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Q9Z2R9 (E2AK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 2-alpha kinase 1

EC=2.7.11.1
Alternative name(s):
Heme-controlled repressor
Short name=HCR
Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase
Heme-regulated inhibitor
Hemin-sensitive initiation factor 2-alpha kinase
Gene names
Name:Eif2ak1
Synonyms:Hri
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions. Ref.2 Ref.10 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Induced by acute heme depletion, that not only increases EIF2AK1 protein levels, but also stimulates kinase activity by autophosphorylation. Inhibited by the heme-degradation products biliverdin and bilirubin. Induced by oxidative stress generated by arsenite treatment. Binding of nitric oxide (NO) to the heme iron in the N-terminal heme-binding domain activates the kinase activity, while binding of carbon monoxide (CO) suppresses kinase activity. Ref.8 Ref.9 Ref.12

Subunit structure

Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation By similarity. Forms oligomers. Has been reported as a homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin. Ref.10

Subcellular location

Cytoplasm Ref.11.

Tissue specificity

Expressed predominantly in erythroid cells, mature reticulocytes, as well as fetal liver nucleated erythroid cells. At much lower levels, expressed in hepatocytes and bone marrow-derived macrophages (at protein level). Ref.7 Ref.11 Ref.12

Developmental stage

Highly expressed in fetal liver erythroid precursor cells at 14.5 dpc (at protein level). Ref.11

Induction

By phenobarbital. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Post-translational modification

Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-485 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations. Ref.1 Ref.6 Ref.8

Involvement in disease

Defects in Eif2ak1 are a cause of hyperchromic anemia in animals suffering from iron deficiency. The number of red blood cells is decreased due to increased apoptosis of erythroid precursor cells, probably because globins misfold and aggregate in the absence of heme.

Disruption phenotype

Mice are viable and fertile without gross morphological abnormalities. Dramatically altered response to diet-induced iron deficiency shifting from an adaptive decrease in RBC volume and intracellular hemoglobin content to an increased production of abnormally dense red blood cells (RBCs) with decreasing red cell counts. The decrease in RBC number is the result of increased apoptosis of erythroid precursors. Diminished levels of phosphorylated EIF2S1 in bone marrow-derived macrophages (BMDMs). Impaired maturation of BMDMs and blunted inflammatory response to LPS with a reduced cytokine production. Impaired phagocytosis of senescent RBCs by macrophages, resulting in a lower phagocytosis index and lower percentage of macrophages with ingested RBC. In hepatocytes, cytochromes P450 CYP2B6 and CYP3A induction by phenobarbital is not impaired in response to acute heme depletion and CYP2B6 and CYP3A proteins continue to accumulate to supranormal levels, irrespective of the hepatic heme pool status. These cells also exhibit a weak, albeit significant, elevation of the basal ER-stress as reflected by elevated levels of autophosphorylated EIF2AK3/PERK and EIF2AK4/GCN2, the ER-stress related chaperones HSPA5 and HSP90B1, and total hepatic protein ubiquitination. Ref.2 Ref.11 Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.

Contains 2 HRM (heme regulatory motif) repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAD32438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Protein synthesis inhibitor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cell proliferation

Inferred from direct assay PubMed 11050009. Source: UniProtKB

negative regulation of hemoglobin biosynthetic process

Inferred from direct assay PubMed 11050009. Source: UniProtKB

negative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

protein autophosphorylation

Inferred from expression pattern Ref.6. Source: UniProtKB

protoporphyrinogen IX metabolic process

Inferred from genetic interaction PubMed 15931390. Source: MGI

regulation of eIF2 alpha phosphorylation by heme

Inferred from genetic interaction PubMed 15931390. Source: MGI

regulation of hemoglobin biosynthetic process

Inferred from genetic interaction PubMed 15931390. Source: MGI

regulation of translation

Inferred from mutant phenotype Ref.2. Source: MGI

response to external stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11050009. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

eukaryotic translation initiation factor 2alpha kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

heme binding

Inferred from direct assay PubMed 10671563. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21223507. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.6. Source: UniProtKB

protein kinase activity

Inferred from mutant phenotype Ref.2. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Eif2s1Q6ZWX66EBI-642878,EBI-1202234

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Eukaryotic translation initiation factor 2-alpha kinase 1
PRO_0000085942

Regions

Domain167 – 580414Protein kinase
Repeat408 – 4136HRM 1
Repeat549 – 5546HRM 2
Nucleotide binding173 – 1819ATP By similarity

Sites

Active site4401Proton acceptor By similarity
Binding site1961ATP By similarity
Site801Heme-binding By similarity

Amino acid modifications

Modified residue4831Phosphothreonine; by autocatalysis Ref.8
Modified residue4851Phosphothreonine; by autocatalysis Ref.8
Modified residue4901Phosphothreonine; by autocatalysis Ref.8

Experimental info

Mutagenesis1961K → R: Abolishes kinase activity. Ref.1 Ref.8
Mutagenesis4831T → A: No effect on kinase activity. Ref.8
Mutagenesis4831T → D: No effect on kinase activity. Ref.8
Mutagenesis4851T → A: Abolishes kinase activity. Ref.8
Mutagenesis4851T → D: Constitutively active kinase; loss of regulation by heme and arsenite. Ref.8
Mutagenesis4901T → A: Almost complete loss of kinase activity; even upon arsenite treatment. Ref.8
Mutagenesis4901T → D: Almost complete loss of kinase activity; even upon arsenite treatment. Ref.8
Sequence conflict201A → S in BAB32242. Ref.5
Sequence conflict711S → C in BAB32242. Ref.5
Sequence conflict138 – 15013DPCQD…MQKIR → VSPTGCTLYDKYI in BAB32242. Ref.5
Sequence conflict196 – 1972KK → IE in BAB29545. Ref.5
Sequence conflict3711E → D in AAC79201. Ref.1
Sequence conflict3711E → D in AAK55766. Ref.2
Sequence conflict5651V → A in AAH28923. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9Z2R9 [UniParc].

Last modified April 5, 2011. Version 2.
Checksum: 39DC5FF950C92F2A

FASTA61969,702
        10         20         30         40         50         60 
MLGGSSVDGE RDTDDDAAGA VAAPPAIDFP AEVSDPKYDE SDVPAELQVL KEPLQQPTFP 

        70         80         90        100        110        120 
FLVANQLLLV SLLEHLSHVH EPNPLHSKQV FKLLCQTFIK MGLLSSFTCS DEFSSLRLHH 

       130        140        150        160        170        180 
NRAITHLMRS AKERVRQDPC QDNSYMQKIR SREIAFEAQT SRYLNEFEEL AILGKGGYGR 

       190        200        210        220        230        240 
VYKVRNKLDG QHYAIKKILI KSATKTDCMK VLREVKVLAG LQHPNIVGYH TAWIEHVHVV 

       250        260        270        280        290        300 
QPQDRVPIQL PSLEVLSEQE GDRDQGGVKD NESSSSIVFA ELTPEKEKPF GESEVKNENN 

       310        320        330        340        350        360 
NLVSYTANLV VRNSSESESS IELQEDGLTD LSVRPVVRHQ LPLGHSSELE GNFTSTDESS 

       370        380        390        400        410        420 
EGNLNLLGQT EVRYHLMLHI QMQLCELSLW DWITERNKRS REYVDEAACP YVMASVATKI 

       430        440        450        460        470        480 
FQELVEGVFY IHNMGIVHRD LKPRNIFLHG PDQQVKIGDF GLACADIIQN ADWTNRNGKG 

       490        500        510        520        530        540 
TRTHTSRVGT CLYASPEQLE GSQYDAKSDM YSLGVILLEL FQPFGTEMER ATVLTGVRTG 

       550        560        570        580        590        600 
RIPESLSKRC PVQAKYIQLL TGRNVSQRPS ALQLLQSELF QTTGNVNLTL QMKIIEQEKE 

