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P55735 (SEC13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein SEC13 homolog
Alternative name(s):
SEC13-like protein 1
SEC13-related protein
Gene names
Name:SEC13
Synonyms:D3S1231E, SEC13L1, SEC13R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway. Ref.9 Ref.17

Subunit structure

At the nuclear pore: component of the Y-shaped Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with SEC31A and SEC31B. Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. Ref.10 Ref.11 Ref.12 Ref.17 Ref.18

Subcellular location

Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleusnuclear pore complex. Note: In interphase, localizes at both sides of the NPC. Ref.9 Ref.10 Ref.18

Sequence similarities

Belongs to the WD repeat SEC13 family.

Contains 6 WD repeats.

Sequence caution

The sequence AAH02634.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processER-Golgi transport
mRNA transport
Protein transport
Translocation
Transport
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
WD repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCOPII vesicle coating

Traceable author statement. Source: Reactome

ER to Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

intracellular protein transport

Non-traceable author statement Ref.1. Source: UniProtKB

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

membrane organization

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: GOC

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nuclear envelope

Inferred from direct assay PubMed 15146057. Source: UniProtKB

nuclear pore outer ring

Inferred from direct assay PubMed 17360435. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15146057. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUP145P496879EBI-1046596,EBI-11730From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55735-1)

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: P55735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P55735-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYRACAGKDEMGKM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 322321Protein SEC13 homolog
PRO_0000051203

Regions

Repeat11 – 5040WD 1
Repeat55 – 9642WD 2
Repeat101 – 14444WD 3
Repeat148 – 20457WD 4
Repeat210 – 25344WD 5
Repeat260 – 29940WD 6

Amino acid modifications

Modified residue21N-acetylvaline Ref.7 Ref.13 Ref.16
Modified residue3091Phosphoserine Ref.14

Natural variations

Alternative sequence1 – 1414Missing in isoform 2.
VSP_046191
Alternative sequence11M → MREPVLTWCVPLELLCSHPL PLSAFLKSQVKLYTYRACAG KDEMGKM in isoform 3.
VSP_054695
Natural variant1721S → L.
Corresponds to variant rs34078590 [ dbSNP | Ensembl ].
VAR_053413

Experimental info

Sequence conflict511A → V in L09260. Ref.1

Secondary structure

................................................................. 322
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 18E29627D87FB3DD

FASTA32235,541
        10         20         30         40         50         60 
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV 

        70         80         90        100        110        120 
WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA GHDSSVNSVC WAPHDYGLIL 

       130        140        150        160        170        180 
ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK 

       190        200        210        220        230        240 
RFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV 

       250        260        270        280        290        300 
FIWTCDDASS NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI 

       310        320 
SDVNKGQGSV SASVTEGQQN EQ 

« Hide

Isoform 2 [UniParc].

Checksum: F4D5BC3F757FE7BB
Show »

FASTA30834,012
Isoform 3 [UniParc].

Checksum: E738D9D307CF2308
Show »

FASTA36840,747

References

« Hide 'large scale' references
[1]"Molecular characterization of a novel human gene, SEC13R, related to the yeast secretory pathway gene SEC13, and mapping to a conserved linkage group on human chromosome 3p24-p25 and mouse chromosome 6."
Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C., Agarwal N., Meisler M.H., Smith D.I.
Hum. Mol. Genet. 3:1281-1286(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[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] (ISOFORM 3).
Tissue: Testis.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1).
Tissue: Placenta and Uterus.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-27.
Tissue: Platelet.
[7]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[9]"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex."
Enninga J., Levay A., Fontoura B.M.
Mol. Cell. Biol. 23:7271-7284(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUP96.
[11]"Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat."
Stankewich M.C., Stabach P.R., Morrow J.S.
J. Cell Sci. 119:958-969(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC31B.
[12]"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC31A.
[13]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1."
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.
Science 340:1100-1106(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN GATOR COMPLEX, INTERACTION WITH RRAG PROTEINS.
[18]"Architecture of a coat for the nuclear pore membrane."
Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.
Cell 131:1313-1326(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST NUP145C, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09260 mRNA. No translation available.
AF052155 mRNA. No translation available.
AK301999 mRNA. Translation: BAG63403.1.
AC022384 Genomic DNA. No translation available.
BC002634 mRNA. Translation: AAH02634.2. Different initiation.
BC006167 mRNA. Translation: AAH06167.1.
BC091506 mRNA. Translation: AAH91506.1.
CCDSCCDS2599.1. [P55735-1]
CCDS46751.1. [P55735-2]
RefSeqNP_001129498.1. NM_001136026.2. [P55735-3]
NP_001129704.1. NM_001136232.2. [P55735-2]
NP_109598.2. NM_030673.3.
NP_899195.1. NM_183352.2. [P55735-1]
XP_005265436.1. XM_005265379.1.
XP_006713349.1. XM_006713286.1. [P55735-3]
XP_006713351.1. XM_006713288.1. [P55735-2]
UniGeneHs.166924.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BG0X-ray3.15A/D/E/H1-316[»]
3BG1X-ray3.00A/D/E/H1-316[»]
ProteinModelPortalP55735.
SMRP55735. Positions 14-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112296. 32 interactions.
DIPDIP-39091N.
IntActP55735. 17 interactions.
MINTMINT-1154053.
STRING9606.ENSP00000312122.

PTM databases

PhosphoSiteP55735.

Polymorphism databases

DMDM50403748.

Proteomic databases

MaxQBP55735.
PaxDbP55735.
PRIDEP55735.

Protocols and materials databases

DNASU6396.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337354; ENSP00000336566; ENSG00000157020.
ENST00000350697; ENSP00000312122; ENSG00000157020. [P55735-1]
ENST00000383801; ENSP00000373312; ENSG00000157020.
ENST00000397109; ENSP00000380298; ENSG00000157020. [P55735-2]
GeneID6396.
KEGGhsa:6396.
UCSCuc003bvl.3. human. [P55735-1]

Organism-specific databases

CTD6396.
GeneCardsGC03M010337.
HGNCHGNC:10697. SEC13.
HPAHPA035292.
MIM600152. gene.
neXtProtNX_P55735.
PharmGKBPA35620.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000216895.
HOVERGENHBG057343.
InParanoidP55735.
KOK14004.
OrthoDBEOG7966GP.
PhylomeDBP55735.
TreeFamTF300815.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.
SignaLinkP55735.

Gene expression databases

ArrayExpressP55735.
BgeeP55735.
CleanExHS_SEC13.
GenevestigatorP55735.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 6 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP55735.
GeneWikiSEC13.
GenomeRNAi6396.
NextBio24846.
PROP55735.
SOURCESearch...

Entry information

Entry nameSEC13_HUMAN
AccessionPrimary (citable) accession number: P55735
Secondary accession number(s): A8MV37 expand/collapse secondary AC list , B4DXJ1, Q5BJF0, Q9BRM6, Q9BUG7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 138 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM