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Q9BRK5 (CAB45_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
45 kDa calcium-binding protein

Short name=Cab45
Alternative name(s):
Stromal cell-derived factor 4
Short name=SDF-4
Gene names
Name:SDF4
Synonyms:CAB45
ORF Names:PSEC0034
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment By similarity.

Isoform 5 may be involved in the exocytosis of zymogens by pancreatic acini.

Subunit structure

Isoform 5 interacts with STXBP1; the interaction is enhanced in presence of calcium. Isoform 5 interacts with STX3. Ref.11

Subcellular location

Isoform 1: Golgi apparatus lumen By similarity Ref.11.

Isoform 5: Cytoplasm. Cell projectionbleb. Note: Isoform 5 colocalizes with STX3 and STXBP1 isoform 2 at the plasma membrane and cell surface blebs. Ref.11

Tissue specificity

Ubiquitous. Isoform 5 is expressed in pancreas. Ref.11

Domain

Binds calcium via its EF-hands By similarity. Isoform 5 binds calcium.

Sequence similarities

Belongs to the CREC family.

Contains 6 EF-hand domains.

Sequence caution

The sequence AAL75950.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BRK5-1)

Also known as: Cab45a; Cab45-G;

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: Q9BRK5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.
Isoform 3 (identifier: Q9BRK5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     193-254: TQEVLENLKD...LDQDGDKQLS → SCAPLSTGSP...GDRPGPGPGR
     255-362: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BRK5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     193-202: TQEVLENLKD → RHGPPGPRAL
     203-362: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9BRK5-5)

Also known as: Cab45b; Cab45-C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
Isoform 6 (identifier: Q9BRK5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     305-362: SYMDPMNEYN...DYARSVHEEF → NVPTLPLQPI...PLARRATWTP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 36232645 kDa calcium-binding protein
PRO_0000004156

Regions

Domain98 – 13336EF-hand 1
Domain137 – 17236EF-hand 2
Domain197 – 23236EF-hand 3
Domain233 – 26836EF-hand 4
Domain278 – 31336EF-hand 5
Domain314 – 34936EF-hand 6
Calcium binding111 – 122121 Potential
Calcium binding150 – 161122 Potential
Calcium binding209 – 220123 Potential
Calcium binding246 – 257124 Potential
Calcium binding291 – 302125 Potential
Calcium binding327 – 338126 Potential
Region309 – 36254Necessary for intracellular retention in Golgi apparatus lumen By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 232232Missing in isoform 5.
VSP_037484
Alternative sequence1 – 103103Missing in isoform 2.
VSP_037485
Alternative sequence193 – 25462TQEVL…DKQLS → SCAPLSTGSPGEPEGPLVPG GQPPCRPAADGGGVPVGPPP RAQPGNAQVHGEGDRPGPGP GR in isoform 3.
VSP_037486
Alternative sequence193 – 20210TQEVLENLKD → RHGPPGPRAL in isoform 4.
VSP_037487
Alternative sequence203 – 362160Missing in isoform 4.
VSP_037488
Alternative sequence255 – 362108Missing in isoform 3.
VSP_037489
Alternative sequence305 – 36258SYMDP…VHEEF → NVPTLPLQPIGTLNSHFVRL AAELGGGKATLTCAPLARRA TWTP in isoform 6.
VSP_040559
Natural variant501N → D.
Corresponds to variant rs12745364 [ dbSNP | Ensembl ].
VAR_048659
Natural variant1481A → T in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035461

Experimental info

Mutagenesis2571E → Q: Does not affect calcium-binding. Ref.11
Mutagenesis3021E → Q: Inhibits calcium-binding. Ref.11
Mutagenesis3381E → Q: Does not affect calcium-binding. Ref.11
Sequence conflict781H → Q in AAL75950. Ref.2
Sequence conflict861D → N in AAL75950. Ref.2
Sequence conflict891G → C in AAL75950. Ref.2
Sequence conflict921E → R in AAL75950. Ref.2
Sequence conflict941A → T in AAL75950. Ref.2
Sequence conflict971R → P in AAL75950. Ref.2
Sequence conflict1171K → R in BAC11563. Ref.6
Sequence conflict1331E → G in BAC11563. Ref.6
Sequence conflict1501D → G in AAL75950. Ref.2
Sequence conflict1881K → R in BAG37898. Ref.5
Sequence conflict1931T → A in BAD96241. Ref.7
Sequence conflict2341L → P in BAD96799. Ref.7
Sequence conflict281 – 2822DR → KK in AAL75950. Ref.2
Sequence conflict2861F → L in AAL75950. Ref.2
Sequence conflict3211Q → R in BAD96799. Ref.7
Sequence conflict3561R → S in AAL75950. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Cab45a) (Cab45-G) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 440C6990149AAE2C

FASTA36241,807
        10         20         30         40         50         60 
MVWPWVAMAS RWGPLIGLAP CCLWLLGAVL LMDASARPAN HSSTRERVAN REENEILPPD 

        70         80         90        100        110        120 
HLNGVKLEMD GHLNRGFHQE VFLGKDLGGF DEDAEPRRSR RKLMVIFSKV DVNTDRKISA 

       130        140        150        160        170        180 
KEMQRWIMEK TAEHFQEAME ESKTHFRAVD PDGDGHVSWD EYKVKFLASK GHSEKEVADA 

       190        200        210        220        230        240 
IRLNEELKVD EETQEVLENL KDRWYQADSP PADLLLTEEE FLSFLHPEHS RGMLRFMVKE 

       250        260        270        280        290        300 
IVRDLDQDGD KQLSVPEFIS LPVGTVENQQ GQDIDDNWVK DRKKEFEELI DSNHDGIVTA 

       310        320        330        340        350        360 
EELESYMDPM NEYNALNEAK QMIAVADENQ NHHLEPEEVL KYSEFFTGSK LVDYARSVHE 


EF 

« Hide

Isoform 2 [UniParc].

Checksum: 3745A23BB8FF6D40
Show »

FASTA25930,197
Isoform 3 [UniParc].

Checksum: 77FACCE59B472125
Show »

FASTA25427,826
Isoform 4 [UniParc].

Checksum: 5F208F14504756F7
Show »

FASTA20223,031
Isoform 5 (Cab45b) (Cab45-C) [UniParc].

Checksum: 22545D121BB56827
Show »

FASTA13015,139
Isoform 6 [UniParc].

Checksum: 1832BC4741A9506A
Show »

FASTA34839,608

References

« Hide 'large scale' references
[1]"Sequence of a human cDNA encoding Cab45, a Ca2+-binding protein with six EF-hand motifs."
Koivu T., Laitinen S., Riento K., Olkkonen V.M.
DNA Seq. 7:217-220(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
[2]"Cloning of a new human cDNA homologous to Mus musculus calcium-binding protein Cab45b."
Yue P., Yu L., Zhao S.Y.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Novel human calcium-binding protein precursor."
Zhang W., Wan T., Yuan Z., Cao X.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"Identification of a novel calcium-binding protein Cab45 from dendritic cells."
Zhang W., Wan T., Cao X.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. 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] (ISOFORMS 1; 2 AND 4).
Tissue: Brain and Tongue.
[6]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[7]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adipose tissue.
[8]"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. expand/collapse author list , 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].
[9]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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, Pancreas and Prostate.
[11]"A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on amylase secretion by pancreatic acini."
Lam P.P., Hyvaerinen K., Kauppi M., Cosen-Binker L., Laitinen S., Keraenen S., Gaisano H.Y., Olkkonen V.M.
Mol. Biol. Cell 18:2473-2480(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STX3 AND STXBP1, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 5), MUTAGENESIS OF GLU-257; GLU-302 AND GLU-338, TISSUE SPECIFICITY.
[12]"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].
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-148.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L79912 mRNA. Translation: AAL40084.1.
AF132749 mRNA. Translation: AAL75950.1. Frameshift.
AF153686 mRNA. Translation: AAD51612.1.
AF178986 mRNA. Translation: AAF44350.1.
AK027277 mRNA. Translation: BAB55012.1.
AK299810 mRNA. Translation: BAG61683.1.
AK315517 mRNA. Translation: BAG37898.1.
AK075352 mRNA. Translation: BAC11563.1.
AK222521 mRNA. Translation: BAD96241.1.
AK223079 mRNA. Translation: BAD96799.1.
AL162741 Genomic DNA. Translation: CAI23251.1.
AL162741 Genomic DNA. Translation: CAI23252.1.
CH471183 Genomic DNA. Translation: EAW56272.1.
CH471183 Genomic DNA. Translation: EAW56273.1.
BC006211 mRNA. Translation: AAH06211.1.
BC007625 mRNA. Translation: AAH07625.1.
BC008917 mRNA. Translation: AAH08917.1.
BC011244 mRNA. Translation: AAH11244.1.
BC022375 mRNA. Translation: AAH22375.1.
RefSeqNP_057260.2. NM_016176.3.
NP_057631.1. NM_016547.2.
XP_005244813.1. XM_005244756.1.
UniGeneHs.42806.

3D structure databases

ProteinModelPortalQ9BRK5.
SMRQ9BRK5. Positions 100-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119334. 21 interactions.
IntActQ9BRK5. 20 interactions.
MINTMINT-1186958.

PTM databases

PhosphoSiteQ9BRK5.

Polymorphism databases

DMDM21263447.

Proteomic databases

PaxDbQ9BRK5.
PRIDEQ9BRK5.

Protocols and materials databases

DNASU51150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263741; ENSP00000263741; ENSG00000078808. [Q9BRK5-6]
ENST00000360001; ENSP00000353094; ENSG00000078808. [Q9BRK5-1]
ENST00000545427; ENSP00000444451; ENSG00000078808. [Q9BRK5-4]
GeneID51150.
KEGGhsa:51150.
UCSCuc001adh.4. human. [Q9BRK5-1]
uc001adi.4. human. [Q9BRK5-6]

Organism-specific databases

CTD51150.
GeneCardsGC01M001143.
HGNCHGNC:24188. SDF4.
HPACAB015227.
HPA011249.
MIM614282. gene.
neXtProtNX_Q9BRK5.
PharmGKBPA142670940.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277464.
HOVERGENHBG097344.
InParanoidQ9BRK5.
OMAFMVKEII.
OrthoDBEOG7M0NSC.
TreeFamTF314849.

Gene expression databases

ArrayExpressQ9BRK5.
BgeeQ9BRK5.
CleanExHS_SDF4.
GenevestigatorQ9BRK5.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR027240. CAB45.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERPTHR10827:SF1. PTHR10827:SF1. 1 hit.
PfamPF13202. EF-hand_5. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 5 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 5 hits.
PS50222. EF_HAND_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDF4. human.
GeneWikiSDF4.
GenomeRNAi51150.
NextBio54034.
PROQ9BRK5.
SOURCESearch...

Entry information

Entry nameCAB45_HUMAN
AccessionPrimary (citable) accession number: Q9BRK5
Secondary accession number(s): B1AME5 expand/collapse secondary AC list , B1AME6, B2RDF1, B4DSM1, Q53G52, Q53HQ9, Q8NBQ3, Q96AA1, Q9NZP7, Q9UN53
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 125 of the entry and version 1 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 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 1

Human chromosome 1: entries, gene names and cross-references to MIM