Reviewed, UniProtKB/Swiss-Prot Q9BRK5 (CAB45_HUMAN)

Names and origin

Protein names

Recommended name:
    45 kDa calcium-binding protein
Alternative name(s):
    Cab45
    Stromal cell-derived factor 4
      Short name=SDF-4

Gene names

Name:	SDF4
Synonyms:	CAB45
ORF Names:	PSEC0034

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. Isoform 5 may be involved in the exocytosis of zymogens by pancreatic acini By similarity.
Cofactor	Binds calcium By similarity. Isoform 5 binds calcium.
Subunit structure	Isoform 5 interacts with STXBP1; the interaction is enhanced in presence of calcium. Isoform 5 interacts with STX3.
Subcellular location	Isoform 1: Golgi apparatus lumen By similarity. Isoform 5: Cytoplasm. Note: Isoform 5 colocalizes with STX3 and STXBP1 isoform 2 at the plasma membrane and cell surface blebs.
Tissue specificity	Ubiquitous. Isoform 5 is expressed in pancreas.
Sequence similarities	Belongs to the CREC family. Contains 6 EF-hand domains.
Sequence caution	The sequence AAF44350.1 differs from that shown. Reason: Frameshift at position 305.

Ontologies

Keywords
Biological process	Exocytosis
Cellular component	Cytoplasm Golgi apparatus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Ligand	Calcium
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	UV protection Inferred from sequence or structural similarity. Source: UniProtKB cerebellum development Inferred from sequence or structural similarity. Source: UniProtKB fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB response to ethanol Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi lumen Inferred from sequence or structural similarity. Source: UniProtKB late endosome Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 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.

Note: Isoform 5 colocalizes with STX3 and STXBP1 isoform 2 at the plasma membrane and cell surface blebs.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Potential
	Chain	37 – 362	326	45 kDa calcium-binding protein		PRO_0000004156
Regions
	Domain	98 – 133	36	EF-hand 1
	Domain	137 – 172	36	EF-hand 2
	Domain	197 – 232	36	EF-hand 3
	Domain	233 – 268	36	EF-hand 4
	Domain	278 – 313	36	EF-hand 5
	Domain	314 – 349	36	EF-hand 6
	Calcium binding	111 – 122	12	1 Potential
	Calcium binding	150 – 161	12	2 Potential
	Calcium binding	209 – 220	12	3 Potential
	Calcium binding	246 – 257	12	4 Potential
	Calcium binding	291 – 302	12	5 Potential
	Calcium binding	327 – 338	12	6 Potential
	Region	309 – 362	54	Necessary for intracellular retention in Golgi apparatus lumen By similarity
Amino acid modifications
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 232	232	Missing in isoform 5.		VSP_037484
	Alternative sequence	1 – 103	103	Missing in isoform 2.		VSP_037485
	Alternative sequence	193 – 254	62	TQEVL…DKQLS → SCAPLSTGSPGEPEGPLVPG GQPPCRPAADGGGVPVGPPP RAQPGNAQVHGEGDRPGPGP GR in isoform 3.		VSP_037486
	Alternative sequence	193 – 202	10	TQEVLENLKD → RHGPPGPRAL in isoform 4.		VSP_037487
	Alternative sequence	203 – 362	160	Missing in isoform 4.		VSP_037488
	Alternative sequence	255 – 362	108	Missing in isoform 3.		VSP_037489
	Natural variant	50	1	N → D: dbSNP rs12745364.		VAR_048659
	Natural variant	148	1	A → T in a colorectal cancer sample; somatic mutation. Ref.13		VAR_035461
Experimental info
	Mutagenesis	257	1	E → Q: Does not affect calcium-binding.
	Mutagenesis	302	1	E → Q: Inhibits calcium-binding.
	Mutagenesis	338	1	E → Q: Does not affect calcium-binding.
	Sequence conflict	70 – 78	9	DGHLNRGFH → ERALKSGFQ in AAL75950. Ref.2
	Sequence conflict	86 – 97	12	DLGGF…DAEPR → NLVALIGNGAP in AAL75950. Ref.2
	Sequence conflict	117	1	K → R in BAC11563. Ref.5
	Sequence conflict	133	1	E → G in BAC11563. Ref.5
	Sequence conflict	150	1	D → G in AAL75950. Ref.2
	Sequence conflict	188	1	K → R in BAG37898. Ref.6
	Sequence conflict	193	1	T → A in BAD96241. Ref.7
	Sequence conflict	234	1	L → P in BAD96799. Ref.7
	Sequence conflict	281 – 282	2	DR → KK in AAL75950. Ref.2
	Sequence conflict	286	1	F → L in AAL75950. Ref.2
	Sequence conflict	321	1	Q → R in BAD96799. Ref.7
	Sequence conflict	322 – 325	4	MIAV → IRL in AAL75950. Ref.2
	Sequence conflict	356	1	R → S in AAL75950. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Cab45a) (Cab45-G) [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 440C6990149AAE2C	FASTA	362	41,807
	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
	Isoform 2. Checksum: 3745A23BB8FF6D40	FASTA	259	30,197
	10 20 30 40 50 60 MVIFSKVDVN TDRKISAKEM QRWIMEKTAE HFQEAMEESK THFRAVDPDG DGHVSWDEYK 70 80 90 100 110 120 VKFLASKGHS EKEVADAIRL NEELKVDEET QEVLENLKDR WYQADSPPAD LLLTEEEFLS 130 140 150 160 170 180 FLHPEHSRGM LRFMVKEIVR DLDQDGDKQL SVPEFISLPV GTVENQQGQD IDDNWVKDRK 190 200 210 220 230 240 KEFEELIDSN HDGIVTAEEL ESYMDPMNEY NALNEAKQMI AVADENQNHH LEPEEVLKYS 250 EFFTGSKLVD YARSVHEEF
	Isoform 3. Checksum: 77FACCE59B472125	FASTA	254	27,826
	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 EESCAPLSTG SPGEPEGPLV PGGQPPCRPA ADGGGVPVGP PPRAQPGNAQ 250 VHGEGDRPGP GPGR
	Isoform 4. Checksum: 5F208F14504756F7	FASTA	202	23,031
	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 IRLNEELKVD EERHGPPGPR AL
	Isoform 5 (Cab45b) (Cab45-C). Checksum: 22545D121BB56827	FASTA	130	15,139
	10 20 30 40 50 60 MLRFMVKEIV RDLDQDGDKQ LSVPEFISLP VGTVENQQGQ DIDDNWVKDR KKEFEELIDS 70 80 90 100 110 120 NHDGIVTAEE LESYMDPMNE YNALNEAKQM IAVADENQNH HLEPEEVLKY SEFFTGSKLV 130 DYARSVHEEF

References

	« Hide 'large scale' referencesShow '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: 9254016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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]	"HRI human cDNA sequencing project." Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Teratocarcinoma.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). Tissue: Brain and Tongue.
[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. , 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: 16710414] [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. , 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: 15489334] [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: 17442889] [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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-148.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L79912 mRNA. Translation: AAL40084.1. AF132749 mRNA. Translation: AAL75950.1. AF153686 mRNA. Translation: AAD51612.1. AF178986 mRNA. Translation: AAF44350.1. Frameshift. AK075352 mRNA. Translation: BAC11563.1. AK027277 mRNA. Translation: BAB55012.1. AK299810 mRNA. Translation: BAG61683.1. AK315517 mRNA. Translation: BAG37898.1. AK222521 mRNA. Translation: BAD96241.1. AK223079 mRNA. Translation: BAD96799.1. AL162741 Genomic DNA. Translation: CAI23251.1. 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.
IPI	IPI00009794. IPI00106646. IPI00384644.
RefSeq	NP_057260.2. NP_057631.1.
UniGene	Hs.42806
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q9BRK5.
Proteomic databases
PRIDE	Q9BRK5.
Genome annotation databases
Ensembl	ENSG00000078808. Homo sapiens. [Contig view]
GeneID	51150.
KEGG	hsa:51150.
Organism-specific databases
GeneCards	GC01M001143.
HGNC	HGNC:24188. SDF4.
HPA	CAB015227.
PharmGKB	PA142670940.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9BRK5.
HOVERGEN	Q9BRK5.
OMA	Q9BRK5. HDGIVTM.
Gene expression databases
ArrayExpress	Q9BRK5.
Bgee	Q9BRK5.
CleanEx	HS_SDF4.
GermOnline	ENSG00000078808. Homo sapiens.
Family and domain databases
InterPro	IPR011992. EF-Hand_type. IPR018247. EF_HAND_1. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 2 hits.
ProDom	PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00054. EFh. 5 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 5 hits. PS50222. EF_HAND_2. 5 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	54034.

Entry information

Entry name

CAB45_HUMAN

Accession

Primary (citable) accession number: Q9BRK5
Secondary accession number(s): B1AME5 , 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:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)