       610 
IEELKKQLSL LSQDRGLKR 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the hemin-sensitive eukaryotic initiation factor 2alpha kinase from mouse nonerythroid cells."
Berlanga J.J., Herrero S., de Haro C.
J. Biol. Chem. 273:32340-32346(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-196, AUTOPHOSPHORYLATION.
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency."
Han A.-P., Yu C., Lu L., Fujiwara Y., Browne C., Chin G., Fleming M., Leboulch P., Orkin S.H., Chen J.-J.
EMBO J. 20:6909-6918(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
Tissue: Erythroleukemia.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreatic islet.
[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].
Strain: C57BL/6J and FVB/N.
Tissue: Eye and Salivary gland.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-211 AND 445-619.
Strain: C57BL/6J.
Tissue: Head, Olfactory bulb and Retina.
[6]"Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase."
Bauer B.N., Rafie-Kolpin M., Lu L., Han A., Chen J.-J.
Biochemistry 40:11543-11551(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, HEME-BINDING.
[7]"Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses."
Lu L., Han A.P., Chen J.J.
Mol. Cell. Biol. 21:7971-7980(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION BY HEME DEFICIENCY; HEAT SHOCK; OSMOTIC STRESS AND OXIDATIVE STRESS, TISSUE SPECIFICITY.
[8]"Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI."
Rafie-Kolpin M., Han A.P., Chen J.J.
Biochemistry 42:6536-6544(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT THR-483; THR-485 AND THR-490, ENZYME REGULATION, MUTAGENESIS OF LYS-196; THR-483; THR-485 AND THR-490.
[9]"Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: optical absorption, electron spin resonance, and resonance raman spectral studies."
Igarashi J., Sato A., Kitagawa T., Yoshimura T., Yamauchi S., Sagami I., Shimizu T.
J. Biol. Chem. 279:15752-15762(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: HEME-BINDING, ENZYME REGULATION.
[10]"Characterization of heme-regulated eIF2alpha kinase: roles of the N-terminal domain in the oligomeric state, heme binding, catalysis, and inhibition."
Miksanova M., Igarashi J., Minami M., Sagami I., Yamauchi S., Kurokawa H., Shimizu T.
Biochemistry 45:9894-9905(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, OLIGOMERIZATION, HEME-BINDING, INDUCTION.
[11]"The function of heme-regulated eIF2alpha kinase in murine iron homeostasis and macrophage maturation."
Liu S., Suragani R.N., Wang F., Han A., Zhao W., Andrews N.C., Chen J.J.
J. Clin. Invest. 117:3296-3305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[12]"Hepatic heme-regulated inhibitor (HRI) eukaryotic initiation factor 2alpha kinase: a protagonist of heme-mediated translational control of CYP2B enzymes and a modulator of basal endoplasmic reticulum stress tone."
Acharya P., Chen J.J., Correia M.A.
Mol. Pharmacol. 77:575-592(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, ENZYME REGULATION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF028808 mRNA. Translation: AAC79201.1.
AY033898 mRNA. Translation: AAK55766.1.
AK173160 mRNA. Translation: BAD32438.1. Different initiation.
BC028923 mRNA. Translation: AAH28923.1.
BC111035 mRNA. Translation: AAI11036.1.
AK014775 mRNA. Translation: BAB29545.1.
AK020887 mRNA. Translation: BAB32242.1.
AK032508 mRNA. Translation: BAC27901.1.
RefSeqNP_038585.2. NM_013557.2.
UniGeneMm.389709.
Mm.431968.

3D structure databases

ProteinModelPortalQ9Z2R9.
SMRQ9Z2R9. Positions 162-235, 378-619.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200421. 1 interaction.
IntActQ9Z2R9. 2 interactions.
MINTMINT-1746990.
STRING10090.ENSMUSP00000098056.

Chemistry

ChEMBLCHEMBL1938213.

PTM databases

PhosphoSiteQ9Z2R9.

Proteomic databases

PRIDEQ9Z2R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100487; ENSMUSP00000098056; ENSMUSG00000029613.
GeneID15467.
KEGGmmu:15467.
UCSCuc029vqe.1. mouse.

Organism-specific databases

CTD27102.
MGIMGI:1353448. Eif2ak1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000062984.
HOVERGENHBG051429.
InParanoidQ69ZK8.
KOK16194.
OMANADWTNR.
OrthoDBEOG70GMF6.
PhylomeDBQ9Z2R9.
TreeFamTF329383.

Gene expression databases

ArrayExpressQ9Z2R9.
BgeeQ9Z2R9.
GenevestigatorQ9Z2R9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF2AK1. mouse.
NextBio288300.
PROQ9Z2R9.
SOURCESearch...

Entry information

Entry nameE2AK1_MOUSE
AccessionPrimary (citable) accession number: Q9Z2R9
Secondary accession number(s): Q2TA96 expand/collapse secondary AC list , Q69ZK8, Q8C024, Q8K123, Q9CTP5, Q9D601
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 5, 2011
Last modified: June 11, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot