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O15127 (SCAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Secretory carrier-associated membrane protein 2

Short name=Secretory carrier membrane protein 2
Gene names
Name:SCAMP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.

Subunit structure

Interacts with SLC6A4 and SLC9A7. Ref.6 Ref.7

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein Ref.6.

Tissue specificity

Widely expressed.

Sequence similarities

Belongs to the SCAMP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Secretory carrier-associated membrane protein 2
PRO_0000191254

Regions

Topological domain1 – 153153Cytoplasmic Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 1817Lumenal Potential
Transmembrane182 – 20221Helical; Potential
Topological domain203 – 21816Cytoplasmic Potential
Transmembrane219 – 23921Helical; Potential
Topological domain240 – 26223Lumenal Potential
Transmembrane263 – 28321Helical; Potential
Topological domain284 – 32946Cytoplasmic Potential
Region203 – 21816Interaction with SLC9A7

Amino acid modifications

Modified residue3191Phosphoserine Ref.10
Modified residue3201Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
O15127 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 046ACB926FD951DD

FASTA32936,649
        10         20         30         40         50         60 
MSAFDTNPFA DPVDVNPFQD PSVTQLTNAP QGGLAEFNPF SETNAATTVP VTQLPGSSQP 

        70         80         90        100        110        120 
AVLQPSVEPT QPTPQAVVSA AQAGLLRQQE ELDRKAAELE RKERELQNTV ANLHVRQNNW 

       130        140        150        160        170        180 
PPLPSWCPVK PCFYQDFSTE IPADYQRICK MLYYLWMLHS VTLFLNLLAC LAWFSGNSSK 

       190        200        210        220        230        240 
GVDFGLSILW FLIFTPCAFL CWYRPIYKAF RSDNSFSFFV FFFVFFCQIG IYIIQLVGIP 

       250        260        270        280        290        300 
GLGDSGWIAA LSTLDNHSLA ISVIMMVVAG FFTLCAVLSV FLLQRVHSLY RRTGASFQQA 

       310        320 
QEEFSQGIFS SRTFHRAASS AAQGAFQGN 

« Hide

References

« Hide 'large scale' references
[1]"Three mammalian SCAMPs (secretory carrier membrane proteins) are highly related products of distinct genes having similar subcellular distributions."
Singleton D.R., Wu T.T., Castle J.D.
J. Cell Sci. 110:2099-2107(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Singleton D.R., Wu T.T., Castle J.D.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Skin.
[6]"Secretory carrier membrane proteins interact and regulate trafficking of the organellar (Na+,K+)/H+ exchanger NHE7."
Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.
J. Cell Sci. 118:1885-1897(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SLC9A7.
[7]"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC6A4.
[8]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005038 mRNA. Translation: AAB62723.2.
AK315516 mRNA. Translation: BAG37897.1.
CH471136 Genomic DNA. Translation: EAW99300.1.
BC001376 mRNA. Translation: AAH01376.1.
BC004385 mRNA. Translation: AAH04385.1.
CCDSCCDS10271.1.
RefSeqNP_005688.2. NM_005697.3.
UniGeneHs.458917.

3D structure databases

ProteinModelPortalO15127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115377. 6 interactions.
IntActO15127. 4 interactions.
MINTMINT-5003778.
STRING9606.ENSP00000268099.

PTM databases

PhosphoSiteO15127.

Proteomic databases

MaxQBO15127.
PaxDbO15127.
PeptideAtlasO15127.
PRIDEO15127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268099; ENSP00000268099; ENSG00000140497.
GeneID10066.
KEGGhsa:10066.
UCSCuc002azb.1. human.

Organism-specific databases

CTD10066.
GeneCardsGC15M075136.
HGNCHGNC:10564. SCAMP2.
HPAHPA014699.
HPA019194.
MIM606912. gene.
neXtProtNX_O15127.
PharmGKBPA34977.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285953.
HOGENOMHOG000294221.
HOVERGENHBG071938.
InParanoidO15127.
OMASIIMMVV.
OrthoDBEOG7FZ009.
PhylomeDBO15127.
TreeFamTF313797.

Gene expression databases

ArrayExpressO15127.
BgeeO15127.
CleanExHS_SCAMP2.
GenevestigatorO15127.

Family and domain databases

InterProIPR007273. SCAMP.
[Graphical view]
PANTHERPTHR10687. PTHR10687. 1 hit.
PfamPF04144. SCAMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSCAMP2. human.
GeneWikiSCAMP2.
GenomeRNAi10066.
NextBio38041.
PROO15127.
SOURCESearch...

Entry information

Entry nameSCAM2_HUMAN
AccessionPrimary (citable) accession number: O15127
Secondary accession number(s): B2RDF0, Q9BQE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 11, 2001
Last modified: July 9, 2014
This is version 112 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM