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Protein

Vesicle-trafficking protein SEC22b

Gene

SEC22B

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

Functioni

SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-trafficking protein SEC22b
Alternative name(s):
ER-Golgi SNARE of 24 kDa
Short name:
ERS-24
Short name:
ERS24
SEC22 vesicle-trafficking protein homolog B
SEC22 vesicle-trafficking protein-like 1
Gene namesi
Name:SEC22B
Synonyms:SEC22L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10700. SEC22B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 194193CytoplasmicSequence analysisAdd
BLAST
Transmembranei195 – 21521Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 215214Vesicle-trafficking protein SEC22bPRO_0000206770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-acetyllysineCombined sources
Modified residuei137 – 1371PhosphoserineCombined sources
Modified residuei140 – 1401PhosphothreonineCombined sources
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75396.
MaxQBiO75396.
PeptideAtlasiO75396.
PRIDEiO75396.
TopDownProteomicsiO75396.

PTM databases

iPTMnetiO75396.
PhosphoSiteiO75396.
SwissPalmiO75396.

Expressioni

Gene expression databases

CleanExiHS_SEC22B.
ExpressionAtlasiO75396. baseline and differential.
GenevisibleiO75396. HS.

Interactioni

Subunit structurei

Interacts with STX17 (By similarity). Component of two distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B in either complex.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
STX18Q9P2W92EBI-1058865,EBI-725334

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114926. 89 interactions.
DIPiDIP-50458N.
IntActiO75396. 31 interactions.
MINTiMINT-5000824.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Turni10 – 123Combined sources
Beta strandi15 – 195Combined sources
Helixi30 – 4314Combined sources
Beta strandi50 – 567Combined sources
Beta strandi59 – 668Combined sources
Beta strandi69 – 768Combined sources
Helixi81 – 9919Combined sources
Turni100 – 1056Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1153Combined sources
Helixi116 – 1238Combined sources
Turni124 – 1263Combined sources
Turni129 – 1313Combined sources
Beta strandi150 – 1523Combined sources
Helixi153 – 1564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NUPX-ray2.80C1-195[»]
2NUTX-ray2.30C1-195[»]
3EGDX-ray2.70C1-157[»]
3EGXX-ray3.30C1-157[»]
ProteinModelPortaliO75396.
SMRiO75396. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 119114LonginPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 19461v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 longin domain.PROSITE-ProRule annotation
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052748.
InParanoidiO75396.
KOiK08517.
PhylomeDBiO75396.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT
60 70 80 90 100
RCTLEAGAMT FHYIIEQGVC DLVLCEAAFP KTLAFAYLED LHSEFDEQHG
110 120 130 140 150
KKVPTVSRPY SFIEFDTFIQ KTKKLYIDSC ARRNLGSINT ELQDVQRIMV
160 170 180 190 200
ANIEEVLQRG EALSALDSKA NNLSSLSKKY RQDAKYLNMH STYAKLAAVA
210
VFFIMLIVYV RFWWL
Length:215
Mass (Da):24,593
Last modified:January 11, 2011 - v4
Checksum:i9FA59C20F2D3F690
GO

Sequence cautioni

The sequence AL359758 differs from that shown. Reason: Erroneous termination at position 39. Translated as Gln.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711D → Y.3 Publications
Corresponds to variant rs2596331 [ dbSNP | Ensembl ].
VAR_060311
Natural varianti82 – 821T → K.3 Publications
Corresponds to variant rs2794053 [ dbSNP | Ensembl ].
VAR_060312
Natural varianti108 – 1081R → Q.
Corresponds to variant rs2655551 [ dbSNP | Ensembl ].
VAR_057343
Natural varianti130 – 1301C → R.Combined sources3 Publications
Corresponds to variant rs2590131 [ dbSNP | Ensembl ].
VAR_060313
Natural varianti190 – 1901H → R.3 Publications
Corresponds to variant rs2655557 [ dbSNP | Ensembl ].
VAR_060314
Natural varianti214 – 2141W → C.
Corresponds to variant rs7534444 [ dbSNP | Ensembl ].
VAR_057344

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047442 mRNA. Translation: AAC39893.1.
AK289875 mRNA. Translation: BAF82564.1.
AL359758 Genomic DNA. No translation available.
BX537145 Genomic DNA. No translation available.
BC001364 mRNA. Translation: AAH01364.1.
RefSeqiNP_004883.3. NM_004892.5.
UniGeneiHs.632438.

Genome annotation databases

EnsembliENST00000578049; ENSP00000463393; ENSG00000265808.
GeneIDi9554.
KEGGihsa:9554.
UCSCiuc031unv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047442 mRNA. Translation: AAC39893.1.
AK289875 mRNA. Translation: BAF82564.1.
AL359758 Genomic DNA. No translation available.
BX537145 Genomic DNA. No translation available.
BC001364 mRNA. Translation: AAH01364.1.
RefSeqiNP_004883.3. NM_004892.5.
UniGeneiHs.632438.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NUPX-ray2.80C1-195[»]
2NUTX-ray2.30C1-195[»]
3EGDX-ray2.70C1-157[»]
3EGXX-ray3.30C1-157[»]
ProteinModelPortaliO75396.
SMRiO75396. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114926. 89 interactions.
DIPiDIP-50458N.
IntActiO75396. 31 interactions.
MINTiMINT-5000824.

PTM databases

iPTMnetiO75396.
PhosphoSiteiO75396.
SwissPalmiO75396.

Proteomic databases

EPDiO75396.
MaxQBiO75396.
PeptideAtlasiO75396.
PRIDEiO75396.
TopDownProteomicsiO75396.

Protocols and materials databases

DNASUi9554.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000578049; ENSP00000463393; ENSG00000265808.
GeneIDi9554.
KEGGihsa:9554.
UCSCiuc031unv.2. human.

Organism-specific databases

CTDi9554.
GeneCardsiSEC22B.
HGNCiHGNC:10700. SEC22B.
MIMi604029. gene.
neXtProtiNX_O75396.
PharmGKBiPA35623.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG052748.
InParanoidiO75396.
KOiK08517.
PhylomeDBiO75396.

Enzyme and pathway databases

ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.

Miscellaneous databases

EvolutionaryTraceiO75396.
GeneWikiiSEC22B.
GenomeRNAii9554.
NextBioi35831.
PROiO75396.
SOURCEiSearch...

Gene expression databases

CleanExiHS_SEC22B.
ExpressionAtlasiO75396. baseline and differential.
GenevisibleiO75396. HS.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS TYR-71; LYS-82; ARG-130 AND ARG-190.
    Tissue: Umbilical cord blood.
  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.
    , 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], VARIANTS TYR-71; LYS-82; ARG-130 AND ARG-190.
    Tissue: Caudate nucleus.
  3. "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].
  4. "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], VARIANTS TYR-71; LYS-82; ARG-130 AND ARG-190.
    Tissue: Skin.
  5. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  6. "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion."
    Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K., Nagahama M., Tani K., Yamamoto A., Tagaya M.
    EMBO J. 23:3216-3226(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BNIP1; STX18 AND USE1L.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 LYS-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-137; THR-140 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSC22B_HUMAN
AccessioniPrimary (citable) accession number: O75396
Secondary accession number(s): A8K1G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 11, 2011
Last modified: May 11, 2016
This is version 148 of the entry and version 4 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

Caution

The reference genome displays a polymorphic premature stop codon in position 39.Curated

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. 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.