTNSCMNPLVYGLYNIRGRMNNNNPSVNNRHTSLSNRLDSSNQLMQKQLTNNSLLNGRGQVMAAAVSATTKLANVVSLKGTANGNGSAAAAGTVPITPPLTVTIAPLATDDEANDDSCLSAVTIRCQDQSPIRQKCGDSIELTSVVK