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P98088

- MUC5A_HUMAN

UniProt

P98088 - MUC5A_HUMAN

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Protein

Mucin-5AC

Gene

MUC5AC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Gel-forming glycoprotein of gastric and respiratoy tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microrganisms and particles that are subsequently removed by the mucocilary system.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei4302 – 43032Cleavage

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. extracellular fibril organization Source: MGI
  3. O-glycan processing Source: Reactome
  4. post-translational protein modification Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_115606. O-linked glycosylation of mucins.
REACT_115835. Termination of O-glycan biosynthesis.

Protein family/group databases

MEROPSiI08.951.

Names & Taxonomyi

Protein namesi
Recommended name:
Mucin-5AC
Short name:
MUC-5AC
Alternative name(s):
Gastric mucin
Lewis B blood group antigen
Short name:
LeB
Major airway glycoprotein
Mucin-5 subtype AC, tracheobronchial
Tracheobronchial mucin
Short name:
TBM
Gene namesi
Name:MUC5AC
Synonyms:MUC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:7515. MUC5AC.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. fibril Source: MGI
  3. Golgi lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2122 – 21221W → A: No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum. 1 Publication
Mutagenesisi4302 – 43021D → A or E: Abolishes cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 50305003Mucin-5ACPRO_0000158957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi? ↔ 4995By similarity
Disulfide bondi103 ↔ 111By similarity
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi456 ↔ 464By similarity
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1308 – 13081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1389 – 13891C-linked (Man)Curated
Glycosylationi1584 – 15841C-linked (Man)Curated
Glycosylationi1749 – 17491C-linked (Man)Curated
Glycosylationi1957 – 19571C-linked (Man)Curated
Glycosylationi2122 – 21221C-linked (Man)
Glycosylationi2652 – 26521C-linked (Man)Curated
Glycosylationi2950 – 29501C-linked (Man)Curated
Glycosylationi3198 – 31981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3383 – 33831C-linked (Man)Curated
Glycosylationi4009 – 40091C-linked (Man)Curated
Glycosylationi4245 – 42451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4318 – 43181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4433 – 44331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4469 – 44691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4612 – 46121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4723 – 47231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4753 – 47531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4762 – 47621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4831 – 48311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4904 – 49041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4908 ↔ 4958By similarity
Disulfide bondi4922 ↔ 4972By similarity
Disulfide bondi4933 ↔ 4988By similarity
Disulfide bondi4937 ↔ 4990By similarity
Glycosylationi4967 – 49671N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

C-, O- and N-glycosylated. O-glycosylated on the Thr-/Ser-rich tandem repeats. C-mannosylation in the Cys-rich subdomains may be required for proper folding of these regions and for export from the endoplasmic reticulum during biosynthesis.1 Publication
Proteolytic cleavage in the C-terminal is initiated early in the secretory pathway and does not involve a serine protease. The extent of cleavage is increased in the acidic parts of the secretory pathway. Cleavage generates a reactive group which could link the protein to a primary amide.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP98088.
PRIDEiP98088.

PTM databases

UniCarbKBiP98088.

Expressioni

Tissue specificityi

Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum.2 Publications

Gene expression databases

GenevestigatoriP98088.

Organism-specific databases

HPAiCAB002774.
CAB009395.
HPA040615.

Interactioni

Subunit structurei

Multimeric. Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD).1 Publication

Protein-protein interaction databases

IntActiP98088. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP98088.
SMRiP98088. Positions 336-394, 800-873, 4589-4652, 4903-4994.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 281202VWFD 1PROSITE-ProRule annotationAdd
BLAST
Domaini433 – 647215VWFD 2PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 1109208VWFD 3PROSITE-ProRule annotationAdd
BLAST
Repeati1383 – 148199Cys-rich subdomain 1Add
BLAST
Repeati1577 – 1677101Cys-rich subdomain 2Add
BLAST
Repeati1743 – 1847105Cys-rich subdomain 3Add
BLAST
Repeati1950 – 2050101Cys-rich subdomain 4Add
BLAST
Repeati2116 – 2220105Cys-rich subdomain 5Add
BLAST
Repeati2646 – 2750105Cys-rich subdomain 6Add
BLAST
Repeati2944 – 3084141Cys-rich subdomain 7Add
BLAST
Repeati3377 – 3481105Cys-rich subdomain 8Add
BLAST
Repeati4003 – 4107105Cys-rich subdomain 9Add
BLAST
Domaini4296 – 4507212VWFD 4PROSITE-ProRule annotationAdd
BLAST
Domaini4652 – 472170VWFC 1PROSITE-ProRule annotationAdd
BLAST
Domaini4757 – 482468VWFC 2PROSITE-ProRule annotationAdd
BLAST
Domaini4908 – 499689CTCKPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1383 – 410727259 X Cys-rich subdomain repeatsAdd
BLAST
Regioni2257 – 262436846 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
BLAST
Regioni2787 – 292213617 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
BLAST
Regioni3085 – 335527134 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
BLAST
Regioni3517 – 397145558 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-PAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1193 – 11953Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4896 – 49016Poly-Pro

Domaini

The cysteine residues in the Cys-rich subdomain repeats are not involved in disulfide bonding.

Sequence similaritiesi

Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 2 VWFC domains.PROSITE-ProRule annotation
Contains 4 VWFD domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoidiP98088.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
IPR025155. WxxW_domain.
[Graphical view]
PfamiPF08742. C8. 4 hits.
PF13330. Mucin2_WxxW. 9 hits.
PF01826. TIL. 3 hits.
PF00094. VWD. 4 hits.
[Graphical view]
SMARTiSM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00214. VWC. 6 hits.
SM00216. VWD. 4 hits.
[Graphical view]
SUPFAMiSSF57567. SSF57567. 4 hits.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
PS51233. VWFD. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98088-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSVGRRKLAL LWALALALAC TRHTGHAQDG SSESSYKHHP ALSPIARGPS
60 70 80 90 100
GVPLRGATVF PSLRTIPVVR ASNPAHNGRV CSTWGSFHYK TFDGDVFRFP
110 120 130 140 150
GLCNYVFSEH CGAAYEDFNI QLRRSQESAA PTLSRVLMKV DGVVIQLTKG
160 170 180 190 200
SVLVNGHPVL LPFSQSGVLI QQSSSYTKVE ARLGLVLMWN HDDSLLLELD
210 220 230 240 250
TKYANKTCGL CGDFNGMPVV SELLSHNTKL TPMEFGNLQK MDDPTEQCQD
260 270 280 290 300
PVPEPPRNCS TGFGICEELL HGQLFSGCVA LVDVGSYLEA CRQDLCFCED
310 320 330 340 350
TDLLSCVCHT LAEYSRQCTH AGGLPQDWRG PDFCPQKCPN NMQYHECRSP
360 370 380 390 400
CADTCSNQEH SRACEDHCVA GCFCPEGTVL DDIGQTGCVP VSKCACVYNG
410 420 430 440 450
AAYAPGATYS TDCTNCTCSG GRWSCQEVPC PDTCSVLGGA HFSTFDGKQY
460 470 480 490 500
TVHGDCSYVL TKPCDSSAFT VLAELRRCGL TDSETCLKSV TLSLDGAQTV
510 520 530 540 550
VVIKASGEVF LNQIYTQLPI SAANVTIFRP STFFIIAQTS LGLQLNLQPV
560 570 580 590 600
PTMQLFMQLA PKLRGQTCGL CGNFNSIQAD DFRTLSGVVE ATAAAFFNTF
610 620 630 640 650
KTQAACPNIR NSFEDPCSLS VENEKYAQHW CSQLTDADGP FGRCHAAVKP
660 670 680 690 700
GTYYSNCVFD TCNCERSEDC LCAALSSYVH ACAAKGVQLG GWRDGVCTKP
710 720 730 740 750
MTTCPKSMTY HYHVSTCQPT CRSLSEGDIT CSVGFIPVDG CICPKGTFLD
760 770 780 790 800
DTGKCVQASN CPCYHRGSMI PNGESVHDSG AICTCTHGKL SCIGGQAPAP
810 820 830 840 850
VCAAPMVFFD CRNATPGDTG AGCQKSCHTL DMTCYSPQCV PGCVCPDGLV
860 870 880 890 900
ADGEGGCITA EDCPCVHNEA SYRAGQTIRV GCNTCTCDSR MWRCTDDPCL
910 920 930 940 950
ATCAVYGDGH YLTFDGQSYS FNGDCEYTLV QNHCGGKDST QDSFRVVTEN
960 970 980 990 1000
VPCGTTGTTC SKAIKIFLGG FELKLSHGKV EVIGTDESQE VPYTIQQMGI
1010 1020 1030 1040 1050
YLVVDTDIGL VLLWDKKTSI FINLSPEFKG RVCGLCGNFD DIAVNDFATR
1060 1070 1080 1090 1100
SRSVVGDVLE FGNSWKLSPS CPDALAPKDP CTANPFRKSW AQKQCSILHG
1110 1120 1130 1140 1150
PTFAACHAHV EPARYYEACV NDACACDSGG DCECFCTAVA AYAQACHEVG
1160 1170 1180 1190 1200
LCVCLRTPSI CPLFCDYYNP EGQCEWHYQP CGVPCLRTCR NPRGDCLRDV
1210 1220 1230 1240 1250
RGLEGCYPKC PPEAPIFDED KMQCVATCPT PPLPPRCHVH GKSYRPGAVV
1260 1270 1280 1290 1300
PSDKNCQSCL CTERGVECTY KAEACVCTYN GQRFHPGDVI YHTTDGTGGC
1310 1320 1330 1340 1350
ISARCGANGT IERRVYPCSP TTPVPPTTFS FSTPPLVVSS THTPSNGPSS
1360 1370 1380 1390 1400
AHTGPPSSAW PTTAGTSPRT RLPTASASLP PVCGEKCLWS PWMDVSRPGR
1410 1420 1430 1440 1450
GTDSGDFDTL ENLRAHGYRV CESPRSVECR AEDAPGVPLR ALGQRVQCSP
1460 1470 1480 1490 1500
DVGLTCRNRE QASGLCYNYQ IRVQCCTPLP CSTSSSPAQT TPPTTSKTTE
1510 1520 1530 1540 1550
TRASGSSAPS STPGTVSLST ARTTPAPGTA TSVKKTFSTP SPPPVPATST
1560 1570 1580 1590 1600
SSMSTTAPGT SVVSSKPTPT EPSTSSCLQE LCTWTEWIDG SYPAPGINGG
1610 1620 1630 1640 1650
DFDTFQNLRD EGYTFCESPR SVQCRAESFP NTPLADLGQD VICSHTEGLI
1660 1670 1680 1690 1700
CLNKNQLPPI CYNYEIRIQC CETVNVCRDI TRLPKTVATT RPTPHPTGAQ
1710 1720 1730 1740 1750
TQTTFTTHMP SASTEQPTAT SRGGPTATSV TQGTHTTLVT RNCHPRCTWT
1760 1770 1780 1790 1800
KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRV QCRAKSHPEV
1810 1820 1830 1840 1850
SIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPRGCHMT
1860 1870 1880 1890 1900
STPGSTSSSP AQTTPSTTSK TTEIQASGSS APSSTPGTVS LSTARTTPAP
1910 1920 1930 1940 1950
GTATSVKKTF STPSPPPVPA TSTSSMSTTA PGTSVVSSKP TPTEPSTSSC
1960 1970 1980 1990 2000
LQELCTWTEW IDGSYPAPGI NGGDFDTFQN LRDEGYTFCE SPRSVQCRAE
2010 2020 2030 2040 2050
SFPNTPLGRL GQDVICSHTE GLICLNKNQL PPICYNYEIR IQCCETVNVC
2060 2070 2080 2090 2100
RDITRPPKTV ATTRPTPHPT GAQTQTTFTT HMPSASTEQP TATSRGGPTA
2110 2120 2130 2140 2150
TSVTQGTHTT PVTRNCHPRC TWTTWFDVDF PSPGPHGGDK ETYNNIIRSG
2160 2170 2180 2190 2200
EKICRRPEEI TRLQCRAKSH PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP
2210 2220 2230 2240 2250
FKMCLNIEVR VLCCETPKGC PVTSTPVTAP STPSGRAISP TQSTSSWQKS
2260 2270 2280 2290 2300
RTTTLVTTST TSTPQTSTTY AHTTSTTSAP TARTTSAPTT STTSVPTTST
2310 2320 2330 2340 2350
ISGPKTTPSP VPTTSTTSAA TTSTISAPTT STTSVPGTTP SPVLTTSTTS
2360 2370 2380 2390 2400
APTTRTTSAS PAGTTSGPGN TPSPVPTTST ISAPTTSITS APTTSTTSAP
2410 2420 2430 2440 2450
TSSTTSGPGT TPSPVPTTSI TSAPTTSTTS APTTSTTSAP TTSTTSAPTT
2460 2470 2480 2490 2500
STTSAPTTST TSTPTSSTTS TPQTSTTSAS TTSITSGPGT TPSPVPTTST
2510 2520 2530 2540 2550
TSAPTTSTTS AATTSTISAP TTSTTSAPTT STTSASTASK TSGLGTTPSP
2560 2570 2580 2590 2600
IPTTSTTSPP TTSTTSASTA SKTSGPGTTP SPVPTTSTIF APRTSTTSAS
2610 2620 2630 2640 2650
TTSTTPGPGT TPSPVPTTST ASVSKTSTSH VSISKTTHSQ PVTRDCHLRC
2660 2670 2680 2690 2700
TWTKWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI TRLQCRAESH
2710 2720 2730 2740 2750
PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNYEVR VLCCETPKGC
2760 2770 2780 2790 2800
PVTSTPVTAP STPSGRATSP TQSTSSWQKS RTTTLVTTST TSTPQTSTTS
2810 2820 2830 2840 2850
APTTSTTSAP TTSTTSAPTT STTSTPQTSI SSAPTSSTTS APTSSTISAR
2860 2870 2880 2890 2900
TTSIISAPTT STTSSPTTST TSATTTSTTS APTSSTTSTP QTSKTSAATS
2910 2920 2930 2940 2950
STTSSSGTTP SPVTTTSTAS VSKTSTSHVS VSKTTHSQPV TRDCHPRCTW
2960 2970 2980 2990 3000
TKWFDVDFPS PGPHGGDKET YNNIIRSGEK ICRRPQEITR LQCRAKSHPE
3010 3020 3030 3040 3050
VSIEHLGQVV QCSREEGLVC RNQDQQGPFK MCLNYEVRVL CCETPKGCPV
3060 3070 3080 3090 3100
TSTSVTAPSP LVGEPPAQTQ STSSWQKSRT TTLVTSSITS TTQTSTTSAP
3110 3120 3130 3140 3150
TTSTTPASIP STTSAPTTST TSAPTTSTTS APTTSTTSTP QTTTSSAPTS
3160 3170 3180 3190 3200
STTSAPTTST ISAPTTSTIS APTTSTTSAP TASTTSAPTS TSSAPTTNTT
3210 3220 3230 3240 3250
SAPTTSTTSA PITSTISAPT TSTTSTPQTS TISSPTTSTT PTPQTSTTSS
3260 3270 3280 3290 3300
PTTSTTSAPT TSTTSAPTTS TTSTPQTSIS SAPTSSTTSA PTASTISAPT
3310 3320 3330 3340 3350
TSTTSFHTTS TTSPPTSSTS STPQTSKTSA ATSSTTSGSG TTPSPVPTTS
3360 3370 3380 3390 3400
TASVSKTSTS HVSVSKTTHS QPVTRDCHPR CTWTKWFDVD FPSPGPHGGD
3410 3420 3430 3440 3450
KETYNNIIRS GEKICRRPEE ITRLQCRAES HPEVSIEHLG QVVQCSREEG
3460 3470 3480 3490 3500
LVCRNQDQQG PFKMCLNYEV RVLCCETPKG CPVTSTPVTA PSTPSGRATS
3510 3520 3530 3540 3550
PTQSTSSWQK SRTTTLVTTS TTSTPQTSTT SAPTTSTIPA STPSTTSAPT
3560 3570 3580 3590 3600
TSTTSAPTTS TTSAPTHRTT SGPTTSTTLA PTTSTTSAPT TSTNSAPTTS
3610 3620 3630 3640 3650
TISASTTSTI SAPTTSTISS PTSSTTSTPQ TSKTSAATSS TTSGSGTTPS
3660 3670 3680 3690 3700
PVPTTSTTSA STTSTTSAPT TSTTSGPGTT PSPVPSTSIT SAATTSTTSA
3710 3720 3730 3740 3750
PTTRTTSAPT SSMTSGPGTT PSPVPTTSTT SAPTTSTTSG PGTTPSPVPT
3760 3770 3780 3790 3800
TSTTSAPITS TTSGPGSTPS PVPTTSTTSA PTTSTTSAST ASTTSGPTTS
3810 3820 3830 3840 3850
TTSASTTSTI SPLTTSTTSA PITSMPSGPG TTPSPVPTTS TTSAPTTSTT
3860 3870 3880 3890 3900
SGPGTTPSPV PTTSTTSAPT TSTTSASTAS TTSGPGTTPS PVPTTSTTSA
3910 3920 3930 3940 3950
PTTSTTSAST ASTTSGPGTS LSPVPTTSTT SAPTTSTTSG PGTTPSPVPT
3960 3970 3980 3990 4000
TSTTSAPTTS TTSGPGTTPS PVPTTSTTPV SKTSTSHLSV SKTTHSQPVT
4010 4020 4030 4040 4050
SDCHPLCAWT KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRL
4060 4070 4080 4090 4100
QCRAESHPEV NIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC
4110 4120 4130 4140 4150
CETPRGCPVT SVTPYGTSPT NALYPSLSTS MVSASVASTS VASSSVASSS
4160 4170 4180 4190 4200
VAYSTQTCFC NVADRLYPAG STIYRHRDLA GHCYYALCSQ DCQVVRGVDS
4210 4220 4230 4240 4250
DCPSTTLPPA PATSPSISTS EPVTELGCPN AVPPRKKGET WATPNCSEAT
4260 4270 4280 4290 4300
CEGNNVISLS PRTCPRVEKP TCANGYPAVK VADQDGCCHH YQCQCVCSGW
4310 4320 4330 4340 4350
GDPHYITFDG TYYTFLDNCT YVLVQQIVPV YGHFRVLVDN YFCGAEDGLS
4360 4370 4380 4390 4400
CPRSIILEYH QDRVVLTRKP VHGVMTNEII FNNKVVSPGF RKNGIVVSRI
4410 4420 4430 4440 4450
GVKMYATIPE LGVQVMFSGL IFSVEVPFSK FANNTEGQCG TCTNDRKDEC
4460 4470 4480 4490 4500
RTPRGTVVAS CSEMSGLWNV SIPDQPACHR PHPTPTTVGP TTVGSTTVGP
4510 4520 4530 4540 4550
TTVGSTTVGP TTPPAPCLPS PICHLILSKV FEPCHTVIPP LLFYEGCVFD
4560 4570 4580 4590 4600
RCHMTDLDVV CSSLELYAAL CASHDICIDW RGRTGHMCPF TCPADKVYQP
4610 4620 4630 4640 4650
CGPSNPSYCY GNDSASLGAL REAGPITEGC FCPEGMTLFS TSAQVCVPTG
4660 4670 4680 4690 4700
CPRCLGPHGE PVKVGHTVGM DCQECTCEAA TWTLTCRPKL CPLPPACPLP
4710 4720 4730 4740 4750
GFVPVPAAPQ AGQCCPQYSC ACNTSRCPAP VGCPEGARAI PTYQEGACCP
4760 4770 4780 4790 4800
VQNCSWTVCS INGTLYQPGA VVSSSLCETC RCELPGGPPS DAFVVSCETQ
4810 4820 4830 4840 4850
ICNTHCPVGF EYQEQSGQCC GTCVQVACVT NTSKSPAHLF YPGETWSDAG
4860 4870 4880 4890 4900
NHCVTHQCEK HQDGLVVVTT KKACPPLSCS LDEARMSKDG CCRFCPLPPP
4910 4920 4930 4940 4950
PYQNQSTCAV YHRSLIIQQQ GCSSSEPVRL AYCRGNCGDS SSMYSLEGNT
4960 4970 4980 4990 5000
VEHRCQCCQE LRTSLRNVTL HCTDGSSRAF SYTEVEECGC MGRRCPAPGD
5010 5020 5030
TQHSEEAEPE PSQEAESGSW ERGVPVSPMH
Length:5,030
Mass (Da):526,608
Last modified:October 23, 2007 - v3
Checksum:i00523008FF20ACAB
GO

Sequence cautioni

The sequence AAA18431.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAC15950.1 differs from that shown. Reason: Frameshift at positions 24, 44, 671 and 683. Curated
The sequence CAA88307.1 differs from that shown. Reason: Frameshift at position 5024. Curated
The sequence CAH56330.1 differs from that shown. Reason: Frameshift at position 4616. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211S → R in AAC15950. (PubMed:9506983)Curated
Sequence conflicti432 – 4321D → G in AAC15950. (PubMed:9506983)Curated
Sequence conflicti549 – 5491P → L in AAC15950. (PubMed:9506983)Curated
Sequence conflicti658 – 6581V → M in AAC15950. (PubMed:9506983)Curated
Sequence conflicti702 – 7021T → I in AAC15950. (PubMed:9506983)Curated
Sequence conflicti716 – 7161T → A in AAC15950. (PubMed:9506983)Curated
Sequence conflicti817 – 8182GD → RG in AAC15950. (PubMed:9506983)Curated
Sequence conflicti869 – 8691E → K in AAC15950. (PubMed:9506983)Curated
Sequence conflicti978 – 9781G → R in AAC15950. (PubMed:9506983)Curated
Sequence conflicti996 – 9961Q → R in AAC15950. (PubMed:9506983)Curated
Sequence conflicti1803 – 18031E → N AA sequence (PubMed:2656675)Curated
Sequence conflicti2176 – 21761E → N AA sequence (PubMed:2656675)Curated
Non-adjacent residuesi2448 – 24492Curated
Sequence conflicti3004 – 30041E → N AA sequence (PubMed:2656675)Curated
Non-adjacent residuesi3797 – 37982Curated
Sequence conflicti3990 – 39912VS → HE in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4203 – 42031P → R in CAA88307. (PubMed:7775418)Curated
Sequence conflicti4260 – 42623SPR → RPP in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4275 – 42751G → A in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4389 – 43891G → A in CAA88307. (PubMed:7775418)Curated
Sequence conflicti4457 – 44604VVAS → HASA in AAH33831. (PubMed:15489334)Curated
Sequence conflicti4524 – 45241H → Q in CAA04737. (PubMed:9620876)Curated
Sequence conflicti4524 – 45241H → Q in CAA04738. (PubMed:9620876)Curated
Sequence conflicti4569 – 45691A → R in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4621 – 46211R → P in CAA88307. (PubMed:7775418)Curated
Sequence conflicti4640 – 46401S → T in CAA04737. (PubMed:9620876)Curated
Sequence conflicti4640 – 46401S → T in CAA04738. (PubMed:9620876)Curated
Sequence conflicti4732 – 47321G → R in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4739 – 47391A → R in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4809 – 48091G → R in AAA18431. (PubMed:7513696)Curated
Sequence conflicti4922 – 49221C → S in AAA18431. (PubMed:7513696)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4897 – 48971L → P.2 Publications
Corresponds to variant rs1132436 [ dbSNP | Ensembl ].
VAR_036832

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298317 mRNA. Translation: CAC83674.1.
AJ298318 Genomic DNA. Translation: CAC83675.1.
AJ298319 Genomic DNA. Translation: CAC83676.1.
AF015521 mRNA. Translation: AAC15950.1. Frameshift.
X81649 mRNA. Translation: CAA57309.1.
AJ001402 mRNA. Translation: CAA04737.1.
AJ001403 Genomic DNA. Translation: CAA04738.1.
U06711 mRNA. Translation: AAA18431.1. Frameshift.
Z48314 mRNA. Translation: CAA88307.1. Frameshift.
BC033831 mRNA. Translation: AAH33831.1.
AL833060 mRNA. Translation: CAH56330.1. Frameshift.
PIRiA33811.
JE0095.
UniGeneiHs.534332.
Hs.558950.
Hs.721515.

Polymorphism databases

DMDMi160370004.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mucin database
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298317 mRNA. Translation: CAC83674.1 .
AJ298318 Genomic DNA. Translation: CAC83675.1 .
AJ298319 Genomic DNA. Translation: CAC83676.1 .
AF015521 mRNA. Translation: AAC15950.1 . Frameshift.
X81649 mRNA. Translation: CAA57309.1 .
AJ001402 mRNA. Translation: CAA04737.1 .
AJ001403 Genomic DNA. Translation: CAA04738.1 .
U06711 mRNA. Translation: AAA18431.1 . Frameshift.
Z48314 mRNA. Translation: CAA88307.1 . Frameshift.
BC033831 mRNA. Translation: AAH33831.1 .
AL833060 mRNA. Translation: CAH56330.1 . Frameshift.
PIRi A33811.
JE0095.
UniGenei Hs.534332.
Hs.558950.
Hs.721515.

3D structure databases

ProteinModelPortali P98088.
SMRi P98088. Positions 336-394, 800-873, 4589-4652, 4903-4994.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P98088. 1 interaction.

Protein family/group databases

MEROPSi I08.951.

PTM databases

UniCarbKBi P98088.

Polymorphism databases

DMDMi 160370004.

Proteomic databases

MaxQBi P98088.
PRIDEi P98088.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC11P001151.
H-InvDB HIX0201650.
HGNCi HGNC:7515. MUC5AC.
HPAi CAB002774.
CAB009395.
HPA040615.
MIMi 158373. gene.
neXtProti NX_P98088.
GenAtlasi Search...

Phylogenomic databases

InParanoidi P98088.

Enzyme and pathway databases

Reactomei REACT_115606. O-linked glycosylation of mucins.
REACT_115835. Termination of O-glycan biosynthesis.

Miscellaneous databases

NextBioi 125477.
PROi P98088.
SOURCEi Search...

Gene expression databases

Genevestigatori P98088.

Family and domain databases

InterProi IPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
IPR025155. WxxW_domain.
[Graphical view ]
Pfami PF08742. C8. 4 hits.
PF13330. Mucin2_WxxW. 9 hits.
PF01826. TIL. 3 hits.
PF00094. VWD. 4 hits.
[Graphical view ]
SMARTi SM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00214. VWC. 6 hits.
SM00216. VWD. 4 hits.
[Graphical view ]
SUPFAMi SSF57567. SSF57567. 4 hits.
PROSITEi PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
PS51233. VWFD. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human mucin gene MUC5AC: organization of its 5'-region and central repetitive region."
    Escande F., Aubert J.-P., Porchet N., Buisine M.P.
    Biochem. J. 358:763-772(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2448, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2449-3797, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3798-4169.
  2. "Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC mucin gene and transcriptional up-regulation by bacterial exoproducts."
    Li D., Gallup M., Fan N., Szymkowski D.E., Basbaum C.B.
    J. Biol. Chem. 273:6812-6820(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1104.
    Tissue: Trachea.
  3. "Cloning and analysis of human gastric mucin cDNA reveals two types of conserved cysteine-rich domains."
    Klomp L.W., Van Rens L., Strous G.J.
    Biochem. J. 308:831-838(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1854.
  4. "Proteolytic fragmentation and peptide mapping of human carboxyamidomethylated tracheobronchial mucin."
    Rose M.C., Kaufman B., Martin B.M.
    J. Biol. Chem. 264:8193-8199(1989) [PubMed] [Europe PMC] [Abstract]
    Tissue: Tracheobronchial mucosa.
  5. "Genomic organization of the 3'-region of the human MUC5AC mucin gene: additional evidence for a common ancestral gene for the 11p15.5 mucin gene family."
    Buisine M.P., Desseyn J.-L., Porchet N., Degand P., Laine A., Aubert J.-P.
    Biochem. J. 332:729-738(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 3950-5030, VARIANT PRO-4897.
    Tissue: Placenta and Trachea.
  6. "Cloning and analysis of cDNA encoding a major airway glycoprotein, human tracheobronchial mucin (MUC5)."
    Meerzaman D., Charles P., Daskal E., Polymeropoulos M.H., Martin B.M., Rose M.C.
    J. Biol. Chem. 269:12932-12939(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3990-5030, PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
    Tissue: Nasal polyp.
  7. "Characterization of a mucin cDNA clone isolated from HT-29 mucus secreting cells: the 3' end of MUC5AC?"
    Lesuffleur T., Roche F., Hill A.S., Lacasa M., Fox M., Swallow D.M., Zweibaum A., Real F.X.
    J. Biol. Chem. 270:13665-13673(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4081-5030.
  8. "Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin."
    Lidell M.E., Hansson G.C.
    Biochem. J. 399:121-129(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 4303-4312, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-4302.
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4457-5030, VARIANT PRO-4897.
    Tissue: Colon.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4569-5030.
    Tissue: Stomach.
  11. Cited for: STRUCTURE OF O-LINKED CARBOHYDRATES.
  12. "The MUC5AC glycoprotein is the primary receptor for Helicobacter pylori in the human stomach."
    Van de Bovenkamp J.H., Mahdavi J., Korteland-Van Male A.M., Bueller H.A., Einerhand A.W., Boren T., Dekker J.
    Helicobacter 8:521-532(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS LEWIS B BLOOD GROUP ANTIGEN, TISSUE SPECIFICITY, INTERACTION WITH HELICOBACTER PYLORI.
  13. "C-Mannosylation of MUC5AC and MUC5B Cys subdomains."
    Perez-Vilar J., Randell S.H., Boucher R.C.
    Glycobiology 14:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-2122, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-2122.

Entry informationi

Entry nameiMUC5A_HUMAN
AccessioniPrimary (citable) accession number: P98088
Secondary accession number(s): O60460
, O76065, Q13792, Q14425, Q658Q1, Q7M4S5, Q8N4M9, Q8WWQ3, Q8WWQ4, Q8WWQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 23, 2007
Last modified: October 1, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3