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Q8IYB5 (SMAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromal membrane-associated protein 1
Gene names
Name:SMAP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis By similarity.

Subunit structure

Interacts with ARF6. Interacts with clathrin heavy chains via the clathrin box-like motif By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Tissue specificity

Detected in bone marrow, adrenal gland, trachea, lymph node, spinal cord, peripheral blood leukocytes, thyroid and stomach. Ref.1

Sequence similarities

Contains 1 Arf-GAP domain.

Sequence caution

The sequence AAH08672.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGTPase activation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processregulation of ARF GTPase activity

Inferred from electronic annotation. Source: InterPro

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionARF GTPase activator activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYB5-1)

Also known as: SMAP1A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8IYB5-2)

Also known as: SMAP1B;

The sequence of this isoform differs from the canonical sequence as follows:
     139-165: Missing.
Isoform 3 (identifier: Q8IYB5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     139-165: Missing.
     424-467: MNQQMAGMSI...GQTLSTQLWK → IMQKGDAVLQ...ESADGWHEYQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Stromal membrane-associated protein 1
PRO_0000235838

Regions

Domain18 – 136119Arf-GAP
Zinc finger33 – 5624C4-type
Motif218 – 2225Interaction with clathrin heavy chains By similarity

Natural variations

Alternative sequence139 – 16527Missing in isoform 2 and isoform 3.
VSP_018502
Alternative sequence424 – 46744MNQQM…TQLWK → IMQKGDAVLQHSISAIYWPM TRWLKCPLVDESADGWHEYQ in isoform 3.
VSP_018503
Natural variant2121A → V. Ref.4
Corresponds to variant rs2273566 [ dbSNP | Ensembl ].
VAR_048326

Experimental info

Sequence conflict3941P → H in AAH36123. Ref.6

Secondary structure

........................ 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SMAP1A) [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 75935CB6F9F99DA9

FASTA46750,386
        10         20         30         40         50         60 
MATRSCREKA QKLNEQHQLI LSKLLREEDN KYCADCEAKG PRWASWNIGV FICIRCAGIH 

        70         80         90        100        110        120 
RNLGVHISRV KSVNLDQWTA EQIQCMQDMG NTKARLLYEA NLPENFRRPQ TDQAVEFFIR 

       130        140        150        160        170        180 
DKYEKKKYYD KNAIAITNIS SSDAPLQPLV SSPSLQAAVD KNKLEKEKEK KKEEKKREKE 

       190        200        210        220        230        240 
PEKPAKPLTA EKLQKKDQQL EPKKSTSPKK AAEPTVDLLG LDGPAVAPVT NGNTTVPPLN 

       250        260        270        280        290        300 
DDLDIFGPMI SNPLPATVMP PAQGTPSAPA AATLSTVTSG DLDLFTEQTT KSEEVAKKQL 

       310        320        330        340        350        360 
SKDSILSLYG TGTIQQQSTP GVFMGPTNIP FTSQAPAAFQ GFPSMGVPVP AAPGLIGNVM 

       370        380        390        400        410        420 
GQSPSMMVGM PMPNGFMGNA QTGVMPLPQN VVGPQGGMVG QMGAPQSKFG LPQAQQPQWS 

       430        440        450        460 
LSQMNQQMAG MSISSATPTA GFGQPSSTTA GWSGSSSGQT LSTQLWK 

« Hide

Isoform 2 (SMAP1B) [UniParc].

Checksum: B7D7AE5387DB9E25
Show »

FASTA44047,609
Isoform 3 [UniParc].

Checksum: B4C4E780E6BEDCED
Show »

FASTA43647,862

References

« Hide 'large scale' references
[1]"Cloning, characterization and chromosome mapping of the human SMAP1 gene."
Marcos I., Borrego S., Rodriguez de Cordoba S., Galan J.J., Antinolo G.
Gene 292:167-171(2002) [PubMed: 12119110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Tissue: Blood and Bone marrow.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[3]Guo J.H., Zan Q., Yu L.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-212.
Tissue: Colon.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Ovary.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-467.
Tissue: Testis.
[8]"Solution structure of ARFGAP domain from human SMAP1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 9-136 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY055003 mRNA. Translation: AAL14714.1.
AY055004 mRNA. Translation: AAL14715.1.
AY055015 expand/collapse EMBL AC list , AY055005, AY055006, AY055007, AY055008, AY055009, AY055010, AY055011, AY055012, AY055013, AY055014 Genomic DNA. Translation: AAL14716.1.
AY055015 expand/collapse EMBL AC list , AY055005, AY055006, AY055007, AY055008, AY055010, AY055011, AY055012, AY055013, AY055014 Genomic DNA. Translation: AAL14717.1.
AK023221 mRNA. Translation: BAB14473.1.
AF442495 mRNA. Translation: AAP97320.1.
AK222711 mRNA. Translation: BAD96431.1.
AL354943, AL591049, AL121961 Genomic DNA. Translation: CAI12310.1.
AL354943, AL121961, AL591049 Genomic DNA. Translation: CAI12311.1.
AL354943, AL121961, AL591049 Genomic DNA. Translation: CAI12312.1.
AL591049, AL121961, AL354943 Genomic DNA. Translation: CAI14240.1.
AL591049, AL121961, AL354943 Genomic DNA. Translation: CAI14241.1.
AL591049, AL121961, AL354943 Genomic DNA. Translation: CAI14242.1.
AL121961, AL591049, AL354943 Genomic DNA. Translation: CAI42146.1.
AL121961, AL354943, AL591049 Genomic DNA. Translation: CAI42147.1.
AL121961, AL354943, AL591049 Genomic DNA. Translation: CAI42148.1.
BC008672 mRNA. Translation: AAH08672.1. Sequence problems.
BC028074 mRNA. Translation: AAH28074.1.
BC036123 mRNA. Translation: AAH36123.1.
AL833906 mRNA. Translation: CAD38762.1.
IPIIPI00102096.
IPI00185325.
IPI00604487.
RefSeqNP_001037770.1. NM_001044305.1.
NP_068759.2. NM_021940.3.
UniGeneHs.485717.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRRNMR-A9-136[»]
ProteinModelPortalQ8IYB5.
SMRQ8IYB5. Positions 9-141.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8IYB5.

PTM databases

PhosphoSiteQ8IYB5.

Polymorphism databases

DMDM97190718.

Proteomic databases

PRIDEQ8IYB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370455; ENSP00000359484; ENSG00000112305.
GeneID60682.
KEGGhsa:60682.
UCSCuc003pfr.1. human.
uc003pfs.1. human.
uc010kao.1. human.

Organism-specific databases

CTD60682.
GeneCardsGC06P071377.
H-InvDBHIX0005999.
HGNCHGNC:19651. SMAP1.
HPAHPA030574.
MIM611372. gene.
neXtProtNX_Q8IYB5.
PharmGKBPA134893764.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18336.
GeneTreeENSGT00530000062917.
HOVERGENHBG055260.
InParanoidQ8IYB5.
OMAAQQPQWS.
PhylomeDBQ8IYB5.

Gene expression databases

ArrayExpressQ8IYB5.
BgeeQ8IYB5.
CleanExHS_SMAP1.
GenevestigatorQ8IYB5.
GermOnlineENSG00000112305. Homo sapiens.

Family and domain databases

InterProIPR001164. ArfGAP.
[Graphical view]
KOK12486.
PfamPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00105. ArfGap. 1 hit.
[Graphical view]
SUPFAMSSF57863. ArfGAP. 1 hit.
PROSITEPS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio65508.
SOURCESearch...

Entry information

Entry nameSMAP1_HUMAN
AccessionPrimary (citable) accession number: Q8IYB5
Secondary accession number(s): Q53H70 expand/collapse secondary AC list , Q5SYQ2, Q6PK24, Q8NDH4, Q96L38, Q96L39, Q9H8X4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 80 of the entry and version 2 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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families