wanglab/gogpt-training-data huggingface dataset:
Protein: Type-1 angiotensin II receptor B (AT3) (Angiotensin II type-1 receptor B) (AT1 receptor B) (P29755)
Organism: Mus musculus (Mouse)
Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30556}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
Interaction partners:
- Angiotensinogen
- Type-2 angiotensin II receptor
- Guanine nucleotide-binding protein G
- Type-1 angiotensin II receptor A
- Plasminogen activator inhibitor 1
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Prothrombin
- Angiotensin-converting enzyme 2
Sequence:
MILNSSIEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYQWPFGNHLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLMAGLASLPAVIHRNVYFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFVFPFVIILTSYTLIWKALKKAYKIQKNTPRNDDIFRIIMAIVLFFFFSWVPHQIFSFLDVLIQLGVIHDCEIADVVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKARSHAGLSTKMSTLSYRPSDNMSSSARKSAYCFEVE
Protein: Cation transporter (Q381T0)
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:
MIGEAVRLFKKGDDLEMHKLRCVATVFFFLWVVDTLIGTFSGCRILQVNAFITFNTCAAVASGVVSLNYCRIVQAPSFRVKEQITAQPNPQPHSLLLGGQEHRNQQNGAISLEGIQGYYFGAKRLHTLISFGASIFVLFGSLTVMLESVHDIAHTRQPSPKLLLLTGVVHALLITVFGGEIDAHDRISGTLSSQREPRGLPSIHVTIRQVLRRPLLLFSRAFSQQYRIIRIVLRSFSAFTCILVSLLVRLGGSSMWETIGVMLLAFYVLAVTLNQSTSMAWLLLNNATCQPNVAAKCERAIRSVQLVPGVMQIKSSCFWEVSEGELMALVQLILLTSADPLAVTQEAHKILASVAAYVFVEVRKPDEEDNFDPGESSSYQCHNHSHGHDHGHSHGHNHDYGHHHHHGGGERHAFSSEGCKPVVTPEEPESTPSANVALSSSLYTVPPATNNIAGHSGVHANVSTLLGGTRGSVTAV
Protein: Chronophin (EC 3.1.3.16) (EC 3.1.3.74) (Pyridoxal 5'-phosphate phosphatase) (Pyridoxal phosphate phosphatase) (PLP phosphatase) (P60487)
Organism: Mus musculus (Mouse)
Function: Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism. Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
Interaction partners:
- Pyridoxal kinase
- Pyridoxine-5'-phosphate oxidase
- Aldehyde oxidase 1
- Aldehyde oxidase 3
- Aldehyde oxidase 2
- Aldehyde oxidase 4
- Pyridoxal phosphate phosphatase PHOSPHO2
- Cofilin-1
- Cofilin-2
- LIM domain kinase 1
Sequence:
MARCERLRGAALRDVLGQAQGVLFDCDGVLWNGERIVPGAPELLQRLARAGKNTLFVSNNSRRARPELALRFARLGFAGLRAEQLFSSALCAARLLRQRLSGPPDASGAVFVLGGEGLRAELRAAGLRLAGDPGEDPRVRAVLVGYDEQFSFSRLTEACAHLRDPDCLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFQCITEDFSVDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSSLEEAQAYLTAGQRDLVPHYYVESIADLMEGLED
Protein: SLIT and NTRK-like protein 6 (Q9H5Y7)
Organism: Homo sapiens (Human)
Function: Regulator of neurite outgrowth required for normal hearing and vision.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23543054, ECO:0000269|PubMed:23946138}; Single-pass type I membrane protein {ECO:0000269|PubMed:23543054, ECO:0000269|PubMed:23946138}.
