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Q6ICB4

- SESQ2_HUMAN

UniProt

Q6ICB4 - SESQ2_HUMAN

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Protein

Sesquipedalian-2

Gene

FAM109B

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

Functioni

Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.1 Publication

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. endosome organization Source: UniProtKB
  2. receptor recycling Source: UniProtKB
  3. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Sesquipedalian-2
Short name:
Ses2
Alternative name(s):
27 kDa inositol polyphosphate phosphatase interacting protein B
Short name:
IPIP27B
Gene namesi
Name:FAM109B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:27161. FAM109B.

Subcellular locationi

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.

GO - Cellular componenti

  1. clathrin-coated vesicle Source: UniProtKB
  2. early endosome Source: UniProtKB
  3. recycling endosome Source: UniProtKB
  4. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi224 – 2241F → A: Loss of OCRL-binding. 1 Publication
Mutagenesisi228 – 2281H → A: Loss of OCRL-binding. 1 Publication
Mutagenesisi234 – 2352EI → AA: Loss of OCRL-binding. 1 Publication

Organism-specific databases

PharmGKBiPA143485467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259Sesquipedalian-2PRO_0000254133Add
BLAST

Proteomic databases

MaxQBiQ6ICB4.
PaxDbiQ6ICB4.
PRIDEiQ6ICB4.

PTM databases

PhosphoSiteiQ6ICB4.

Expressioni

Gene expression databases

BgeeiQ6ICB4.
CleanExiHS_FAM109B.
ExpressionAtlasiQ6ICB4. baseline and differential.
GenevestigatoriQ6ICB4.

Organism-specific databases

HPAiHPA000647.

Interactioni

Subunit structurei

Forms homodimers and heterodimers with FAM109A. Interacts with OCRL and INPP5B.2 Publications

Protein-protein interaction databases

BioGridi127287. 1 interaction.
STRINGi9606.ENSP00000312753.

Structurei

3D structure databases

ProteinModelPortaliQ6ICB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 121105PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili124 – 14926Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi223 – 23513F&HAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the sesquipedalian family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG117159.
GeneTreeiENSGT00440000034671.
HOVERGENiHBG061708.
InParanoidiQ6ICB4.
OMAiLRTWGGP.
OrthoDBiEOG7966HQ.
PhylomeDBiQ6ICB4.
TreeFamiTF326731.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6ICB4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLNERSVAH YALSDSPADH MGFLRTWGGP GTPPTPSGTG RRCWFVLKGN
60 70 80 90 100
LLFSFESREG RAPLSLVVLE GCTVELAEAP VPEEFAFAIC FDAPGVRPHL
110 120 130 140 150
LAAEGPAAQE AWVKVLSRAS FGYMRLVVRE LESQLQDARQ SLALQRRSSW
160 170 180 190 200
KSVASRCKPQ APNHRAAGLE NGHCLSKDSS PVGLVEEAGS RSAGWGLAEW
210 220 230 240 250
ELQGPASLLL GKGQSPVSPE TSCFSTLHDW YGQEIVELRQ CWQKRAQGSH

SKCEEQDRP
Length:259
Mass (Da):28,338
Last modified:July 5, 2004 - v1
Checksum:iF82FDD0D2314BB0F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881A → G.1 Publication
Corresponds to variant rs1807493 [ dbSNP | Ensembl ].
VAR_028822

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33655.1.
RefSeqiNP_001002034.2. NM_001002034.2.
XP_005261430.1. XM_005261373.1.
UniGeneiHs.368312.

Genome annotation databases

EnsembliENST00000321753; ENSP00000312753; ENSG00000177096.
GeneIDi150368.
KEGGihsa:150368.
UCSCiuc003bbz.3. human.

Polymorphism databases

DMDMi74757717.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS33655.1.
RefSeqi NP_001002034.2. NM_001002034.2.
XP_005261430.1. XM_005261373.1.
UniGenei Hs.368312.

3D structure databases

ProteinModelPortali Q6ICB4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127287. 1 interaction.
STRINGi 9606.ENSP00000312753.

PTM databases

PhosphoSitei Q6ICB4.

Polymorphism databases

DMDMi 74757717.

Proteomic databases

MaxQBi Q6ICB4.
PaxDbi Q6ICB4.
PRIDEi Q6ICB4.

Protocols and materials databases

DNASUi 150368.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321753 ; ENSP00000312753 ; ENSG00000177096 .
GeneIDi 150368.
KEGGi hsa:150368.
UCSCi uc003bbz.3. human.

Organism-specific databases

CTDi 150368.
GeneCardsi GC22P042470.
HGNCi HGNC:27161. FAM109B.
HPAi HPA000647.
neXtProti NX_Q6ICB4.
PharmGKBi PA143485467.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG117159.
GeneTreei ENSGT00440000034671.
HOVERGENi HBG061708.
InParanoidi Q6ICB4.
OMAi LRTWGGP.
OrthoDBi EOG7966HQ.
PhylomeDBi Q6ICB4.
TreeFami TF326731.

Miscellaneous databases

GenomeRNAii 150368.
NextBioi 86424.
PROi Q6ICB4.

Gene expression databases

Bgeei Q6ICB4.
CleanExi HS_FAM109B.
ExpressionAtlasi Q6ICB4. baseline and differential.
Genevestigatori Q6ICB4.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
PROSITEi PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiSESQ2_HUMAN
AccessioniPrimary (citable) accession number: Q6ICB4
Secondary accession number(s): Q3SXQ3, Q8N6L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 82 of the entry and version 1 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

Miscellaneous

Was named after 'sesquipedalian', an unnecessarily long description of a simple thing.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3