wanglab/gogpt-training-data huggingface dataset:
Protein: Polyphosphatidylinositol phosphatase INP52 (Synaptojanin-like protein 2) [Includes: SAC1-like phosphoinositide phosphatase (EC 3.1.3.-); Phosphatidylinositol 4,5-bisphosphate 5-phosphatase (EC 3.1.3.36)] (P50942)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:11094088, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15798181, ECO:0000269|PubMed:16406366}.
Interaction partners:
- Phosphoinositide 3-phosphatase
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP51
- Polyphosphatidylinositol phosphatase INP53
- Phosphatidylinositol 4-phosphate 5-kinase MSS4
- Phosphatidylinositol 4-kinase PIK1
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 4-kinase STT4
- Reduced viability upon starvation protein 167
- Probable phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TEP1
- Actin cytoskeleton-regulatory complex protein SLA1
Sequence:
MKILLSKQQTRKIAIVSETHGLVFRPINSKNSRRSTCAVELVPKAELNGNGFRRLSNHEIYGFIGLIEIEGLMFIATITGKSKVAQPIPNKTVNKIYAVDFFCLNNSKWDFMDIDSSGYPIVTNDGDFAISSPPSISTHSSRSSLRSSSSRSLNAQEQAPKHPCHELRKLLSNGSFYYSTDFDLTCTLQKRGFTEHSLSFDDFDREFMWNSFLMDEIITYRDRLDVTAKELLDQRGFLTTVIRGFAETIFSYINRLKVGLTIISRQSWKRAGTRFNARGIDDDGHVANFVETEMIMYSSQYCYAFTQIRGSLPIFWEQDTSLISPKIQITRSVEATQPTFDEHFIRLFKKYGPVHIINLLSTKSSEIQLSRRYKEQLKNSEKMKIGRDVFLTSFDFHRETSQDGFAAASRIIPKIRNTILDAGYFSYDVKEGRLISEQDGVFRTNCLDCLDRTNLIQQTISLAVFKLFLEDFRLVKPSSFIDDNEFVQKVNALWADNGDQISQIYTGTNALKSSYSRKGKMSFSGALSDATKSVSRMYINNFVDKGKQQNIDTLLGKLPHQQVVELYDPICEYVNERLLESEEKFTTHSNINLFVGTFNVNGNSRRADLSKWLFPIGDKFKPDVVVLGLQEVIELTAGSILNADYTKSSFWETMVTDCLNQYEEKYLLLRVEQMSSLLILFFARSDRAYNIKEVGGSTKKTGFGGITGNKGAVAIRFDYGATSFCFVNTHLSAGASNIDERRNDYNNIYRNITFPRSKTIPHHDSLFWLGDLNYRITLTNDEVRRELRAQKDGYIDRLLQYDQLTQEINEGVVFQGFKEPTLQFRPTYKYDYGTDNYDTSEKARTPSWTDRIIYKGENLHPLAYSDAPLKISDHKPVYAAYRANVKFVDEKEKLNLVEKLYAEYKNTHPEALTTGPDELSHARMEKQKESIPLDATVQSAGIKLIDLDDTSSCVSPLLSGPSPQPSVVGPGGLSNVSPDKSKLNVLPPPPPTSRHNKEPSSKLLSPTKEISIVSVSPRKGESNLPALERHSTPKPLPPVPALSLSKPVSLQKSSSELQHAKETIDNGKIVPRPCPPIRRKSSTAPDEISTSTKNSGVSTTEDPEPAKASTKPEKPPVVKKPHYLSVAANKLNTSQEHSIKVSPSNSKSEEELPCKKKSKPKVPAKNPELEKLSVHPLKPCDPN
Protein: UBX domain-containing protein 10 (UBX domain-containing protein 3) (Q96LJ8)
Organism: Homo sapiens (Human)
Function: VCP/p97-binding protein required for ciliogenesis. Acts as a tethering factor that facilitates recruitment of VCP/p97 to the intraflagellar transport complex B (IFT-B) in cilia. UBX domain-containing proteins act as tethering factors for VCP/p97 and may specify substrate specificity of VCP/p97.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:26389662}. Note=Recruited to cilia in a VCP-dependent manner. {ECO:0000269|PubMed:26389662}.
Interaction partners:
- UBX domain-containing protein 6
- UBX domain-containing protein 2A
- NSFL1 cofactor p47
- Tether containing UBX domain for GLUT4
- Transitional endoplasmic reticulum ATPase
- Nuclear protein localization protein 4 homolog
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 56
Sequence:
MATEAPVNIAPPECSTVVSTAVDSLIWQPNSLNMHMIRPKSAKGRTRPSLQKSQGVEVCAHHIPSPPPAIPYELPSSQKPGACAPKSPNQGASDEIPELQQQVPTGASSSLNKYPVLPSINRKNLEEEAVETVAKKASSLQLSSIRALYQDETGTMKTSEEDSRARACAVERKFIVRTKKQGSSRAGNLEEPSDQEPRLLLAVRSPTGQRFVRHFRPTDDLQTIVAVAEQKNKTSYRHCSIETMEVPRRRFSDLTKSLQECRIPHKSVLGISLEDGEGWP
Protein: Cstf2 protein (B4F7F1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cleavage stimulation factor subunit 1
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Pre-mRNA cleavage complex 2 protein Pcf11
- WD repeat domain 33
- Pre-mRNA 3'-end-processing factor FIP1
Sequence:
MAGLPVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGESISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLISGNPQPVHVAGPGSGPNVSMNQQNPQAPQAQSLSGMHVNGAPPMMQASMPGGVPAPVQMAAAVAGPGPGSLAPAGVMQAQVGMQGAGPVPMERGQVPMQDPRAAMQRGALPANVPTPRGLLGDAPNDPRGGTLMTVTGEVEPRAYLGPPPPPHQGPPMHHVPGHEGRGPPPHDMRGGPLAEPRPLMAEPRGPMLDQRGPPLDARGGRDPRGLDARGMEARAMEARGLEARAMEARAMEARAMEARAMEARAMEARAMEARGMDTRGPVPGPRGPIPSGIQGPNPMNMGAVVPQGSRQVPVMQGAGMQGASMQGGSQPGGFSPGQSQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP
Protein: Transient receptor potential cation channel subfamily A member 1b (Transient receptor potential cation channel, subfamily A, member 1b) (B6D5I5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQFGKELVRRNSFYKCVINEDETEESADVFELAFKGKASAIDRLIQKGPEHLSLRDENGASLLHYASAGGNLDIIRLIVSIVGPEVLNVQDEQGRTPLHWAVEQDQQQSCAVLLDLGADPNILNNALMGPLHLAVTKQYNHLAEVLLSCDKTNSNLEGDLGNTPVMLACSNNNCQALQILIKRGAKMCIQNKLGHYPIHTVAFAGAKEAMEMVLKIGEELGVSSTLHINYLDKSKSTPLHLAVRGGNIEVIKLCILKGAKVEQHQSGKCTALHFACSQGSLEAVKIMLSSYNRTEDIVNIRDGANRTPLHRATLFDHVELAEYLISKGAEIDSIDCKGLSPLLLASSCSAWKTVAYLLSIGADFKIKEKTGRNFLHFVILQPKGLKNLPETVLQSTAVKEMLSDEDVEGCTPLHYACKLGIHDSVKNMLGLNICLGQKSREKKSALHFAAEYGRINTCHRLLETLTDSKMLNDWDEKGLTPLHLASRAGHAQVVDLLLRKGALFQSDYKGWTCLHHAAAEGYTQTMKILLAANVKLLDEKNEDGNTALHIAAQAGHVSAVLLLLDRGAEIALNDADNSFLHEAVRNERREVVNATIEHERCDESMTSFKAKSRCVVLDIIEFLPESFQHLLDQCITESDHDANSQDYHIMYNFQWLQAPIQLKKYAKTDKTKAFQPLAALNAMVRYNRLELLIHPLSRKYLEMKWTAYGSKVHFLNLAIYLLGLLPLTYLILNLRPSQDFSKGNGTSVIMVPVSFSEQQYLISVCIIMVIVMNVYSICKEVVQLAQQRVNYFTDFSNPADWSAAISALVFVVPMCCSVEATWQWEAGAYAILTSWIGFLLYFQRFERIGIYVVMFNGIVRTLVCIMVLFVFLLLAFGLAFYALMLHRPEFSSISLALAQTFVMTVGELNYQSTFLNSYEEGHMAFPAITYLVFVFFVLLMPILLMNLMIGLAVGDIAEVQRNAELKRIAMQIDLHTALEEKLPYWFLKRVDKPSTVVYPNKCKKVLLEALVHGEIQNTVRTRLNLCSRKEGLLERELHKQKNRLKEMSCMLEKQHNLLKLIIQKMEITSEADEYDGPQNHGALKQHTSSTSQKSKWVPLLQAIKAKK
Protein: Type III secretion system chaperone SseA (T3SS chaperone SseA) (Secretion system effector A) (O84944)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Functions as a type III secretion system (TTSS) chaperone, which is required for SseB and SseD accumulation and secretion. May have a direct role in secretion of SseB and SseD, or may facilitate their correct folding, for efficient secretion and function. Required for survival and replication within epithelial cells and macrophages.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:12603739, ECO:0000305|PubMed:12787732}. Note=May associate with the inner membrane.
Interaction partners:
- Secreted effector protein SseB
- SPI-2 type 3 secretion system translocon protein SctB
- Secretion system chaparone
- Secretion system effector
- SPI-2 type 3 secretion system translocon protein SctE
- Secretion system apparatus lipoprotein SsaJ
- Secretion system chaparone
- Secretion system apparatus protein SsaL
- Secretion system apparatus protein
- SPI-2 type 3 secretion system ATPase
Sequence:
MMIKKKAAFSEYRDLEQSYMQLNHCLKKFHQIRAKVSQQLAERAESPKNSRETESILHNLFPQGVAGVNQEAEKDLKKIVSLFKQLEVRLKQLNAQAPVEIPSGKTKR
Protein: Protein FAM156A/FAM156B (Transmembrane protein 29/29B) (Q8NDB6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDPLQKRNPASPSKSSPMTAAETSQEGPAPSQPSYSEQPMMGLSNLSPGPGPSQAVPLPEGLLRQRYREEKTLEERRWERLEFLQRKKAFLRHVRRRHRDHMAPYAVGREARISPLGDRSQNRFRCECRYCQSHRPNLSGIPGESNRAPHPSSWETLVQGLSGLTLSLGTNQPGPLPEAALQPQETEEKRQRERQQESKIMFQRLLKQWLEEN
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 7.1.1.2) (Complex I-23kD) (CI-23kD) (NADH-ubiquinone oxidoreductase 23 kDa subunit) (TYKY subunit) (P42028)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
Sequence:
MRCLTMPMLLRALAQAQAARAGHASVRGLHSSAVAATYKYVNLREPSMDMKSVTDRAAQTLLWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR
Protein: PDZ domain-containing protein 7 (E9Q9W7)
Organism: Mus musculus (Mouse)
Function: In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q9H5P4}. Nucleus {ECO:0000250|UniProtKB:Q9H5P4}. Cell projection, stereocilium {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. Note=Localizes at the ankle region of the stereocilia. {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}.
Interaction partners:
- Adhesion G-protein coupled receptor V1
- Usherin
- Whirlin
- Vezatin
- F-BAR and double SH3 domains protein 2
- pre-mRNA splicing regulator USH1G
- Harmonin
- Unconventional myosin-VIIa
- Clarin-1
- Calcium and integrin-binding family member 2
Sequence:
MARGFTVGFDPLGLGELSSGSLSSVSSRGHLGSDSGSTATRYLLRKQQRLLNGPSRGIRASSPMGRVILINSPIEANSDESDIIHAVRVEKSPSGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVRLLTSSSCLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCSSTPSDRSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSYASSAPCSSGSLPSDRMDVCLGPEEPTSHGPGWGRADTAMQTEPDLDSRVETWCSVRPTVILRDTAIRSDGPSSTRHLDSALSESPKTALLLALSRPRTPITRSQSHLTLWEEKKQRKKEKSGSSGEKGALQRSKTLMNLFFKGGRQGRPAGDGHREAWTLDSRSPTKVRPRLDLEKAGSVGPVQKFVTWRLRRDRERGRALLSARSGSPSGQAPTVNEQVQAWESRRPLIQDLARRLLTDDEVLAVTRHCSRYVHEGGVEDLVRPLLAILDRPTKLLLLRDIRSVVAPTDLGRFDSMVMPVELEAFEALKSRAVGPSALRPTRQDTPPKRHLITPVPDSRGGFYLLPVNSSEDEDGEIREKLGVLKVSLGASAPHHKGIPPLQDVPVDAFSLRRGACAPPPQPPPVAPRPPRPNWLLTEPLSREDTQQNQSQTPAQSCSRSRSRSRSRSHSRGQGKSPGRRRSPSPAPIATAATANGRYHRPRKARPLLPRLLDGQVAKVGARQGPLENGRIAEEAVGNVSTGALRTITLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLCGDLQAGFELVAVDGESLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPGLLPLASDLRVVKDQSLAPDCPSALGPVDDARILTQLPPPEARQLQQSLSSALKVPQSIPKLSPILKDPHDPS
Protein: Diguanylate cyclase DgcM (DGC) (EC 2.7.7.65) (P77302)
Organism: Escherichia coli (strain K12)
Function: Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two cyclic-di-GMP (c-di-GMP) control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. DgcM stimulates activity of MlrA by direct interaction, leading to the transcription of csgD. It also catalyzes the synthesis of c-di-GMP via the condensation of 2 GTP molecules, which contributes to the c-di-GMP pool generated by module I in a positive feedback loop. Production of c-di-GMP contributes to but is not essential for MlrA activation.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeR
- HTH-type transcriptional regulator MlrA
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeD
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeB
- Cyclic di-GMP phosphodiesterase PdeH
- Oxygen sensor protein DosP
Sequence:
MITHNFNTLDLLTSPVWIVSPFEEQLIYANSAAKLLMQDLTFSQLRTGPYSVSSQKELPKYLSDLQNQHDIIEILTVQRKEEETALSCRLVLRKLTETEPVIIFEGIEAPATLGLKASRSANYQRKKQGFYARFFLTNSAPMLLIDPSRDGQIVDANLAALNFYGYNHETMCQKHTWEINMLGRRVMPIMHEISHLPGGHKPLNFVHKLADGSTRHVQTYAGPIEIYGDKLMLCIVHDITEQKRLEEQLEHAAHHDAMTGLLNRRQFYHITEPGQMQHLAIAQDYSLLLIDTDRFKHINDLYGHSKGDEVLCALARTLESCARKGDLVFRWGGEEFVLLLPRTPLDTALSLAETIRVSVAKVSISGLPRFTVSIGVAHHEGNESIDELFKRVDDALYRAKNDGRNRVLAA
Protein: Chemokine (C-C motif) receptor 7 (cDNA FLJ45911 fis, clone PEBLM2005615, highly similar to C-C chemokine receptor type 7) (A0N0Q0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDLGKPMKSVLVVALLVIFQVCLCQDEVTDDYIGDNTTVDYTLFESLCSKKDVRNFKAWFLPIMYSIICFVGLLGNGLVVLTYIYFKRLKTMTDTYLLNLAVADILFLLTLPFWAYSAAKSWVFGVHFCKLIFAIYKMSFFSGMLLLLCISIDRYVAIVQAVSAHRHRARVLLISKLSCVGIWILATVLSIPELLYSDLQRSSSEQAMRCSLITEHVEAFITIQVAQMVIGFLVPLLAMSFCYLVIIRTLLQARNFERNKAIKVIIAVVVVFIVFQLPYNGVVLAQTVANFNITSSTCELSKQLNIAYDVTYSLACVRCCVNPFLYAFIGVKFRNDLFKLFKDLGCLSQEQLRQWSSCRHIRRSSMSVEAETTTTFSP
Protein: Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (Q9VHS8)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. Involved in exon definition of genes containing long introns, including the rolled/MAPK gene. Has a role in oskar mRNA localization at the posterior pole of the developing oocyte.
Subcellular location: Nucleus {ECO:0000269|PubMed:14973490}.
Interaction partners:
- RNA-binding protein 8A
- Protein mago nashi
- Protein CASC3
- Pre-mRNA-splicing factor CWC22 homolog
- FI21285p1
- LD23870p
- LD24793p
- ATP-dependent RNA helicase WM6
- RE04053p
- LD40489p
Sequence:
MARKNAQAEDLSNVEFETSEDVEVIPTFNAMNLKEELLRGIYAYGFEKPSAIQQRSITPIVKGRDVIAQAQSGTGKTATFSISILQSLDTTLRETQVLCLSPTRELAVQIQKVILALGDMMNVQCHVCIGGTNLGEDIRKLDYGQHIVSGTPGRVFDMIKRRVLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERDEIMKEFRAGQSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIRILRDIEQYYSTQIDEMPMNVADLI
Protein: Harmonin (PDZ domain-containing protein) (Usher syndrome type-1C protein homolog) (Q9ES64)
Organism: Mus musculus (Mouse)
Function: Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles. As part of the intermicrovillar adhesion complex/IMAC plays a role in brush border differentiation, controlling microvilli organization and length. Probably plays a central regulatory role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the microvilli tips.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6N9}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19447093}. Cell projection, microvillus {ECO:0000269|PubMed:24725409}. Note=Colocalizes with F-actin (PubMed:19447093). Detected at the tip of cochlear hair cell stereocilia (PubMed:19447093). Enriched in microvilli of the intestinal brush border (PubMed:24725409). {ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:24725409}.
Interaction partners:
- Unconventional myosin-VIIa
- pre-mRNA splicing regulator USH1G
- Cadherin-23
- Protocadherin-15
- Ankyrin repeat and SAM domain-containing protein 4B
- Usherin
- Unconventional myosin-VIIb
- Adhesion G-protein coupled receptor V1
- Whirlin
- Clarin-1
Sequence:
MDRKVAREFRHKVDFLIENDAEKDYLYDVLRMYHQTMDVAVLVGDLKLVINEPNRLPLFDAIRPLIPLKHQVEYDQLTPRRSRKLKEVRLDRLHPEGLGLSVRGGLEFGCGLFISHLIKGGQADSVGLQVGDEIVRINGYSISSCTHEEVINLIRTKKTVSIKVRHIGLIPVKSSPEESLKWQYVDQFVSESGGVRGGLGSPGNRTTKEKKVFISLVGSRGLGCSISSGPIQKPGIFVSHVKPGSLSAEVGLETGDQIVEVNGIDFTNLDHKEAVNVLKSSRSLTISIVAGAGRELFMTDRERLEEARQRELQRQELLMQKRLAMESNKILQEQQEMERQRRKEIAQKAAEENERYRKEMEQISEEEEKFKKQWEEDWGSKEQLILPKTITAEVHPVPLRKPKSFGWFYRYDGKFPTIRKKAKEKKKAKYDSLQDLRKNKKELEFEQKLYKEKEEMLEKEKQLKINRLAQEVSETEREDLEESEKTQYWVERLCQTRLEQISSAENEIPEMTTGPPPPPPSVSPLAPPLRRFAGGIHLHTTDLDDIPLDMFYYPPKTPSALPVMPHPPSVNSPSKVPAPPVLPSSGHVSSSSSPWVQRTPPPIPIPPPPSIPTQDLTPTRPLPSALEEALGNHPFRTGDPGHPADDWEANTHSGKPSSSPTTERSFPPAPKTFCPSPQPPRGPGVSTISKPVMVHQEHNFVYRPAVKSEVLPQEMLKRMVVYQTAFRQDFRKYEEGFDPYSMFSPEQIAGKDVRLLRIKKEGSLDLALEGGVDSPVGKVVVSAVYEGGAAERHGGVVKGDEIMAINGKIVTDYTLAEAEAALQKAWNQGGDWIDLVVAVCPPKEYDDELSSLPSSAAESPQLARKQLEAYEPVCRHGFFLQLEPTNLLLKSRERNQTDPSWRPASSAPSP
Protein: Poly(ethylene terephthalate) hydrolase (PET hydrolase) (PETase) (EC 3.1.1.101) (PET-digesting enzyme) (A0A0K8P6T7)
Organism: Piscinibacter sakaiensis (Ideonella sakaiensis)
Function: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET. Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product. Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties. In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS). Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro.
Subcellular location: Secreted {ECO:0000305|PubMed:26965627}.
Interaction partners:
- Protein kinase domain-containing protein
Sequence:
MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS
Protein: Collagen alpha-1(XI) chain (Q28083)
Organism: Bos taurus (Bovine)
Function: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen type V alpha 2 chain.
- Collagen alpha-1
- Collagen type III alpha 1 chain
- Collagen alpha-2
- VWFA domain-containing protein.
- Collagen alpha-3
Sequence:
YDYCEHYSPXCDSSAPEAAQAQEPPVDEYAPEDIMEYDYEYGEAEYKEAESVTETPTVTEETIAQTEANIVDDFQEYNYGTESYQTEAPRSVSGSNEPNPVEEVFTEEYLTGEDYDSQRKNSEDMLYENKQIDGRDSDLLVDGDLGEYDFYEYKEYEDKPTSPTNEEFGPGVPAETDITETSINGHGAYGEKGQKGEPAVVEPGMLIEGPPGPAGPAGLMGPPGLQGPTGPPGDPGERGPPGRPGLPGADGLPGPPGTMLVLPFRYGGDSSKGPTVSAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSSGAKGEMGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGAKGDRGFDGLPGLPGDKGHRGERGPQGPPGPPGEDGIRGEDGEIGPRGLPGEAGPRGLLGPRGTPGPIGQPGIAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGSLGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPPGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPGKDGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGVSGKDGPAGLRGFPGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKE
Protein: Beta-1,4-galactosyltransferase 5 (Beta-1,4-GalTase 5) (Beta4Gal-T5) (b4Gal-T5) (EC 2.4.1.-) (Beta-1,4-GalT II) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5) (Q9JMK0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation. Plays a role in the glycosylation of BMPR1A and regulation of its protein stability. Essential for extraembryonic development during early embryogenesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Ceramide glucosyltransferase
Sequence:
MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMVQAQGILLRDNVRTIGAQVYEQVVRSAYAKRNSSLNDSDYPLDLNHSEAFPPTTTFLPEDFTYFANHPCPERLPSMKGPIDINMSEIAMDDIHELFSRDPAIKLGGHWKPADCVPRWKVAILIPFRNRHEHLPVLLRHLLPMLQRQRLQFAFYVIEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYSANVTYDALYKNITVNLTPELAQVTEY
Protein: Ammonium transporter Rh type C (Rhesus blood group family type C glycoprotein) (Rh family type C glycoprotein) (Rh type C glycoprotein) (Q7TNN9)
Organism: Rattus norvegicus (Rat)
Function: Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UBD6}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:12138130, ECO:0000269|PubMed:12595489, ECO:0000269|PubMed:16434569}; Multi-pass membrane protein {ECO:0000255}. Note=Also detected at the basolateral membrane and in subapical vesicles. Chronic acidosis induces relocalization to the apical cell membrane.
Interaction partners:
Sequence:
MAWNTNLRGRLPITCLILQVTMVVLFGVFVRYDIQADAHWWLEKKRKNISSDVENEFYYRYPSFEDVHAMVFVGFGFLMTYLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFFEEGHILLSVENLIQADFCVASTCVAFGAVLGKISPMQLLIMTFFQVTLFTVNEFILLNLIEAKDAGGSMTIHTFGAYFGLTVTWILYRKNLEQSKQRQSSVYHSDLFAMIGTLFLWIYWPSFNSASSFHGDTQHRAALNTYLSLAASVLTTVAVSSVIHKKGKLDMVHIQNATLAGGVGVGTAAEMMLTPYGALIVGFFCGILSTLGFAYLSPFLESRLRIQDTCGIHNLHGIPGIIGGIVGAVTAAYSSPDVYGEPGIVHSFGFGGYKADWTKRMQGRSQIFGLLLSLAMALVGGIIVGFILKLPFWGQASDENCFEDAIYWEVPEEVNTVYIPEDLAHKHSTSLVPAIPLVLSTPSASIVPPVPPTPPASLATVTSSSLVH