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Q6ICB4 (SESQ2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Sesquipedalian-2

Short name=Ses2
Alternative name(s):
27 kDa inositol polyphosphate phosphatase interacting protein B
Short name=IPIP27B
Gene names
Name:FAM109B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Ref.5

Subunit structure

Forms homodimers and heterodimers with FAM109A. Interacts with OCRL and INPP5B. Ref.4 Ref.5

Subcellular location

Early endosome. Recycling endosome. Golgi apparatustrans-Golgi network. Cytoplasmic vesicleclathrin-coated vesicle. Note: Also found on macropinosomes. Not detected in late endosomes, nor in lysosomes. Ref.4 Ref.5

Domain

The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B.

Miscellaneous

Was named after 'sesquipedalian', an unnecessarily long description of a simple thing (Ref.4).

Sequence similarities

Belongs to the sesquipedalian family.

Contains 1 PH domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Sesquipedalian-2
PRO_0000254133

Regions

Domain17 – 121105PH
Coiled coil124 – 14926 Potential
Motif223 – 23513F&H

Natural variations

Natural variant1881A → G. Ref.3
Corresponds to variant rs1807493 [ dbSNP | Ensembl ].
VAR_028822

Experimental info

Mutagenesis2241F → A: Loss of OCRL-binding. Ref.5
Mutagenesis2281H → A: Loss of OCRL-binding. Ref.5
Mutagenesis234 – 2352EI → AA: Loss of OCRL-binding.

Sequences

Sequence LengthMass (Da)Tools
Q6ICB4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F82FDD0D2314BB0F

FASTA25928,338
        10         20         30         40         50         60 
MKLNERSVAH YALSDSPADH MGFLRTWGGP GTPPTPSGTG RRCWFVLKGN LLFSFESREG 

        70         80         90        100        110        120 
RAPLSLVVLE GCTVELAEAP VPEEFAFAIC FDAPGVRPHL LAAEGPAAQE AWVKVLSRAS 

       130        140        150        160        170        180 
FGYMRLVVRE LESQLQDARQ SLALQRRSSW KSVASRCKPQ APNHRAAGLE NGHCLSKDSS 

       190        200        210        220        230        240 
PVGLVEEAGS RSAGWGLAEW ELQGPASLLL GKGQSPVSPE TSCFSTLHDW YGQEIVELRQ 

       250 
CWQKRAQGSH SKCEEQDRP 

« Hide

References

« Hide 'large scale' references
[1]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT GLY-188.
Tissue: Colon.
[4]"Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OCRL, F&H MOTIF, SUBCELLULAR LOCATION.
[5]"The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
Noakes C.J., Lee G., Lowe M.
Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH OCRL AND INPP5B, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-224; HIS-228 AND 234-GLU-ILE-235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR456454 mRNA. Translation: CAG30340.1.
Z99716, Z82192 Genomic DNA. Translation: CAI41696.1.
Z82192, Z99716 Genomic DNA. Translation: CAI19712.1.
BC029776 mRNA. Translation: AAH29776.1.
BC104175 mRNA. Translation: AAI04176.1.
BC104176 mRNA. Translation: AAI04177.1.
CCDSCCDS33655.1.
RefSeqNP_001002034.2. NM_001002034.2.
XP_005261430.1. XM_005261373.1.
UniGeneHs.368312.

3D structure databases

ProteinModelPortalQ6ICB4.
SMRQ6ICB4. Positions 39-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127287. 1 interaction.
STRING9606.ENSP00000312753.

PTM databases

PhosphoSiteQ6ICB4.

Polymorphism databases

DMDM74757717.

Proteomic databases

PaxDbQ6ICB4.
PRIDEQ6ICB4.

Protocols and materials databases

DNASU150368.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321753; ENSP00000312753; ENSG00000177096.
ENST00000606597; ENSP00000475542; ENSG00000273121.
ENST00000607126; ENSP00000475303; ENSG00000273378.
GeneID150368.
KEGGhsa:150368.
UCSCuc003bbz.3. human.

Organism-specific databases

CTD150368.
GeneCardsGC22P042470.
HGNCHGNC:27161. FAM109B.
HPAHPA000647.
neXtProtNX_Q6ICB4.
PharmGKBPA143485467.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG117159.
HOVERGENHBG061708.
InParanoidQ6ICB4.
OMALRTWGGP.
OrthoDBEOG7966HQ.
PhylomeDBQ6ICB4.
TreeFamTF326731.

Gene expression databases

ArrayExpressQ6ICB4.
BgeeQ6ICB4.
CleanExHS_FAM109B.
GenevestigatorQ6ICB4.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi150368.
NextBio86424.
PROQ6ICB4.

Entry information

Entry nameSESQ2_HUMAN
AccessionPrimary (citable) accession number: Q6ICB4
Secondary accession number(s): Q3SXQ3, Q8N6L9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 79 of the entry and version 1 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

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 22

Human chromosome 22: entries, gene names and cross-references to MIM