Interaction partners:
Sequence:
MKLWIHLFYSSLLACISLHSQTPVLSSRGSCDSLCNCEEKDGTMLINCEAKGIKMVSEISVPPSRPFQLSLLNNGLTMLHTNDFSGLTNAISIHLGFNNIADIEIGAFNGLGLLKQLHINHNSLEILKEDTFHGLENLEFLQADNNFITVIEPSAFSKLNRLKVLILNDNAIESLPPNIFRFVPLTHLDLRGNQLQTLPYVGFLEHIGRILDLQLEDNKWACNCDLLQLKTWLENMPPQSIIGDVVCNSPPFFKGSILSRLKKESICPTPPVYEEHEDPSGSLHLAATSSINDSRMSTKTTSILKLPTKAPGLIPYITKPSTQLPGPYCPIPCNCKVLSPSGLLIHCQERNIESLSDLRPPPQNPRKLILAGNIIHSLMKSDLVEYFTLEMLHLGNNRIEVLEEGSFMNLTRLQKLYLNGNHLTKLSKGMFLGLHNLEYLYLEYNAIKEILPGTFNPMPKLKVLYLNNNLLQVLPPHIFSGVPLTKVNLKTNQFTHLPVSNILDDLDLLTQIDLEDNPWDCSCDLVGLQQWIQKLSKNTVTDDILCTSPGHLDKKELKALNSEILCPGLVNNPSMPTQTSYLMVTTPATTTNTADTILRSLTDAVPLSVLILGLLIMFITIVFCAAGIVVLVLHRRRRYKKKQVDEQMRDNSPVHLQYSMYGHKTTHHTTERPSASLYEQHMVSPMVHVYRSPSFGPKHLEEEEERNEKEGSDAKHLQRSLLEQENHSPLTGSNMKYKTTNQSTEFLSFQDASSLYRNILEKERELQQLGITEYLRKNIAQLQPDMEAHYPGAHEELKLMETLMYSRPRKVLVEQTKNEYFELKANLHAEPDYLEVLEQQT
Protein: rRNA biogenesis protein RRP5 (Ribosomal RNA-processing protein 5) (U3 small nucleolar RNA-associated protein RRP5) (U3 snoRNA-associated protein RRP5) (Q05022)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biogenesis of rRNA. Required for the formation of 18S and 5.8S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:8896463}.
Interaction partners:
- Small ribosomal subunit protein uS4A
- Ribosome biogenesis protein MAK21
- U3 small nucleolar RNA-associated protein 13
- Nucleolar complex protein 2
- U3 small nucleolar RNA-associated protein MPP10
- ATP-dependent RNA helicase ROK1
- RNA cytidine acetyltransferase
- NET1-associated nuclear protein 1
- Protein SOF1
- Periodic tryptophan protein 2
Sequence:
MVASTKRKRDEDFPLSREDSTKQPSTSSLVRNTEEVSFPRGGASALTPLELKQVANEAASDVLFGNESVKASEPASRPLKKKKTTKKSTSKDSEASSANSDEARAGLIEHVNFKTLKNGSSLLGQISAITKQDLCITFTDGISGYVNLTHISEEFTSILEDLDEDMDSDTDAADEKKSKVEDAEYESSDDEDEKLDKSNELPNLRRYFHIGQWLRCSVIKNTSLEPSTKKSKKKRIELTIEPSSVNIYADEDLVKSTSIQCAVKSIEDHGATLDVGLPGFTGFIAKKDFGNFEKLLPGAVFLGNITKKSDRSIVVNTDFSDKKNKITQISSIDAIIPGQIVDLLCESITKNGIAGKVFGLVSGVVNVSHLRTFSEEDLKHKFVIGSSIRCRIIACLENKSGDKVLILSNLPHILKLEDALRSTEGLDAFPIGYTFESCSIKGRDSEYLYLALDDDRLGKVHSSRVGEIENSENLSSRVLGYSPVDDIYQLSTDPKYLKLKYLRTNDIPIGELLPSCEITSVSSSGIELKIFNGQFKASVPPLHISDTRLVYPERKFKIGSKVKGRVISVNSRGNVHVTLKKSLVNIEDNELPLVSTYENAKNIKEKNEKTLATIQVFKPNGCIISFFGGLSGFLPNSEISEVFVKRPEEHLRLGQTVIVKLLDVDADRRRIIATCKVSNEQAAQQKDTIENIVPGRTIITVHVIEKTKDSVIVEIPDVGLRGVIYVGHLSDSRIEQNRAQLKKLRIGTELTGLVIDKDTRTRVFNMSLKSSLIKDAKKETLPLTYDDVKDLNKDVPMHAYIKSISDKGLFVAFNGKFIGLVLPSYAVDSRDIDISKAFYINQSVTVYLLRTDDKNQKFLLSLKAPKVKEEKKKVESNIEDPVDSSIKSWDDLSIGSIVKAKIKSVKKNQLNVILAANLHGRVDIAEVFDTYEEITDKKQPLSNYKKDDVIKVKIIGNHDVKSHKFLPITHKISKASVLELSMKPSELKSKEVHTKSLEEINIGQELTGFVNNSSGNHLWLTISPVLKARISLLDLADNDSNFSENIESVFPLGSALQVKVASIDREHGFVNAIGKSHVDINMSTIKVGDELPGRVLKIAEKYVLLDLGNKVTGISFITDALNDFSLTLKEAFEDKINNVIPTTVLSVDEQNKKIELSLRPATAKTRSIKSHEDLKQGEIVDGIVKNVNDKGIFVYLSRKVEAFVPVSKLSDSYLKEWKKFYKPMQYVLGKVVTCDEDSRISLTLRESEINGDLKVLKTYSDIKAGDVFEGTIKSVTDFGVFVKLDNTVNVTGLAHITEIADKKPEDLSALFGVGDRVKAIVLKTNPEKKQISLSLKASHFSKEAELASTTTTTTTVDQLEKEDEDEVMADAGFNDSDSESDIGDQNTEVADRKPETSSDGLSLSAGFDWTASILDQAQEEEESDQDQEDFTENKKHKHKRRKENVVQDKTIDINTRAPESVADFERLLIGNPNSSVVWMNYMAFQLQLSEIEKARELAERALKTINFREEAEKLNIWIAMLNLENTFGTEETLEEVFSRACQYMDSYTIHTKLLGIYEISEKFDKAAELFKATAKKFGGEKVSIWVSWGDFLISHNEEQEARTILGNALKALPKRNHIEVVRKFAQLEFAKGDPERGRSLFEGLVADAPKRIDLWNVYVDQEVKAKDKKKVEDLFERIITKKITRKQAKFFFNKWLQFEESEGDEKTIEYVKAKATEYVASHESQKADE
Protein: Disease resistance protein RML1A (EC 3.2.2.6) (Protein RESISTANCE TO LEPTOSPHAERIA MACULANS 1A) (F4I594)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TIR-NB-LRR receptor-like protein that confers resistance to the pathogen Leptosphaeria maculans (blackleg disease).
Interaction partners:
- Cell wall RBR3-like protein
- Disease resistance protein
- Late embryogenesis abundant
- Neurofilament heavy protein
- GLABRA2 expression modulator
- Senescence-associated and QQS-related protein
- Disease resistance protein RPP13
- Spindle assembly checkpoint component
- Arabinogalactan-protein family
Sequence:
MASSSSSASRTWRYRVFTSFHGSDVRTSFLSHFRKQFNNNGITMFDDQRILRGETISPALTQAIRESRISIVLLSKNYASSGWCLDELLEILKCKDDMGQIVMTVFYGVDPSDVRKQTGEFGIAFNETCACRTEEERQKWSQALNYVGNIAGEHLLNWDNEAKMIEKIARDVSEKLNVTPCRDFDGMVGIEAHLRKIQSLLDLDNDEVKMVAISGPAGIGKSTIGRALHSLLSNRFHHTCFVDNLRGSHPIGLDEYGLKLRLQEQLLSKILNQDGSRICHLGAIKERLCDMKVFIILDDVNDVKQLEALANESNWFGPGSRIIVTTENKELLKQHGINNTYYVGFPSDEEAIKILCRYAFRQSSSRHGFKKLTRSVTELCGKLPLGLRVVGSSLHGKNEEEWEYVIRRLETIIDRDIEQVLRVGYESLHENEQSLFLHIAIFFNYEDGDLVKAMLAENDLDIEHELNILVNKSLIYISTDGRIRMHKLLQLVGRQANQREEPWKRRILIDAQEICHVLENDIGTGAVSGILFDTSGINEVSISNKALRRMCNLRFLSVYKTKHDGYNRMDIPEDMEFPPRLRLLHWDAYPSKCLPLKFRAENLVELDMKDSRLEYLWPGTQLLTKLKKLNLEGSYNLKELPDLSNATNLEMLDLSVCLALAELPSSIKNLHKLDVIYMDLCESLHMIPTNINLASLETMYMTGCPQLKTFPAFSTKIKRLYLVRTGVEEVPASITHCSRLLKIDLSGSRNLKSITHLPSSLQTLDLSSTDIEMIADSCIKDLQRLDHLRLCRCRKLKSLPELPASLRLLTAEDCESLERVTYPLNTPTGQLNFTNCLKLGEEAQRVIIQQSLVKHACFPGSVMPSEFNHRARGNSLKILVKSSASFAFKACVLISPRQLQCERNQRRVKIRCRVTDGRGRFVGSKVVSLEHPNHSTGIRTKHLCFFNGVLTEVSCDALCFVFKISAYNPLDNYEISECAVQILTNEPERRSCDGGSE
Protein: DNA-directed RNA polymerase II subunit RPB2 (EC 2.7.7.6) (3'-5' exoribonuclease) (EC 3.1.13.-) (DNA-directed RNA polymerase II 140 kDa polypeptide) (DNA-directed RNA polymerase II subunit B) (RNA polymerase II subunit 2) (RNA polymerase II subunit B2) (RNA-directed RNA polymerase II subunit RPB2) (EC 2.7.7.48) (Q8CFI7)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30876}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVEDAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETKKAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQKFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLSHLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSEVSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASGVVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIVAIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGMRHAIYEKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSETGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEGITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGYHLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSRDGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGCRNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
Protein: Zinc finger protein 607 (Q96SK3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSYGSITFGDVAIDFSHQEWEYLSLVQKTLYQEVMMENYDNLVSLAGHSVSKPDLITLLEQGKEPWMIVREETRGECTDLDSRCEIISDGKMQLYRKHSCVTLHQRIHNGQKPYECKQCQKSFSHLTELMVHQTIHTSEEPDQCEKFRKAFSHLTDLRKHQKINAREKPYECEECGKVFSYPANLAQHGKVHVEKPYECKECGEAFRTSRQLTVHHRFHYGEKPYECKECGKAFSVYGRLSRHQSIHTGEKPFECNKCGKSFRLKAGLKVHQSIHTGEKPHECKECGKAFRQFSHLVGHKRIHTGEKPYECKECGKGFTCRYQLTMHQRIYSGEKHYECKENGEAFSSGHQLTAPHTFESVEKPYKCEECGKAFSVHGRLTRHQGIHSGKKPYECNKCGKSFRLNSSLKIHQNIHTGEKPYKCKECGKAFSQRAHLAHHNRIHTGYKPFECKECGKSFRCASYLVIHERIHTGEKPYVCQECGKGFSYSHKLTIHRRVHTGEKPYECKECGKAFSVSGQLTQHLSIHSGKKPFECNKCGKSFRFISVLKAHQNIHSAEKPYECKECGKAFRHATSLIYHDRTHAGEKSYECKECGETFSHASHLIIHERIHTSDKPYECKRCGKAFHCASYLVRHESVHADGNPYMCEECGKAFNSSHELSIHHRVHTGEKPFKCNKCRRSFRLRSILEVHQRIHI
Protein: Juxtamembrane domain-associated catenin (p120 catenin homolog) (Q9U308)
Organism: Caenorhabditis elegans
Function: May act as a positive modulator of hmr-1 function during epidermal morphogenesis. Required for proper localization of other junctional components, such as pac-1.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:25938815}. Nucleus {ECO:0000269|PubMed:25938815}.
Interaction partners:
- Alpha-catenin-like protein hmp-1
- Cadherin-related hmr-1
- Beta-catenin-like protein hmp-2
- Tight junction protein ZO-1
- Protein pop-1
- Disks large homolog 1
- Beta-catenin/armadillo-related protein 1
- PAC-1 interacting and coiled-coil domain-containing protein 1
- Cell death protein 3
- Armadillo repeat-containing protein wrm-1
Sequence:
MISSGWMQEMEPIPEEGTEADGSEWGAMSDTAKRTMRKKEVYTSEQINTLVSTVPKEAVPQEWLVENQVVDPEMATSYLTESLAGPTSARGSSYSYSYESHYDNPPEEEYEHFTNDDGVHQMQKVTRVTKVTTTRSVRQVPVQSPYSNIDFDSSGLPTPSPVIDRDPSLEMMARMGGASDHDSEDRSAPPPAPASRFLHEDSGIPSAPGVPDVVDAGIGEVTVVWSAPLQSNGGEVRGYQIEMREFPDGEWESMGVDHLLKDTTCRVTNLTSHEVQFRVSAYGRTGFGPASNPSLPVKIPISETDLATSAGAPLAPGRPTVIAVDGQGVLLEWTPPVADVHSSPPQGYQVEYRVYGSRDWIVANEQLVQENVFTVESLRPNGVYEFRVRGKNQDGLGHPSMSSGGVAIRPAAPQRHVPARKVSESVQPPGQPQMVEVGDDVVKLEWAPSVQNARYIVEYREVGDPEWHTANYDPIVQNGIQVEGLHRNSTYEFCVISIVDNIASQPSETSDIIHLRPTCNTSALRPAPNILEAPEFLEVDGDKITICWLPAQSQLPVMGYDVEFRDLQQDDRWYKVNDQPVFACKMTVGDLIMDHDYQFRVLAHNASGCSQPSPPSDFVHIEPSTNRFSSDTMESPHLGHHDVVKYVEAERFGAVPLLQEEMVRESPPLPERDDSPPPLRRANNNVQWRDPSLKEVIEYLSSADKDKQLNASGYLQHLTYTDNQIKEETREYGGIPKLIALLRSDTPRIQKNACACLKNLSFGKENDANKLAVMEADGVRLIAEVLRTTHDASVKEEAAAALWNLSSADMLKPVILESATEILSQQVIAPVLAVGTSDPTRHFGSTLFKNSTGVLRNVSAASQQARRRLRDIPNLIEALVHFLTHAIQKSQVDSPTVENAVCLLRNLSYRIQEVVDPNYDPAAAHSSSSKNMKHVASPKPEKKKKDKEKKKDKNPKNIVTGPSVLWQPHVVKLYLKLLQDSSNIETLEASAGAIQNLAACQFPPSAEVRAAVRVEKGLPVLVELIRLPEDFVVCAVATALRNLAIDPRNRELIGKYALRDFLDKLPEPGSPRRSAISDQTIGAVLGILFEIVRSSAAYTKDVHELKGTDKLRALSRSYPTYSHRVCKYASQVLYVMWQHKELHDGFKRSGLKEADFYSGTARRGDSSTLARPISSQGRERPSMHQLDETLSSGGGYGTMESNNRAGTLRPASATSQTIQRRYDQVPRDGPVYSSVQKPSPRGGGGGGNIDDSWV
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (A0A2R8YDQ9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}.
Interaction partners:
Sequence:
MSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Protein: Ras-related protein Rab-13 (EC 3.6.5.2) (F1PTE3)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18094055}; Lipid-anchor {ECO:0000269|PubMed:18094055}; Cytoplasmic side {ECO:0000269|PubMed:18094055}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome membrane {ECO:0000269|PubMed:18094055}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells. {ECO:0000250|UniProtKB:P51153, ECO:0000250|UniProtKB:Q9DD03}.
Interaction partners:
- MICAL like 2.
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein kinase cAMP-activated catalytic subunit beta
- Uncharacterized protein.
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Suppression of tumorigenicity 5.
- Rab GDP dissociation inhibitor alpha
- Rab GDP dissociation inhibitor beta
- DENN domain containing 1C.
- Microtubule associated monooxygenase, calponin and LIM domain containing 3.
Sequence:
MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDSFNNTYISTIGIDFKIRTVDVEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQAIKLAREHGIRFFETSAKSSTNVDEAFSSLARDILLKSGGRRSGNSHKAPGTDLKPCDKKNTSKCSLG
Protein: Uncharacterized protein, isoform N (Q9VT55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIEVDDQITKPLNLANSAVLRAVEEEEQQAKCDFYPTERQSRPRQRGEVDALHHTLHQQLLNQIKTDYLSHQQDITIDRDTVLKINRLATKRHLLKRDHSWPPAEQDQPTINPEQSHQISCSPSHSIEALREKFQSPTLVIEPTANEVREQRRRDGGSKERSKTLQKHTKEPDLAEVFHQTPISKGFSAPETKAADVDLGLVAPRCEYYEQLAHKRSATPTLPTQITPYRPRYKRQAHSLDRSRSRKRTVGAPELPPPKPRTSKPKVQRRCIKLATEVKISYGHDGDSEDDPNSGQDVDLETLPLPPTPVSPAAANLNQAKTAGRMVIDNVAVKQQQQMALALATNGSISPVNPSPSPLANTRIVPIRVEASADQLKLSAQQIYDDACSYLQDHQEMEDIQPRTESPTYVSATGGIKLLQRQSSSTPSTPVPPPLPSPIMRSKSGQDSQAKENQTKRQGRIYSLETATEKQHEAHVEIAQLEAKYAHIQQSIAEHLLQIDAYMENAKQALQRSAQTTPVSTPVPIPPTATATPPPPPPPPPTALPARPISSASNEAWDIFAHRQSPILAVESPLQAILRQIYTRAAGLPKRLSKEIKEDADAEAEEESLTENVPIVERALEDLHKIAVALEQKSEPAKLMHVELRTTPAVSEAEHVVIKDEEQDADMEYRHVSDVIANYEQLAKKEFEEWKEEQVVNSEEMLPKTELRKAIEEQLAKKGLRGGKKVLEGEEKPVTKLDVEKDVKKDAKAVAASKEELVEDKSAIQKESKKDLGTSEAPADLTKDADAVEETERSCGHGDSSVYCPVCDEMRCSPNTWGKLNKADQWRIANLHNEPLKNYKATYEIRSPYISRQISWEDMQSAKENVPPEKLQRQRSFVEIVTTPATESPPPSTPPPPPPPPPRQLALQKPETEVTWERSRSPSPLPSRKYPAPLIEAPQRSSSPYGLNPVQTKAPPSPVNLPAKFTHVPQLEGHNIGLLVKTATEPLQQSMSASSTMLAATPPRSAAQPTPFEFPSLEQAEEQHKFKSLASFDEVQRDFGVNRSFDNVSPRPYLGIEGYKRVAWPPASEERIIREFTPQPQTQSPAPGAGGYYPQAHAPTAAAAAPPQQYGAPSYDGQQPGAQWQQQQQQQQVPQQQYQPQSQAQAPYQPPQWNQPQQQQQQPSYQASPYQQQQQQQPSYYPQQNGGSTYAQPPYNSYSQPQLPYSQDQTDLQQQQQQQQQQYPGAYAGQDSYRGASPGIITLRKEAPVSQKPAPVYTSQPAAVSYQGGSKLRGDLKWPPPEYKEAAARENEERRQLALGPVCRPRRVNRDYTPFFAKHQLNNGYPSYKVPPGTQHIFG
Protein: Homeobox protein DLX-3 (O60479)
Organism: Homo sapiens (Human)
Function: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm {ECO:0000250|UniProtKB:Q64205}.
Interaction partners:
- Homeobox protein Meis1
- Homeobox protein Meis2
- Runt-related transcription factor 2
- Osteocalcin
- Protein FAM83H
Sequence:
MSGSFDRKLSSILTDISSSLSCHAGSKDSPTLPESSVTDLGYYSAPQHDYYSGQPYGQTVNPYTYHHQFNLNGLAGTGAYSPKSEYTYGASYRQYGAYREQPLPAQDPVSVKEEPEAEVRMVNGKPKKVRKPRTIYSSYQLAALQRRFQKAQYLALPERAELAAQLGLTQTQVKIWFQNRRSKFKKLYKNGEVPLEHSPNNSDSMACNSPPSPALWDTSSHSTPAPARSQLPPPLPYSASPSYLDDPTNSWYHAQNLSGPHLQQQPPQPATLHHASPGPPPNPGAVY
Protein: NOVA alternative-splicing regulator 1 (Neuro-oncological ventral antigen 1) (RNA-binding protein Nova-1) (Q1LYC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Polypyrimidine tract-binding protein 2b
- Serine/arginine repetitive matrix protein 4
- RNA binding protein fox-1 homolog 1
Sequence:
MMAGGEVQQNGIFSTPQHLSQSPQMDPDLSDSRKRPLETPTEASSTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTVEALNGVHNFIAEKVREMPQSSQKTEPVSILQPQTTVNPDRIKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQNRKAVEIIVQKIQEDPQSSSCLNISYSNITGPVANSNPTGSPFANSTEVLPNAAAAATASTLLGQAGLAGMGGFPAAMSSLSGNDLLAITSALNTLASYGYNTNTLGLGLNPAAASGVLAAVAASANPAAAAAANLLATYASEASGGGGHPAAPSLGGFSLGSLAAATGASNGYLNPSSPLVASSLLGTEKLAEGGKEVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFIPGTRNRKVTITGSPAATQAAQYLISQRITYEQGVRATNPQKVG