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P30626

- SORCN_HUMAN

UniProt

P30626 - SORCN_HUMAN

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

Functioni

Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi83 – 94121 Inferred
Add
BLAST
Calcium bindingi113 – 124122 Inferred
Add
BLAST

GO - Molecular functioni

  1. calcium channel regulator activity Source: ProtInc
  2. calcium ion binding Source: BHF-UCL
  3. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
  4. ion channel binding Source: BHF-UCL
  5. protease binding Source: BHF-UCL
  6. protein binding Source: IntAct
  7. protein heterodimerization activity Source: BHF-UCL
  8. receptor binding Source: ProtInc

GO - Biological processi

  1. action potential Source: ProtInc
  2. calcium ion transport Source: Ensembl
  3. cytoplasmic sequestering of transcription factor Source: Ensembl
  4. heart development Source: ProtInc
  5. intracellular sequestering of iron ion Source: ProtInc
  6. muscle organ development Source: ProtInc
  7. negative regulation of heart rate Source: BHF-UCL
  8. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  9. negative regulation of transcription regulatory region DNA binding Source: Ensembl
  10. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
  11. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  12. proteolysis Source: RefGenome
  13. regulation of calcium ion transport Source: BHF-UCL
  14. regulation of cardiac muscle cell contraction Source: BHF-UCL
  15. regulation of cell communication by electrical coupling Source: BHF-UCL
  16. regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  17. regulation of heart contraction Source: ProtInc
  18. regulation of high voltage-gated calcium channel activity Source: BHF-UCL
  19. regulation of relaxation of muscle Source: BHF-UCL
  20. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  21. regulation of striated muscle contraction Source: ProtInc
  22. signal transduction Source: UniProtKB
  23. transport Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorcin
Alternative name(s):
22 kDa protein
CP-22
Short name:
CP22
V19
Gene namesi
Name:SRI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:11292. SRI.

Subcellular locationi

Cytoplasm. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
Note: Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels.

GO - Cellular componenti

  1. T-tubule Source: BHF-UCL
  2. Z disc Source: BHF-UCL
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: BHF-UCL
  5. endoplasmic reticulum membrane Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProt
  7. membrane Source: BHF-UCL
  8. sarcoplasmic reticulum Source: BHF-UCL
  9. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121F → L: Reduces affinity for calcium 5-fold.

Organism-specific databases

PharmGKBiPA36117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Sorcin
PRO_0000073725Add
BLAST

Proteomic databases

MaxQBiP30626.
PaxDbiP30626.
PRIDEiP30626.

2D gel databases

OGPiP30626.

PTM databases

PhosphoSiteiP30626.

Expressioni

Tissue specificityi

Detected in cardiac myocytes.

Gene expression databases

ArrayExpressiP30626.
BgeeiP30626.
CleanExiHS_SRI.
GenevestigatoriP30626.

Organism-specific databases

HPAiHPA019004.

Interactioni

Subunit structurei

Homodimer. Interacts with GCA, RYR2 and ANXA7.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAT3P407632EBI-750459,EBI-518675

Protein-protein interaction databases

BioGridi112595. 20 interactions.
IntActiP30626. 10 interactions.
MINTiMINT-4999795.
STRINGi9606.ENSP00000265729.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 438
Turni44 – 474
Helixi51 – 6111
Turni62 – 643
Beta strandi65 – 684
Helixi72 – 8211
Beta strandi84 – 863
Helixi92 – 11019
Beta strandi118 – 1203
Helixi122 – 13110
Helixi138 – 14710
Beta strandi150 – 1556
Helixi156 – 17520
Helixi178 – 1803
Beta strandi182 – 1876
Helixi188 – 1958

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JUOX-ray2.20A/B1-198[»]
2JC2X-ray2.50A/B/C/D1-198[»]
ProteinModelPortaliP30626.
SMRiP30626. Positions 27-198.

Miscellaneous databases

EvolutionaryTraceiP30626.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6436EF-hand 1
Add
BLAST
Domaini70 – 10334EF-hand 2
Add
BLAST
Domaini100 – 13536EF-hand 3
Add
BLAST
Domaini134 – 16936EF-hand 4
Add
BLAST

Sequence similaritiesi

Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG298587.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
OMAiIQCVMSI.
OrthoDBiEOG7RV9FM.
PhylomeDBiP30626.
TreeFamiTF314682.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P30626-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAYPGHPGAG GGYYPGGYGG APGGPAFPGQ TQDPLYGYFA AVAGQDGQID    50
ADELQRCLTQ SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA 100
VLNGWRQHFI SFDTDRSGTV DPQELQKALT TMGFRLSPQA VNSIAKRYST 150
NGKITFDDYI ACCVKLRALT DSFRRRDTAQ QGVVNFPYDD FIQCVMSV 198
Length:198
Mass (Da):21,676
Last modified:April 1, 1993 - v1
Checksum:iA4829C7650A5E3FA
GO
Isoform 2 (identifier: P30626-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MAYPGHPGAGGGYYPGG → MQ

Note: No experimental confirmation available.

Show »
Length:183
Mass (Da):20,345
Checksum:iA6B23B49FF8B9778
GO
Isoform 3 (identifier: P30626-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MAYPGHPGAGGGYYPGG → MQ
     191-198: FIQCVMSV → VSLRN

Note: No experimental confirmation available.

