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Q9ULV0 (MYO5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-Vb
Gene names
Name:MYO5B
Synonyms:KIAA1119
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1848 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis By similarity. Ref.7 Ref.9 Ref.11

Subunit structure

Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with RAB11FIP2, RAB11A, and RAB8A. Found in a complex with CFTR and RAB11A. Interacts with NPC1L1. Ref.5 Ref.6 Ref.7 Ref.9 Ref.11

Involvement in disease

Diarrhea 2, with microvillus atrophy (DIAR2) [MIM:251850]: A disease characterized by onset of intractable life-threatening watery diarrhea during infancy. Two forms are recognized: early-onset microvillus inclusion disease with diarrhea beginning in the neonatal period, and late-onset, with first symptoms appearing after 3 or 4 months of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 1 dilute domain.

Contains 6 IQ domains.

Contains 1 myosin motor domain.

Sequence caution

The sequence BAA86433.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18481848Unconventional myosin-Vb
PRO_0000123460

Regions

Domain69 – 761693Myosin motor
Domain769 – 79830IQ 1
Domain792 – 82130IQ 2
Domain817 – 84832IQ 3
Domain840 – 86930IQ 4
Domain865 – 89632IQ 5
Domain888 – 91730IQ 6
Domain1526 – 1803278Dilute
Nucleotide binding163 – 1708ATP Potential
Region640 – 66223Actin-binding Potential
Coiled coil899 – 1266368 Potential
Coiled coil1341 – 1471131 Potential
Compositional bias801 – 916116Arg-rich

Amino acid modifications

Modified residue14461Phosphoserine Ref.10

Natural variations

Natural variant101C → G.
Corresponds to variant rs16951438 [ dbSNP | Ensembl ].
VAR_056182
Natural variant1081V → G in DIAR2. Ref.13
VAR_054993
Natural variant1261T → A. Ref.1 Ref.3
Corresponds to variant rs1815930 [ dbSNP | Ensembl ].
VAR_063141
Natural variant2191R → H in DIAR2. Ref.13
VAR_054994
Natural variant3071K → N.
Corresponds to variant rs17659179 [ dbSNP | Ensembl ].
VAR_056183
Natural variant6561R → C in DIAR2. Ref.13
VAR_054995
Natural variant9181R → H.
Corresponds to variant rs2298624 [ dbSNP | Ensembl ].
VAR_056184
Natural variant9421K → R.
Corresponds to variant rs2277716 [ dbSNP | Ensembl ].
VAR_056185
Natural variant10551L → LL. Ref.1 Ref.3
Corresponds to variant rs72530399 [ dbSNP | Ensembl ].
VAR_063142

Experimental info

Mutagenesis13001Q → L: Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with C-1307. Ref.11
Mutagenesis13071Y → C: Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with L-1300. Ref.11
Mutagenesis17141Y → E: Abolishes interaction with RAB11A; has no effect on RAB8A interaction. Ref.11
Mutagenesis17481Q → R: Abolishes interaction with RAB11A; has no effect on RAB8A interaction. Ref.11

Secondary structure

.................................................. 1848
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ULV0 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 4EB8FA02F6B38707

FASTA1,848213,672
        10         20         30         40         50         60 
MSVGELYSQC TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDETILEY PIDVQRNQLP 

        70         80         90        100        110        120 
FLRNPDILVG ENDLTALSYL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG 

       130        140        150        160        170        180 
QDVIYTYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF 

       190        200        210        220        230        240 
ATVGGSASET NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKYIQIGFDK RYHIIGANMR 

       250        260        270        280        290        300 
TYLLEKSRVV FQADDERNYH IFYQLCAAAG LPEFKELALT SAEDFFYTSQ GGDTSIEGVD 

       310        320        330        340        350        360 
DAEDFEKTRQ AFTLLGVKES HQMSIFKIIA SILHLGSVAI QAERDGDSCS ISPQDVYLSN 

       370        380        390        400        410        420 
FCRLLGVEHS QMEHWLCHRK LVTTSETYVK TMSLQQVINA RNALAKHIYA QLFGWIVEHI 

       430        440        450        460        470        480 
NKALHTSLKQ HSFIGVLDIY GFETFEVNSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK 

       490        500        510        520        530        540 
EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYD RHSSSQHFQK 

       550        560        570        580        590        600 
PRMSNTAFII VHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFHDDKDPVP 

       610        620        630        640        650        660 
ATTPGKGSSS KISVRSARPP MKVSNKEHKK TVGHQFRTSL HLLMETLNAT TPHYVRCIKP 

       670        680        690        700        710        720 
NDEKLPFHFD PKRAVQQLRA CGVLETIRIS AAGYPSRWAY HDFFNRYRVL VKKRELANTD 

       730        740        750        760        770        780 
KKAICRSVLE NLIKDPDKFQ FGRTKIFFRA GQVAYLEKLR ADKFRTATIM IQKTVRGWLQ 

       790        800        810        820        830        840 
KVKYHRLKGA TLTLQRYCRG HLARRLAEHL RRIRAAVVLQ KHYRMQRARQ AYQRVRRAAV 

       850        860        870        880        890        900 
VIQAFTRAMF VRRTYRQVLM EHKATTIQKH VRGWMARRHF QRLRDAAIVI QCAFRMLKAR 

       910        920        930        940        950        960 
RELKALRIEA RSAEHLKRLN VGMENKVVQL QRKIDEQNKE FKTLSEQLSV TTSTYTMEVE 

       970        980        990       1000       1010       1020 
RLKKELVHYQ QSPGEDTSLR LQEEVESLRT ELQRAHSERK ILEDAHSREK DELRKRVADL 

      1030       1040       1050       1060       1070       1080 
EQENALLKDE KEQLNNQILC QSKDEFAQNS VKENLMKKEL EEERSRYQNL VKEYSQLEQR 

      1090       1100       1110       1120       1130       1140 
YDNLRDEMTI IKQTPGHRRN PSNQSSLESD SNYPSISTSE IGDTEDALQQ VEEIGLEKAA 

      1150       1160       1170       1180       1190       1200 
MDMTVFLKLQ KRVRELEQER KKLQVQLEKR EQQDSKKVQA EPPQTDIDLD PNADLAYNSL 

      1210       1220       1230       1240       1250       1260 
KRQELESENK KLKNDLNELR KAVADQATQN NSSHGSPDSY SLLLNQLKLA HEELEVRKEE 

      1270       1280       1290       1300       1310       1320 
VLILRTQIVS ADQRRLAGRN AEPNINARSS WPNSEKHVDQ EDAIEAYHGV CQTNSKTEDW 

      1330       1340       1350       1360       1370       1380 
GYLNEDGELG LAYQGLKQVA RLLEAQLQAQ SLEHEEEVEH LKAQLEALKE EMDKQQQTFC 

      1390       1400       1410       1420       1430       1440 
QTLLLSPEAQ VEFGVQQEIS RLTNENLDLK ELVEKLEKNE RKLKKQLKIY MKKAQDLEAA 

      1450       1460       1470       1480       1490       1500 
QALAQSERKR HELNRQVTVQ RKEKDFQGML EYHKEDEALL IRNLVTDLKP QMLSGTVPCL 

      1510       1520       1530       1540       1550       1560 
PAYILYMCIR HADYTNDDLK VHSLLTSTIN GIKKVLKKHN DDFEMTSFWL SNTCRLLHCL 

      1570       1580       1590       1600       1610       1620 
KQYSGDEGFM TQNTAKQNEH CLKNFDLTEY RQVLSDLSIQ IYQQLIKIAE GVLQPMIVSA 

      1630       1640       1650       1660       1670       1680 
MLENESIQGL SGVKPTGYRK RSSSMADGDN SYCLEAIIRQ MNAFHTVMCD QGLDPEIILQ 

      1690       1700       1710       1720       1730       1740 
VFKQLFYMIN AVTLNNLLLR KDVCSWSTGM QLRYNISQLE EWLRGRNLHQ SGAVQTMEPL 

      1750       1760       1770       1780       1790       1800 
IQAAQLLQLK KKTQEDAEAI CSLCTSLSTQ QIVKILNLYT PLNEFEERVT VAFIRTIQAQ 

      1810       1820       1830       1840 
LQERNDPQQL LLDAKHMFPV LFPFNPSSLT MDSIHIPACL NLEFLNEV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-126 AND LEU-1055 INS.
Tissue: Brain.
[2]Ohara O., Nagase T., Yamakawa H., Kikuno R.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS AND 918.
[3]"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: preparation of full-length cDNA clones encoding motor proteins."
Yamakawa H., Kikuno R.F., Nagase T., Ohara O.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-126 AND LEU-1055 INS.
Tissue: Brain.
[4]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Identification and characterization of a family of Rab11-interacting proteins."
Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.
J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP2.
[6]"CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling."
Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.
Mol. Biol. Cell 16:2470-2482(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CART COMPLEX.
[7]"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAB11A, IDENTIFICATION IN A COMPLEX WITH RAB11A AND CFTR.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPC1L1.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."
Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.
Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAB11A AND RAB8A, MUTAGENESIS OF GLN-1300; TYR-1307; TYR-1714 AND GLN-1748.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity."
Mueller T., Hess M.W., Schiefermeier N., Pfaller K., Ebner H.L., Heinz-Erian P., Ponstingl H., Partsch J., Roellinghoff B., Koehler H., Berger T., Lenhartz H., Schlenck B., Houwen R.J., Taylor C.J., Zoller H., Lechner S., Goulet O. expand/collapse author list , Utermann G., Ruemmele F.M., Huber L.A., Janecke A.R.
Nat. Genet. 40:1163-1165(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DIAR2 GLY-108; HIS-219 AND CYS-656.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032945 mRNA. Translation: BAA86433.2. Different initiation.
AB290160 mRNA. Translation: BAG06714.1.
AC090227 Genomic DNA. No translation available.
AC092705 Genomic DNA. No translation available.
AC105224 Genomic DNA. No translation available.
CCDSCCDS42436.1.
RefSeqNP_001073936.1. NM_001080467.2.
UniGeneHs.720076.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4J5MX-ray2.07A1453-1848[»]
4LNZX-ray3.11A1460-1848[»]
4LWZX-ray2.55B/D1456-1848[»]
4LX0X-ray2.19B/D1456-1848[»]
ProteinModelPortalQ9ULV0.
SMRQ9ULV0. Positions 5-816, 858-898, 1456-1848.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110729. 10 interactions.
IntActQ9ULV0. 4 interactions.
MINTMINT-1209283.
STRING9606.ENSP00000285039.

PTM databases

PhosphoSiteQ9ULV0.

Polymorphism databases

DMDM296439293.

Proteomic databases

MaxQBQ9ULV0.
PaxDbQ9ULV0.
PRIDEQ9ULV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285039; ENSP00000285039; ENSG00000167306.
GeneID4645.
KEGGhsa:4645.
UCSCuc002leb.2. human.

Organism-specific databases

CTD4645.
GeneCardsGC18M047349.
H-InvDBHIX0014446.
HGNCHGNC:7603. MYO5B.
HPAHPA040593.
HPA040902.
MIM251850. phenotype.
606540. gene.
neXtProtNX_Q9ULV0.
Orphanet2290. Microvillous inclusion disease.
PharmGKBPA31408.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000171839.
HOVERGENHBG052556.
InParanoidQ9ULV0.
KOK10357.
OMAQTMEPLI.
OrthoDBEOG7PK8XT.
PhylomeDBQ9ULV0.
TreeFamTF328771.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9ULV0.
BgeeQ9ULV0.
CleanExHS_MYO5B.
GenevestigatorQ9ULV0.

Family and domain databases

InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO5B. human.
GeneWikiMYO5B.
GenomeRNAi4645.
NextBio17900.
PROQ9ULV0.
SOURCESearch...

Entry information

Entry nameMYO5B_HUMAN
AccessionPrimary (citable) accession number: Q9ULV0
Secondary accession number(s): B0I1R3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM