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Protein

Protein S100-A4

Gene

S100A4

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi20 – 33141; low affinityPROSITE-ProRule annotationAdd
BLAST
Calcium bindingi63 – 74122; high affinityPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB
  3. RAGE receptor binding Source: UniProtKB

GO - Biological processi

  1. epithelial to mesenchymal transition Source: HGNC
  2. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A4
Alternative name(s):
Calvasculin
Metastasin
Placental calcium-binding protein
Protein Mts1
S100 calcium-binding protein A4
Gene namesi
Name:S100A4
Synonyms:CAPL, MTS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10494. S100A4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. neuron projection Source: Ensembl
  4. nucleus Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 101100Protein S100-A4PRO_0000143977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei7 – 71N6-acetyllysine1 Publication
Modified residuei35 – 351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP26447.
PaxDbiP26447.
PeptideAtlasiP26447.
PRIDEiP26447.

2D gel databases

DOSAC-COBS-2DPAGEP26447.
SWISS-2DPAGEP26447.

PTM databases

PhosphoSiteiP26447.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiP26447.
CleanExiHS_S100A4.
GenevestigatoriP26447.

Organism-specific databases

HPAiCAB002618.
CAB027387.
CAB058698.
CAB068227.
CAB068228.
HPA007973.

Interactioni

Subunit structurei

Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AREGBP155144EBI-717058,EBI-953674
BTCP350702EBI-717058,EBI-6590057
MDM2Q009873EBI-717058,EBI-389668
TP53P046377EBI-717058,EBI-366083

Protein-protein interaction databases

BioGridi112183. 23 interactions.
DIPiDIP-44938N.
IntActiP26447. 13 interactions.
MINTiMINT-1372269.
STRINGi9606.ENSP00000346294.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Beta strandi22 – 254Combined sources
Helixi31 – 4111Combined sources
Helixi43 – 453Combined sources
Helixi52 – 6211Combined sources
Beta strandi64 – 663Combined sources
Beta strandi67 – 715Combined sources
Helixi72 – 8615Combined sources
Turni89 – 913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M31NMR-A/B1-101[»]
2LNKNMR-A/B1-101[»]
2Q91X-ray1.63A/B1-101[»]
3C1VX-ray1.50A/B/C/D1-101[»]
3CGAX-ray2.03A/B1-101[»]
3KO0X-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-101[»]
3M0WX-ray2.80A/B/C/D/E/F/G/H/I/J2-101[»]
3ZWHX-ray1.94A/B1-101[»]
4CFQX-ray1.37A/B/C/D1-88[»]
4CFRX-ray1.40A/B1-101[»]
4ETOX-ray1.54A/B1-93[»]
4HSZX-ray2.25A/B/C/D1-93[»]
ProteinModelPortaliP26447.
SMRiP26447. Positions 2-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26447.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini50 – 8536EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG40931.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP26447.
OMAiNEFFEGC.
OrthoDBiEOG7R833W.
PhylomeDBiP26447.
TreeFamiTF332727.

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.
IPR028496. S100-A4.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF15. PTHR11639:SF15. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT
60 70 80 90 100
DEAAFQKLMS NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGFPDKQPRK

K
Length:101
Mass (Da):11,729
Last modified:August 1, 1992 - v1
Checksum:i286D2B7B07EDB562
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80563 mRNA. Translation: AAA51920.1.
Z18950 Genomic DNA. Translation: CAA79474.1.
Z33457 Genomic DNA. Translation: CAA83880.1.
CR450345 mRNA. Translation: CAG29341.1.
AK292083 mRNA. Translation: BAF84772.1.
BX470102 Genomic DNA. Translation: CAI14754.1.
CH471121 Genomic DNA. Translation: EAW53310.1.
CH471121 Genomic DNA. Translation: EAW53311.1.
CH471121 Genomic DNA. Translation: EAW53312.1.
CH471121 Genomic DNA. Translation: EAW53313.1.
CH471121 Genomic DNA. Translation: EAW53314.1.
CH471121 Genomic DNA. Translation: EAW53315.1.
BC000838 mRNA. Translation: AAH00838.1.
BC016300 mRNA. Translation: AAH16300.1.
CCDSiCCDS1042.1.
PIRiA48219.
RefSeqiNP_002952.1. NM_002961.2.
NP_062427.1. NM_019554.2.
UniGeneiHs.654444.

Genome annotation databases

EnsembliENST00000354332; ENSP00000346294; ENSG00000196154.
ENST00000368714; ENSP00000357703; ENSG00000196154.
ENST00000368715; ENSP00000357704; ENSG00000196154.
ENST00000368716; ENSP00000357705; ENSG00000196154.
GeneIDi6275.
KEGGihsa:6275.
UCSCiuc001fby.3. human.

Polymorphism databases

DMDMi115601.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80563 mRNA. Translation: AAA51920.1.
Z18950 Genomic DNA. Translation: CAA79474.1.
Z33457 Genomic DNA. Translation: CAA83880.1.
CR450345 mRNA. Translation: CAG29341.1.
AK292083 mRNA. Translation: BAF84772.1.
BX470102 Genomic DNA. Translation: CAI14754.1.
CH471121 Genomic DNA. Translation: EAW53310.1.
CH471121 Genomic DNA. Translation: EAW53311.1.
CH471121 Genomic DNA. Translation: EAW53312.1.
CH471121 Genomic DNA. Translation: EAW53313.1.
CH471121 Genomic DNA. Translation: EAW53314.1.
CH471121 Genomic DNA. Translation: EAW53315.1.
BC000838 mRNA. Translation: AAH00838.1.
BC016300 mRNA. Translation: AAH16300.1.
CCDSiCCDS1042.1.
PIRiA48219.
RefSeqiNP_002952.1. NM_002961.2.
NP_062427.1. NM_019554.2.
UniGeneiHs.654444.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M31NMR-A/B1-101[»]
2LNKNMR-A/B1-101[»]
2Q91X-ray1.63A/B1-101[»]
3C1VX-ray1.50A/B/C/D1-101[»]
3CGAX-ray2.03A/B1-101[»]
3KO0X-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-101[»]
3M0WX-ray2.80A/B/C/D/E/F/G/H/I/J2-101[»]
3ZWHX-ray1.94A/B1-101[»]
4CFQX-ray1.37A/B/C/D1-88[»]
4CFRX-ray1.40A/B1-101[»]
4ETOX-ray1.54A/B1-93[»]
4HSZX-ray2.25A/B/C/D1-93[»]
ProteinModelPortaliP26447.
SMRiP26447. Positions 2-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112183. 23 interactions.
DIPiDIP-44938N.
IntActiP26447. 13 interactions.
MINTiMINT-1372269.
STRINGi9606.ENSP00000346294.

Chemistry

ChEMBLiCHEMBL2362976.
DrugBankiDB00831. Trifluoperazine.

PTM databases

PhosphoSiteiP26447.

Polymorphism databases

DMDMi115601.

2D gel databases

DOSAC-COBS-2DPAGEP26447.
SWISS-2DPAGEP26447.

Proteomic databases

MaxQBiP26447.
PaxDbiP26447.
PeptideAtlasiP26447.
PRIDEiP26447.

Protocols and materials databases

DNASUi6275.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354332; ENSP00000346294; ENSG00000196154.
ENST00000368714; ENSP00000357703; ENSG00000196154.
ENST00000368715; ENSP00000357704; ENSG00000196154.
ENST00000368716; ENSP00000357705; ENSG00000196154.
GeneIDi6275.
KEGGihsa:6275.
UCSCiuc001fby.3. human.

Organism-specific databases

CTDi6275.
GeneCardsiGC01M153518.
HGNCiHGNC:10494. S100A4.
HPAiCAB002618.
CAB027387.
CAB058698.
CAB068227.
CAB068228.
HPA007973.
MIMi114210. gene.
neXtProtiNX_P26447.
PharmGKBiPA34906.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40931.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP26447.
OMAiNEFFEGC.
OrthoDBiEOG7R833W.
PhylomeDBiP26447.
TreeFamiTF332727.

Miscellaneous databases

ChiTaRSiS100A4. human.
EvolutionaryTraceiP26447.
GeneWikiiS100A4.
GenomeRNAii6275.
NextBioi24355.
PROiP26447.
SOURCEiSearch...

Gene expression databases

BgeeiP26447.
CleanExiHS_S100A4.
GenevestigatoriP26447.

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.
IPR028496. S100-A4.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF15. PTHR11639:SF15. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart."
    Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.
    Biochemistry 31:10258-10264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E."
    Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Transcriptional analysis of the mts1 gene with specific reference to 5' flanking sequences."
    Tulchinsky E.M., Ford H.L., Kramerov D., Reshetnyak E., Grigorian M., Zain S., Lukanidin E.
    Proc. Natl. Acad. Sci. U.S.A. 89:9146-9150(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Spleen.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
    Tissue: Synovium.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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].
    Tissue: Cervix and Prostate.
  9. Cited for: PROTEIN SEQUENCE OF 8-18 AND 36-57.
    Tissue: Platelet.
  10. "Liprin beta 1, a member of the family of LAR transmembrane tyrosine phosphatase-interacting proteins, is a new target for the metastasis-associated protein S100A4 (Mts1)."
    Kriajevska M., Fischer-Larsen M., Moertz E., Vorm O., Tulchinsky E., Grigorian M., Ambartsumian N., Lukanidin E.
    J. Biol. Chem. 277:5229-5235(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPFIBP1.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-7 AND LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy."
    Vallely K.M., Rustandi R.R., Ellis K.C., Varlamova O., Bresnick A.R., Weber D.J.
    Biochemistry 41:12670-12680(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiS10A4_HUMAN
AccessioniPrimary (citable) accession number: P26447
Secondary accession number(s): A8K7R8, D3DV46, Q6ICP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: March 4, 2015
This is version 154 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.