Show »
Length:180
Mass (Da):20,006
Checksum:i2F652A7283896808
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717MAYPG…YYPGG → MQ in isoform 2 and isoform 3.
VSP_046277Add
BLAST
Alternative sequencei191 – 1988FIQCVMSV → VSLRN in isoform 3.
VSP_054463

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12387 mRNA. Translation: AAA92155.1.
M32886 mRNA. Translation: AAA60588.1.
AK296601 mRNA. Translation: BAG59214.1.
BM739144 mRNA. No translation available.
AC003991 Genomic DNA. No translation available.
AC005075 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW76909.1.
CH471091 Genomic DNA. Translation: EAW76910.1.
BC011025 mRNA. Translation: AAH11025.1.
CCDSiCCDS47638.1. [P30626-2]
CCDS5612.1. [P30626-1]
CCDS59063.1. [P30626-3]
PIRiS52094.
RefSeqiNP_001243820.1. NM_001256891.1.
NP_001243821.1. NM_001256892.1. [P30626-3]
NP_003121.1. NM_003130.3. [P30626-1]
NP_944490.1. NM_198901.1. [P30626-2]
UniGeneiHs.489040.

Genome annotation databases

EnsembliENST00000265729; ENSP00000265729; ENSG00000075142. [P30626-1]
ENST00000394641; ENSP00000378137; ENSG00000075142. [P30626-2]
ENST00000431660; ENSP00000391148; ENSG00000075142.
GeneIDi6717.
KEGGihsa:6717.
UCSCiuc003ujq.2. human. [P30626-1]

Polymorphism databases

DMDMi267021.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L12387 mRNA. Translation: AAA92155.1 .
M32886 mRNA. Translation: AAA60588.1 .
AK296601 mRNA. Translation: BAG59214.1 .
BM739144 mRNA. No translation available.
AC003991 Genomic DNA. No translation available.
AC005075 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW76909.1 .
CH471091 Genomic DNA. Translation: EAW76910.1 .
BC011025 mRNA. Translation: AAH11025.1 .
CCDSi CCDS47638.1. [P30626-2 ]
CCDS5612.1. [P30626-1 ]
CCDS59063.1. [P30626-3 ]
PIRi S52094.
RefSeqi NP_001243820.1. NM_001256891.1.
NP_001243821.1. NM_001256892.1. [P30626-3 ]
NP_003121.1. NM_003130.3. [P30626-1 ]
NP_944490.1. NM_198901.1. [P30626-2 ]
UniGenei Hs.489040.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JUO X-ray 2.20 A/B 1-198 [» ]
2JC2 X-ray 2.50 A/B/C/D 1-198 [» ]
ProteinModelPortali P30626.
SMRi P30626. Positions 27-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112595. 20 interactions.
IntActi P30626. 10 interactions.
MINTi MINT-4999795.
STRINGi 9606.ENSP00000265729.

PTM databases

PhosphoSitei P30626.

Polymorphism databases

DMDMi 267021.

2D gel databases

OGPi P30626.

Proteomic databases

MaxQBi P30626.
PaxDbi P30626.
PRIDEi P30626.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265729 ; ENSP00000265729 ; ENSG00000075142 . [P30626-1 ]
ENST00000394641 ; ENSP00000378137 ; ENSG00000075142 . [P30626-2 ]
ENST00000431660 ; ENSP00000391148 ; ENSG00000075142 .
GeneIDi 6717.
KEGGi hsa:6717.
UCSCi uc003ujq.2. human. [P30626-1 ]

Organism-specific databases

CTDi 6717.
GeneCardsi GC07M087834.
HGNCi HGNC:11292. SRI.
HPAi HPA019004.
MIMi 182520. gene.
neXtProti NX_P30626.
PharmGKBi PA36117.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298587.
HOGENOMi HOG000231982.
HOVERGENi HBG004492.
OMAi IQCVMSI.
OrthoDBi EOG7RV9FM.
PhylomeDBi P30626.
TreeFami TF314682.

Miscellaneous databases

ChiTaRSi SRI. human.
EvolutionaryTracei P30626.
GeneWikii SRI_(gene).
GenomeRNAii 6717.
NextBioi 26200.
PROi P30626.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30626.
Bgeei P30626.
CleanExi HS_SRI.
Genevestigatori P30626.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 2 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and molecular cloning of human sorcin a calcium-binding protein in vincristine-resistant HOB1 lymphoma cells."
    Wang S.L., Tam M.F., Ho Y.S., Pai S.H., Kao M.C.
    Biochim. Biophys. Acta 1260:285-293(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Purification, cDNA cloning, and expression of human sorcin in vincristine-resistant HOB1 lymphoma cell lines."
    Lee W.P.
    Arch. Biochem. Biophys. 325:217-226(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Isolation of the cDNA clone for human CP22 overexpressed in multidrug-resistant cell lines."
    Sugimoto Y., Asami N., Okochi E., Ogura M., Tsuruo T.
    Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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.
    , 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] (ISOFORM 3).
    Tissue: Colon.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Ascites.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Brain.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 57-116; 128-135 AND 154-165, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 128-135 AND 154-165.
    Tissue: Keratinocyte.
  11. "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro."
    Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.
    FEBS Lett. 545:151-154(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCA.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family."
    Xie X., Dwyer M.D., Swenson L., Parker M.H., Botfield M.C.
    Protein Sci. 10:2419-2425(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  14. "Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor."
    Franceschini S., Ilari A., Verzili D., Zamparelli C., Antaramian A., Rueda A., Valdivia H.H., Chiancone E., Colotti G.
    FASEB J. 22:295-306(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT LEU-112, SUBUNIT, FUNCTION, CALCIUM-BINDING, INTERACTION WITH RYR2 AND ANXA7.

Entry informationi

Entry nameiSORCN_HUMAN
AccessioniPrimary (citable) accession number: P30626
Secondary accession number(s): A8MTH6, B4DKK2, D6W5Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 3, 2014
This is version 153 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

This protein is encoded by an amplified gene in multidrug-resistant cells.
This protein has been shown to bind calcium with high affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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